|
Name |
Accession |
Description |
Interval |
E-value |
| ALDH_F3AB |
cd07132 |
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, ... |
5-446 |
0e+00 |
|
Aldehyde dehydrogenase family 3 members A1, A2, and B1 and related proteins; NAD(P)+-dependent, aldehyde dehydrogenase, family 3 members A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and similar sequences are included in this CD. Human ALDH3A1 is a homodimer with a critical role in cellular defense against oxidative stress; it catalyzes the oxidation of various cellular membrane lipid-derived aldehydes. Corneal crystalline ALDH3A1 protects the cornea and underlying lens against UV-induced oxidative stress. Human ALDH3A2, a microsomal homodimer, catalyzes the oxidation of long-chain aliphatic aldehydes to fatty acids. Human ALDH3B1 is highly expressed in the kidney and liver and catalyzes the oxidation of various medium- and long-chain saturated and unsaturated aliphatic aldehydes.
Pssm-ID: 143450 [Multi-domain] Cd Length: 443 Bit Score: 849.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 5 KEVAARLREAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESIISEVLFTKNEIVCAINNLTEWMKP 84
Cdd:cd07132 1 AEAVRRAREAFSSGKTRPLEFRIQQLEALLRMLEENEDEIVEALAKDLRKPKFEAVLSEILLVKNEIKYAISNLPEWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 85 EYVEKTLVTKLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKYLDKDCFA 164
Cdd:cd07132 81 EPVKKNLATLLDDVYIYKEPLGVVLIIGAWNYPLQLTLVPLVGAIAAGNCVVIKPSEVSPATAKLLAELIPKYLDKECYP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 165 VVCGGVKETTELLEEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTC 244
Cdd:cd07132 161 VVLGGVEETTELLKQRFDYIFYTGSTSVGKIVMQAAAKHLTPVTLELGGKSPCYVDKSCDIDVAARRIAWGKFINAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 245 IAPDYVLCTKAVREELVPALINCLEEFYGKNPQESEDLGRIINEKHFNRLKALLSSGKVAVGGQTDEKDKYIAPTVLVDV 324
Cdd:cd07132 241 IAPDYVLCTPEVQEKFVEALKKTLKEFYGEDPKESPDYGRIINDRHFQRLKKLLSGGKVAIGGQTDEKERYIAPTVLTDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 325 KETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCIMQMTLFSLPFGG 404
Cdd:cd07132 321 KPSDPVMQEEIFGPILPIVTVNNLDEAIEFINSREKPLALYVFSNNKKVINKILSNTSSGGVCVNDTIMHYTLDSLPFGG 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2119029253 405 VGDSGMGMYHGRFSFDTFSHKRACMLRSAGMEKISALRYPPY 446
Cdd:cd07132 401 VGNSGMGAYHGKYSFDTFSHKRSCLVKSLNMEKLNSLRYPPY 442
|
|
| ALDH_F3-13-14_CALDH-like |
cd07087 |
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other ... |
5-429 |
0e+00 |
|
ALDH subfamily: Coniferyl aldehyde dehydrogenase, ALDH families 3, 13, and 14, and other related proteins; ALDH subfamily which includes NAD(P)+-dependent, aldehyde dehydrogenase, family 3 member A1 and B1 (ALDH3A1, ALDH3B1, EC=1.2.1.5) and fatty aldehyde dehydrogenase, family 3 member A2 (ALDH3A2, EC=1.2.1.3), and also plant ALDH family members ALDH3F1, ALDH3H1, and ALDH3I1, fungal ALDH14 (YMR110C) and the protozoan family 13 member (ALDH13), as well as coniferyl aldehyde dehydrogenases (CALDH, EC=1.2.1.68), and other similar sequences, such as the Pseudomonas putida benzaldehyde dehydrogenase I that is involved in the metabolism of mandelate.
Pssm-ID: 143406 [Multi-domain] Cd Length: 426 Bit Score: 716.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 5 KEVAARLREAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESIISEVLFTKNEIVCAINNLTEWMKP 84
Cdd:cd07087 1 AELVARLRETFLTGKTRSLEWRKAQLKALKRMLTENEEEIAAALYADLGKPPAEAYLTEIAVVLGEIDHALKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 85 EYVEKTLVTKLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKYLDKDCFA 164
Cdd:cd07087 81 RRVSVPLLLQPAKAYVIPEPLGVVLIIGPWNYPLQLALAPLIGAIAAGNTVVLKPSELAPATSALLAKLIPKYFDPEAVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 165 VVCGGVKETTELLEEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTC 244
Cdd:cd07087 161 VVEGGVEVATALLAEPFDHIFFTGSPAVGKIVMEAAAKHLTPVTLELGGKSPCIVDKDANLEVAARRIAWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 245 IAPDYVLCTKAVREELVPALINCLEEFYGKNPQESEDLGRIINEKHFNRLKALLSSGKVAVGGQTDEKDKYIAPTVLVDV 324
Cdd:cd07087 241 IAPDYVLVHESIKDELIEELKKAIKEFYGEDPKESPDYGRIINERHFDRLASLLDDGKVVIGGQVDKEERYIAPTILDDV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 325 KETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCIMQMTLFSLPFGG 404
Cdd:cd07087 321 SPDSPLMQEEIFGPILPILTYDDLDEAIEFINSRPKPLALYLFSEDKAVQERVLAETSSGGVCVNDVLLHAAIPNLPFGG 400
|
410 420
....*....|....*....|....*
gi 2119029253 405 VGDSGMGMYHGRFSFDTFSHKRACM 429
Cdd:cd07087 401 VGNSGMGAYHGKAGFDTFSHLKSVL 425
|
|
| PTZ00381 |
PTZ00381 |
aldehyde dehydrogenase family protein; Provisional |
7-452 |
0e+00 |
|
aldehyde dehydrogenase family protein; Provisional
Pssm-ID: 240392 Cd Length: 493 Bit Score: 665.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 7 VAARLREAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESIISEVLFTKNEIVCAINNLTEWMKPEY 86
Cdd:PTZ00381 12 IVKKLKESFLTGKTRPLEFRKQQLRNLLRMLEENKQEFSEAVHKDLGRHPFETKMTEVLLTVAEIEHLLKHLDEYLKPEK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 87 VEKTLVTKLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKYLDKDCFAVV 166
Cdd:PTZ00381 92 VDTVGVFGPGKSYIIPEPLGVVLVIGAWNYPLNLTLIPLAGAIAAGNTVVLKPSELSPHTSKLMAKLLTKYLDPSYVRVI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 167 CGGVKETTELLEEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIA 246
Cdd:PTZ00381 172 EGGVEVTTELLKEPFDHIFFTGSPRVGKLVMQAAAENLTPCTLELGGKSPVIVDKSCNLKVAARRIAWGKFLNAGQTCVA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 247 PDYVLCTKAVREELVPALINCLEEFYGKNPQESEDLGRIINEKHFNRLKALL--SSGKVAVGGQTDEKDKYIAPTVLVDV 324
Cdd:PTZ00381 252 PDYVLVHRSIKDKFIEALKEAIKEFFGEDPKKSEDYSRIVNEFHTKRLAELIkdHGGKVVYGGEVDIENKYVAPTIIVNP 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 325 KETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCIMQMTLFSLPFGG 404
Cdd:PTZ00381 332 DLDSPLMQEEIFGPILPILTYENIDEVLEFINSRPKPLALYYFGEDKRHKELVLENTSSGAVVINDCVFHLLNPNLPFGG 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 2119029253 405 VGDSGMGMYHGRFSFDTFSHKRACMLRSAGMEKISALRYPPYGSHNLS 452
Cdd:PTZ00381 412 VGNSGMGAYHGKYGFDTFSHPKPVLNKSTGNSFDLSLRYPPYTSFKSW 459
|
|
| ALDH_YwdH-P39616 |
cd07136 |
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH ... |
5-446 |
0e+00 |
|
Bacillus subtilis aldehyde dehydrogenase ywdH-like; Uncharacterized Bacillus subtilis ywdH aldehyde dehydrogenase (locus P39616) most closely related to the ALDHs and fatty ALDHs of families 3 and 14, and similar sequences, are included in this CD.
Pssm-ID: 143454 [Multi-domain] Cd Length: 449 Bit Score: 652.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 5 KEVAARLREAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESIISEVLFTKNEIVCAINNLTEWMKP 84
Cdd:cd07136 1 ESLVEKQRAFFKTGATKDVEFRIEQLKKLKQAIKKYENEILEALKKDLGKSEFEAYMTEIGFVLSEINYAIKHLKKWMKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 85 EYVEKTLVTKLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKYLDKDCFA 164
Cdd:cd07136 81 KRVKTPLLNFPSKSYIYYEPYGVVLIIAPWNYPFQLALAPLIGAIAAGNTAVLKPSELTPNTSKVIAKIIEETFDEEYVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 165 VVCGGVKETTELLEEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTC 244
Cdd:cd07136 161 VVEGGVEENQELLDQKFDYIFFTGSVRVGKIVMEAAAKHLTPVTLELGGKSPCIVDEDANLKLAAKRIVWGKFLNAGQTC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 245 IAPDYVLCTKAVREELVPALINCLEEFYGKNPQESEDLGRIINEKHFNRLKALLSSGKVAVGGQTDEKDKYIAPTVLVDV 324
Cdd:cd07136 241 VAPDYVLVHESVKEKFIKELKEEIKKFYGEDPLESPDYGRIINEKHFDRLAGLLDNGKIVFGGNTDRETLYIEPTILDNV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 325 KETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCIMQMTLFSLPFGG 404
Cdd:cd07136 321 TWDDPVMQEEIFGPILPVLTYDTLDEAIEIIKSRPKPLALYLFSEDKKVEKKVLENLSFGGGCINDTIMHLANPYLPFGG 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2119029253 405 VGDSGMGMYHGRFSFDTFSHKRACMLRSAGMEkiSALRYPPY 446
Cdd:cd07136 401 VGNSGMGSYHGKYSFDTFSHKKSILKKSTWFD--LPLRYPPY 440
|
|
| ALDH_F14-YMR110C |
cd07135 |
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde ... |
9-429 |
0e+00 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase family 14 and related proteins; Aldehyde dehydrogenase family 14 (ALDH14), isolated mainly from the mitochondrial outer membrane of Saccharomyces cerevisiae (YMR110C) and most closely related to the plant and animal ALDHs and fatty ALDHs family 3 members, and similar fungal sequences, are present in this CD.
Pssm-ID: 143453 [Multi-domain] Cd Length: 436 Bit Score: 616.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 9 ARLREAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESIISEVLFTKNEIVCAINNLTEWMKPEYVE 88
Cdd:cd07135 12 SRLRATFRSGKTKDLEYRLWQLKQLYWAVKDNEEAIVEALKKDLGRPPFETLLTEVSGVKNDILHMLKNLKKWAKDEKVK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 89 KTLVT-KLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKYLDKDCFAVVC 167
Cdd:cd07135 92 DGPLAfMFGKPRIRKEPLGVVLIIGPWNYPVLLALSPLVGAIAAGCTVVLKPSELTPHTAALLAELVPKYLDPDAFQVVQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 168 GGVKETTELLEEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAP 247
Cdd:cd07135 172 GGVPETTALLEQKFDKIFYTGSGRVGRIIAEAAAKHLTPVTLELGGKSPVIVTKNADLELAAKRILWGKFGNAGQICVAP 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 248 DYVLCTKAVREELVPALINCLEEFYGKNPQESEDLGRIINEKHFNRLKALLSS--GKVAVGGQTDEKDKYIAPTVLVDVK 325
Cdd:cd07135 252 DYVLVDPSVYDEFVEELKKVLDEFYPGGANASPDYTRIVNPRHFNRLKSLLDTtkGKVVIGGEMDEATRFIPPTIVSDVS 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 326 ETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCIMQMTLFSLPFGGV 405
Cdd:cd07135 332 WDDSLMSEELFGPVLPIIKVDDLDEAIKVINSRDTPLALYIFTDDKSEIDHILTRTRSGGVVINDTLIHVGVDNAPFGGV 411
|
410 420
....*....|....*....|....
gi 2119029253 406 GDSGMGMYHGRFSFDTFSHKRACM 429
Cdd:cd07135 412 GDSGYGAYHGKYGFDTFTHERTVV 435
|
|
| ALDH_F3FHI |
cd07137 |
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde ... |
6-429 |
0e+00 |
|
Plant aldehyde dehydrogenase family 3 members F1, H1, and I1 and related proteins; Aldehyde dehydrogenase family members 3F1, 3H1, and 3I1 (ALDH3F1, ALDH3H1, and ALDH3I1), and similar plant sequences, are in this CD. In Arabidopsis thaliana, stress-regulated expression of ALDH3I1 was observed in leaves and osmotic stress expression of ALDH3H1 was observed in root tissue, whereas, ALDH3F1 expression was not stress responsive. Functional analysis of ALDH3I1 suggest it may be involved in a detoxification pathway in plants that limits aldehyde accumulation and oxidative stress.
Pssm-ID: 143455 [Multi-domain] Cd Length: 432 Bit Score: 521.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 6 EVAARLREAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESIISEVLFTKNEIVCAINNLTEWMKPE 85
Cdd:cd07137 3 RLVRELRETFRSGRTRSAEWRKSQLKGLLRLVDENEDDIFAALRQDLGKPSAESFRDEVSVLVSSCKLAIKELKKWMAPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 86 YVEKTLVTKLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKYLDKDCFAV 165
Cdd:cd07137 83 KVKTPLTTFPAKAEIVSEPLGVVLVISAWNFPFLLSLEPVIGAIAAGNAVVLKPSELAPATSALLAKLIPEYLDTKAIKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 166 VCGGVKETTELLEEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARF-LNMGQTC 244
Cdd:cd07137 163 IEGGVPETTALLEQKWDKIFFTGSPRVGRIIMAAAAKHLTPVTLELGGKCPVIVDSTVDLKVAVRRIAGGKWgCNNGQAC 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 245 IAPDYVLCTKAVREELVPALINCLEEFYGKNPQESEDLGRIINEKHFNRLKALLS----SGKVAVGGQTDEKDKYIAPTV 320
Cdd:cd07137 243 IAPDYVLVEESFAPTLIDALKNTLEKFFGENPKESKDLSRIVNSHHFQRLSRLLDdpsvADKIVHGGERDEKNLYIEPTI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 321 LVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCIMQMTLFSL 400
Cdd:cd07137 323 LLDPPLDSSIMTEEIFGPLLPIITVKKIEESIEIINSRPKPLAAYVFTKNKELKRRIVAETSSGGVTFNDTVVQYAIDTL 402
|
410 420
....*....|....*....|....*....
gi 2119029253 401 PFGGVGDSGMGMYHGRFSFDTFSHKRACM 429
Cdd:cd07137 403 PFGGVGESGFGAYHGKFSFDAFSHKKAVL 431
|
|
| ALDH_AlkH-like |
cd07134 |
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name ... |
6-429 |
1.19e-180 |
|
Pseudomonas putida Aldehyde dehydrogenase AlkH-like; Aldehyde dehydrogenase AlkH (locus name P12693, EC=1.2.1.3) of the alkBFGHJKL operon that allows Pseudomonas putida to metabolize alkanes and the aldehyde dehydrogenase AldX of Bacillus subtilis (locus P46329, EC=1.2.1.3), and similar sequences, are present in this CD.
Pssm-ID: 143452 [Multi-domain] Cd Length: 433 Bit Score: 512.16 E-value: 1.19e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 6 EVAARLREAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESIISEVLFTKNEIVCAINNLTEWMKPE 85
Cdd:cd07134 2 RVFAAQQAHALALRASTAAERIAKLKRLKKAILARREEIIAALAADFRKPAAEVDLTEILPVLSEINHAIKHLKKWMKPK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 86 YVEKTLVTKLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKYLDKDCFAV 165
Cdd:cd07134 82 RVRTPLLLFGTKSKIRYEPKGVCLIISPWNYPFNLAFGPLVSAIAAGNTAILKPSELTPHTSAVIAKIIREAFDEDEVAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 166 VCGGVKETTELLEEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCI 245
Cdd:cd07134 162 FEGDAEVAQALLELPFDHIFFTGSPAVGKIVMAAAAKHLASVTLELGGKSPTIVDETADLKKAAKKIAWGKFLNAGQTCI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 246 APDYVLCTKAVREELVPALINCLEEFYGKNP--QESEDLGRIINEKHFNRLKALLS-----SGKVAVGGQTDEKDKYIAP 318
Cdd:cd07134 242 APDYVFVHESVKDAFVEHLKAEIEKFYGKDAarKASPDLARIVNDRHFDRLKGLLDdavakGAKVEFGGQFDAAQRYIAP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 319 TVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCIMQMTLF 398
Cdd:cd07134 322 TVLTNVTPDMKIMQEEIFGPVLPIITYEDLDEVIEYINAKPKPLALYVFSKDKANVNKVLARTSSGGVVVNDVVLHFLNP 401
|
410 420 430
....*....|....*....|....*....|.
gi 2119029253 399 SLPFGGVGDSGMGMYHGRFSFDTFSHKRACM 429
Cdd:cd07134 402 NLPFGGVNNSGIGSYHGVYGFKAFSHERAVL 432
|
|
| ALDH_CALDH_CalB |
cd07133 |
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) ... |
8-427 |
3.17e-162 |
|
Coniferyl aldehyde dehydrogenase-like; Coniferyl aldehyde dehydrogenase (CALDH, EC=1.2.1.68) of Pseudomonas sp. strain HR199 (CalB) which catalyzes the NAD+-dependent oxidation of coniferyl aldehyde to ferulic acid, and similar sequences, are present in this CD.
Pssm-ID: 143451 [Multi-domain] Cd Length: 434 Bit Score: 465.42 E-value: 3.17e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 8 AARLREAFNSGKTRTAefRLKQLKAMLnlmKENEGALLEALKKDL-RKPNFESIISEVLFTKNEIVCAINNLTEWMKPEY 86
Cdd:cd07133 9 AAFLANPPPSLEERRD--RLDRLKALL---LDNQDALAEAISADFgHRSRHETLLAEILPSIAGIKHARKHLKKWMKPSR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 87 VEKTLVTKLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKYLDKDCFAVV 166
Cdd:cd07133 84 RHVGLLFLPAKAEVEYQPLGVVGIIVPWNYPLYLALGPLIAALAAGNRVMIKPSEFTPRTSALLAELLAEYFDEDEVAVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 167 CGGV---KETTELleeKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQT 243
Cdd:cd07133 164 TGGAdvaAAFSSL---PFDHLLFTGSTAVGRHVMRAAAENLTPVTLELGGKSPAIIAPDADLAKAAERIAFGKLLNAGQT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 244 CIAPDYVLCTKAVREELVPALINCLEEFYGkNPQESEDLGRIINEKHFNRLKALLSSGK--------VAVGGQTDEKDKY 315
Cdd:cd07133 241 CVAPDYVLVPEDKLEEFVAAAKAAVAKMYP-TLADNPDYTSIINERHYARLQGLLEDARakgarvieLNPAGEDFAATRK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 316 IAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCIMQM 395
Cdd:cd07133 320 LPPTLVLNVTDDMRVMQEEIFGPILPILTYDSLDEAIDYINARPRPLALYYFGEDKAEQDRVLRRTHSGGVTINDTLLHV 399
|
410 420 430
....*....|....*....|....*....|..
gi 2119029253 396 TLFSLPFGGVGDSGMGMYHGRFSFDTFSHKRA 427
Cdd:cd07133 400 AQDDLPFGGVGASGMGAYHGKEGFLTFSHAKP 431
|
|
| PLN02203 |
PLN02203 |
aldehyde dehydrogenase |
1-455 |
6.14e-159 |
|
aldehyde dehydrogenase
Pssm-ID: 165847 [Multi-domain] Cd Length: 484 Bit Score: 458.81 E-value: 6.14e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 1 MSSTKEVAARLREAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESIISEVLFTKNEIVCAINNLTE 80
Cdd:PLN02203 5 GETLEGSVAELRETYESGRTRSLEWRKSQLKGLLRLLKDNEEAIFKALHQDLGKHRVEAYRDEVGVLTKSANLALSNLKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 81 WMKPEYVEKTLVTKLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKYLDK 160
Cdd:PLN02203 85 WMAPKKAKLPLVAFPATAEVVPEPLGVVLIFSSWNFPIGLSLEPLIGAIAAGNAVVLKPSELAPATSAFLAANIPKYLDS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 161 DCFAVVCGGVKETTELLEEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVD---KSCDINNTAHRIAWARF 237
Cdd:PLN02203 165 KAVKVIEGGPAVGEQLLQHKWDKIFFTGSPRVGRIIMTAAAKHLTPVALELGGKCPCIVDslsSSRDTKVAVNRIVGGKW 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 238 LN-MGQTCIAPDYVLctkaVREELVPALI----NCLEEFYGKNPQESEDLGRIINEKHFNRLKALLSSGKVAV----GGQ 308
Cdd:PLN02203 245 GScAGQACIAIDYVL----VEERFAPILIellkSTIKKFFGENPRESKSMARILNKKHFQRLSNLLKDPRVAAsivhGGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 309 TDEKDKYIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCS 388
Cdd:PLN02203 321 IDEKKLFIEPTILLNPPLDSDIMTEEIFGPLLPIITVKKIEDSIAFINSKPKPLAIYAFTNNEKLKRRILSETSSGSVTF 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119029253 389 NDCIMQMTLFSLPFGGVGDSGMGMYHGRFSFDTFSHKRACMLRSAGMEkiSALRYPPYGSHNLSMIE 455
Cdd:PLN02203 401 NDAIIQYACDSLPFGGVGESGFGRYHGKYSFDTFSHEKAVLRRSLLTE--FEFRYPPWNDFKLGFLR 465
|
|
| PLN02174 |
PLN02174 |
aldehyde dehydrogenase family 3 member H1 |
11-455 |
1.46e-135 |
|
aldehyde dehydrogenase family 3 member H1
Pssm-ID: 177831 Cd Length: 484 Bit Score: 399.42 E-value: 1.46e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 11 LREAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESIISEVLFTKNEIVCAINNLTEWMKPEYVEKT 90
Cdd:PLN02174 19 LRRSFDDGVTRGYEWRVTQLKKLMIICDNHEPEIVAALRDDLGKPELESSVYEVSLLRNSIKLALKQLKNWMAPEKAKTS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 91 LVTKLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKYLDKDCFAVVCGGV 170
Cdd:PLN02174 99 LTTFPASAEIVSEPLGVVLVISAWNYPFLLSIDPVIGAISAGNAVVLKPSELAPASSALLAKLLEQYLDSSAVRVVEGAV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 171 KETTELLEEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARF-LNMGQTCIAPDY 249
Cdd:PLN02174 179 TETTALLEQKWDKIFYTGSSKIGRVIMAAAAKHLTPVVLELGGKSPVVVDSDTDLKVTVRRIIAGKWgCNNGQACISPDY 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 250 VLCTKAVREELVPALINCLEEFYGKNPQESEDLGRIINEKHFNRLKALLS----SGKVAVGGQTDEKDKYIAPTVLVDVK 325
Cdd:PLN02174 259 ILTTKEYAPKVIDAMKKELETFYGKNPMESKDMSRIVNSTHFDRLSKLLDekevSDKIVYGGEKDRENLKIAPTILLDVP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 326 ETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCIMQMTLFSLPFGGV 405
Cdd:PLN02174 339 LDSLIMSEEIFGPLLPILTLNNLEESFDVIRSRPKPLAAYLFTHNKKLKERFAATVSAGGIVVNDIAVHLALHTLPFGGV 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2119029253 406 GDSGMGMYHGRFSFDTFSHKRACMLRSAGMEkiSALRYPPYGSHNLSMIE 455
Cdd:PLN02174 419 GESGMGAYHGKFSFDAFSHKKAVLYRSLFGD--SAVRYPPYSRGKLRLLK 466
|
|
| ALDH |
cd07078 |
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of ... |
6-430 |
2.86e-132 |
|
NAD(P)+ dependent aldehyde dehydrogenase family; The aldehyde dehydrogenase family (ALDH) of NAD(P)+ dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or as osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-like) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group.
Pssm-ID: 143397 [Multi-domain] Cd Length: 432 Bit Score: 388.87 E-value: 2.86e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 6 EVAARLREAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESIIsEVLFTKNEIVCAINNLTEWMKPE 85
Cdd:cd07078 2 AAVAAARAAFKAWAALPPAERAAILRKLADLLEERREELAALETLETGKPIEEALG-EVARAADTFRYYAGLARRLHGEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 86 YVEKTLVTKLdtcFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFA 164
Cdd:cd07078 81 IPSPDPGELA---IVRREPLGVVGAITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALLLAELLAEAgLPPGVLN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 165 VVCGGVKETTELL--EEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQ 242
Cdd:cd07078 158 VVTGDGDEVGAALasHPRVDKISFTGSTAVGKAIMRAAAENLKRVTLELGGKSPLIVFDDADLDAAVKGAVFGAFGNAGQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 243 TCIAPDYVLCTKAVREELVPALINCLEEFYGKNPQESE-DLGRIINEKHFNRLKALLSS-----GKVAVGGQTDEKDK-- 314
Cdd:cd07078 238 VCTAASRLLVHESIYDEFVERLVERVKALKVGNPLDPDtDMGPLISAAQLDRVLAYIEDakaegAKLLCGGKRLEGGKgy 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 315 YIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCIMQ 394
Cdd:cd07078 318 FVPPTVLTDVDPDMPIAQEEIFGPVLPVIPFKDEEEAIELANDTEYGLAAGVFTRDLERALRVAERLEAGTVWINDYSVG 397
|
410 420 430
....*....|....*....|....*....|....*.
gi 2119029253 395 MTlFSLPFGGVGDSGMGMYHGRFSFDTFSHKRACML 430
Cdd:cd07078 398 AE-PSAPFGGVKQSGIGREGGPYGLEEYTEPKTVTI 432
|
|
| ALDH-SF |
cd06534 |
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily ... |
9-430 |
1.67e-104 |
|
NAD(P)+-dependent aldehyde dehydrogenase superfamily; The aldehyde dehydrogenase superfamily (ALDH-SF) of NAD(P)+-dependent enzymes, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. Besides aldehyde detoxification, many ALDH isozymes possess multiple additional catalytic and non-catalytic functions such as participating in metabolic pathways, or as binding proteins, or osmoregulants, to mention a few. The enzyme has three domains, a NAD(P)+ cofactor-binding domain, a catalytic domain, and a bridging domain; and the active enzyme is generally either homodimeric or homotetrameric. The catalytic mechanism is proposed to involve cofactor binding, resulting in a conformational change and activation of an invariant catalytic cysteine nucleophile. The cysteine and aldehyde substrate form an oxyanion thiohemiacetal intermediate resulting in hydride transfer to the cofactor and formation of a thioacylenzyme intermediate. Hydrolysis of the thioacylenzyme and release of the carboxylic acid product occurs, and in most cases, the reduced cofactor dissociates from the enzyme. The evolutionary phylogenetic tree of ALDHs appears to have an initial bifurcation between what has been characterized as the classical aldehyde dehydrogenases, the ALDH family (ALDH) and extended family members or aldehyde dehydrogenase-like (ALDH-L) proteins. The ALDH proteins are represented by enzymes which share a number of highly conserved residues necessary for catalysis and cofactor binding and they include such proteins as retinal dehydrogenase, 10-formyltetrahydrofolate dehydrogenase, non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase, delta(1)-pyrroline-5-carboxylate dehydrogenases, alpha-ketoglutaric semialdehyde dehydrogenase, alpha-aminoadipic semialdehyde dehydrogenase, coniferyl aldehyde dehydrogenase and succinate-semialdehyde dehydrogenase. Included in this larger group are all human, Arabidopsis, Tortula, fungal, protozoan, and Drosophila ALDHs identified in families ALDH1 through ALDH22 with the exception of families ALDH18, ALDH19, and ALDH20 which are present in the ALDH-like group. The ALDH-like group is represented by such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143395 [Multi-domain] Cd Length: 367 Bit Score: 315.71 E-value: 1.67e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 9 ARLREAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPnfesiISEVLFtknEIVCAINNL---TEWMKPE 85
Cdd:cd06534 1 AAARAAFKAWAALPPAERAAILRKIADLLEERREELAALETLETGKP-----IEEALG---EVARAIDTFryaAGLADKL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 86 YVEKTLVTKLDT-CFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCF 163
Cdd:cd06534 73 GGPELPSPDPGGeAYVRREPLGVVGVITPWNFPLLLAAWKLAPALAAGNTVVLKPSELTPLTALALAELLQEAgLPPGVV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 164 AVVCGGVKETTELL--EEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMG 241
Cdd:cd06534 153 NVVPGGGDEVGAALlsHPRVDKISFTGSTAVGKAIMKAAAENLKPVTLELGGKSPVIVDEDADLDAAVEGAVFGAFFNAG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 242 QTCIAPDYVLCTKAVREELVpalincleefygknpqesedlgriinekhfNRLKallssgkvavggqtdekdkyiapTVL 321
Cdd:cd06534 233 QICTAASRLLVHESIYDEFV------------------------------EKLV-----------------------TVL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 322 VDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCIMQMTLfSLP 401
Cdd:cd06534 260 VDVDPDMPIAQEEIFGPVLPVIRFKDEEEAIALANDTEYGLTAGVFTRDLNRALRVAERLRAGTVYINDSSIGVGP-EAP 338
|
410 420
....*....|....*....|....*....
gi 2119029253 402 FGGVGDSGMGMYHGRFSFDTFSHKRACML 430
Cdd:cd06534 339 FGGVKNSGIGREGGPYGLEEYTRTKTVVI 367
|
|
| AdhE |
COG1012 |
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and ... |
8-431 |
2.50e-104 |
|
Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase [Lipid transport and metabolism]; Acyl-CoA reductase or other NAD-dependent aldehyde dehydrogenase is part of the Pathway/BioSystem: Proline degradation
Pssm-ID: 440636 [Multi-domain] Cd Length: 479 Bit Score: 318.99 E-value: 2.50e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 8 AARlrEAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPnfesiISEvlfTKNEIVCAINNLT---EWMKP 84
Cdd:COG1012 51 AAR--AAFPAWAATPPAERAAILLRAADLLEERREELAALLTLETGKP-----LAE---ARGEVDRAADFLRyyaGEARR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 85 EYVEKT-LVTKLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDC 162
Cdd:COG1012 121 LYGETIpSDAPGTRAYVRREPLGVVGAITPWNFPLALAAWKLAPALAAGNTVVLKPAEQTPLSALLLAELLEEAgLPAGV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 163 FAVVCGGVKETTELLEE--KFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNM 240
Cdd:COG1012 201 LNVVTGDGSEVGAALVAhpDVDKISFTGSTAVGRRIAAAAAENLKRVTLELGGKNPAIVLDDADLDAAVEAAVRGAFGNA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 241 GQTCIAPDYVLCTKAVREELVPALINCLEEF-YGkNP-QESEDLGRIINEKHFNRLKALLSSGK-----VAVGGQTDEKD 313
Cdd:COG1012 281 GQRCTAASRLLVHESIYDEFVERLVAAAKALkVG-DPlDPGTDMGPLISEAQLERVLAYIEDAVaegaeLLTGGRRPDGE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 314 K--YIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDC 391
Cdd:COG1012 360 GgyFVEPTVLADVTPDMRIAREEIFGPVLSVIPFDDEEEAIALANDTEYGLAASVFTRDLARARRVARRLEAGMVWINDG 439
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2119029253 392 IMQMTLFsLPFGGVGDSGMGMYHGRFSFDTFSHKRACMLR 431
Cdd:COG1012 440 TTGAVPQ-APFGGVKQSGIGREGGREGLEEYTETKTVTIR 478
|
|
| Aldedh |
pfam00171 |
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. ... |
12-423 |
1.54e-93 |
|
Aldehyde dehydrogenase family; This family of dehydrogenases act on aldehyde substrates. Members use NADP as a cofactor. The family includes the following members: The prototypical members are the aldehyde dehydrogenases EC:1.2.1.3. Succinate-semialdehyde dehydrogenase EC:1.2.1.16. Lactaldehyde dehydrogenase EC:1.2.1.22. Benzaldehyde dehydrogenase EC:1.2.1.28. Methylmalonate-semialdehyde dehydrogenase EC:1.2.1.27. Glyceraldehyde-3-phosphate dehydrogenase EC:1.2.1.9. Delta-1-pyrroline-5-carboxylate dehydrogenase EC: 1.5.1.12. Acetaldehyde dehydrogenase EC:1.2.1.10. Glutamate-5-semialdehyde dehydrogenase EC:1.2.1.41. This family also includes omega crystallin, an eye lens protein from squid and octopus that has little aldehyde dehydrogenase activity.
Pssm-ID: 425500 [Multi-domain] Cd Length: 459 Bit Score: 290.59 E-value: 1.54e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 12 REAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPnfesiISEvlfTKNEIVCAINNLTEW------MKPE 85
Cdd:pfam00171 39 RAAFPAWRKTPAAERAAILRKAADLLEERKDELAELETLENGKP-----LAE---ARGEVDRAIDVLRYYaglarrLDGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 86 YVEktlVTKLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFA 164
Cdd:pfam00171 111 TLP---SDPGRLAYTRREPLGVVGAITPWNFPLLLPAWKIAPALAAGNTVVLKPSELTPLTALLLAELFEEAgLPAGVLN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 165 VVCGGVKETTELLEE--KFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQ 242
Cdd:pfam00171 188 VVTGSGAEVGEALVEhpDVRKVSFTGSTAVGRHIAEAAAQNLKRVTLELGGKNPLIVLEDADLDAAVEAAVFGAFGNAGQ 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 243 TCIAPDYVLCTKAVREELVPALINCLEEFYGKNPQESE-DLGRIINEKHFNRLKALLSSG-----KVAVGGQTDEKDKY- 315
Cdd:pfam00171 268 VCTATSRLLVHESIYDEFVEKLVEAAKKLKVGDPLDPDtDMGPLISKAQLERVLKYVEDAkeegaKLLTGGEAGLDNGYf 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 316 IAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDcimqM 395
Cdd:pfam00171 348 VEPTVLANVTPDMRIAQEEIFGPVLSVIRFKDEEEAIEIANDTEYGLAAGVFTSDLERALRVARRLEAGMVWIND----Y 423
|
410 420 430
....*....|....*....|....*....|.
gi 2119029253 396 TLF---SLPFGGVGDSGMGMYHGRFSFDTFS 423
Cdd:pfam00171 424 TTGdadGLPFGGFKQSGFGREGGPYGLEEYT 454
|
|
| ALDH_DDALDH |
cd07099 |
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4 ... |
6-427 |
4.10e-89 |
|
Methylomonas sp. 4,4'-diapolycopene-dialdehyde dehydrogenase-like; The 4,4'-diapolycopene-dialdehyde dehydrogenase (DDALDH) involved in C30 carotenoid synthesis in Methylomonas sp. strain 16a and other similar sequences are present in this CD. DDALDH converts 4,4'-diapolycopene-dialdehyde into 4,4'-diapolycopene-diacid.
Pssm-ID: 143417 [Multi-domain] Cd Length: 453 Bit Score: 279.11 E-value: 4.10e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 6 EVAARLREAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESIIsEVLFTKNEIVCAINNLTEWMKPE 85
Cdd:cd07099 22 AAVARARAAQRAWAALGVEGRAQRLLRWKRALADHADELAELLHAETGKPRADAGL-EVLLALEAIDWAARNAPRVLAPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 86 YVEKTLVTKLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFA 164
Cdd:cd07099 101 KVPTGLLMPNKKATVEYRPYGVVGVISPWNYPLLTPMGDIIPALAAGNAVVLKPSEVTPLVGELLAEAWAAAgPPQGVLQ 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 165 VVCGGVKETTELLEEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTC 244
Cdd:cd07099 181 VVTGDGATGAALIDAGVDKVAFTGSVATGRKVMAAAAERLIPVVLELGGKDPMIVLADADLERAAAAAVWGAMVNAGQTC 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 245 IAPDYVLCTKAVREELVPALINCLEEF-YGKNPQESEDLGRIINEKHFNRLK-----ALLSSGKVAVGG-QTDEKDKYIA 317
Cdd:cd07099 261 ISVERVYVHESVYDEFVARLVAKARALrPGADDIGDADIGPMTTARQLDIVRrhvddAVAKGAKALTGGaRSNGGGPFYE 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 318 PTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCIMQMTL 397
Cdd:cd07099 341 PTVLTDVPHDMDVMREETFGPVLPVMPVADEDEAIALANDSRYGLSASVFSRDLARAEAIARRLEAGAVSINDVLLTAGI 420
|
410 420 430
....*....|....*....|....*....|
gi 2119029253 398 FSLPFGGVGDSGMGMYHGRFSFDTFSHKRA 427
Cdd:cd07099 421 PALPFGGVKDSGGGRRHGAEGLREFCRPKA 450
|
|
| ALDH_F15-22 |
cd07098 |
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ... |
5-417 |
1.03e-68 |
|
Aldehyde dehydrogenase family 15A1 and 22A1-like; Aldehyde dehydrogenase family members ALDH15A1 (Saccharomyces cerevisiae YHR039C) and ALDH22A1 (Arabidopsis thaliana, EC=1.2.1.3), and similar sequences, are in this CD. Significant improvement of stress tolerance in tobacco plants was observed by overexpressing the ALDH22A1 gene from maize (Zea mays) and was accompanied by a reduction of malondialdehyde derived from cellular lipid peroxidation.
Pssm-ID: 143416 [Multi-domain] Cd Length: 465 Bit Score: 226.41 E-value: 1.03e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 5 KEVAARLREAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESIISEVLFTKNEIVCAINNLTEWMKP 84
Cdd:cd07098 21 DEAIAAARAAQREWAKTSFAERRKVLRSLLKYILENQEEICRVACRDTGKTMVDASLGEILVTCEKIRWTLKHGEKALRP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 85 EYVEKTLVTKLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKYL-----D 159
Cdd:cd07098 101 ESRPGGLLMFYKRARVEYEPLGVVGAIVSWNYPFHNLLGPIIAALFAGNAIVVKVSEQVAWSSGFFLSIIRECLaacghD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 160 KDCFAVVCGgVKETTELLEE--KFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARF 237
Cdd:cd07098 181 PDLVQLVTC-LPETAEALTShpVIDHITFIGSPPVGKKVMAAAAESLTPVVLELGGKDPAIVLDDADLDQIASIIMRGTF 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 238 LNMGQTCIAPDYVLCTKAVREELVPALINCLEEFYGKNP-QESEDLGRIINEKHFNRLKALL----SSG-KVAVGGQ--- 308
Cdd:cd07098 260 QSSGQNCIGIERVIVHEKIYDKLLEILTDRVQALRQGPPlDGDVDVGAMISPARFDRLEELVadavEKGaRLLAGGKryp 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 309 --TDEKDKYIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGF 386
Cdd:cd07098 340 hpEYPQGHYFPPTLLVDVTPDMKIAQEEVFGPVMVVMKASDDEEAVEIANSTEYGLGASVFGKDIKRARRIASQLETGMV 419
|
410 420 430
....*....|....*....|....*....|.
gi 2119029253 387 CSNDCIMQMTLFSLPFGGVGDSGmgmyHGRF 417
Cdd:cd07098 420 AINDFGVNYYVQQLPFGGVKGSG----FGRF 446
|
|
| ALDH_EDX86601 |
cd07102 |
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); ... |
5-430 |
1.99e-66 |
|
Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (EDX86601); Uncharacterized aldehyde dehydrogenase of Synechococcus sp. PCC 7335 (locus EDX86601) and other similar sequences, are present in this CD.
Pssm-ID: 143420 [Multi-domain] Cd Length: 452 Bit Score: 220.20 E-value: 1.99e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 5 KEVAARLREAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPnfesiIS----EVLFTKNEIVCAINNLTE 80
Cdd:cd07102 21 RAALERARAAQKGWRAVPLEERKAIVTRAVELLAANTDEIAEELTWQMGRP-----IAqaggEIRGMLERARYMISIAEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 81 WMKPEYV-EKTLVTKldtcFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-L 158
Cdd:cd07102 96 ALADIRVpEKDGFER----YIRREPLGVVLIIAPWNYPYLTAVNAVIPALLAGNAVILKHSPQTPLCGERFAAAFAEAgL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 159 DKDCFAVVCGGVKETTELLEEK-FDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARF 237
Cdd:cd07102 172 PEGVFQVLHLSHETSAALIADPrIDHVSFTGSVAGGRAIQRAAAGRFIKVGLELGGKDPAYVRPDADLDAAAESLVDGAF 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 238 LNMGQTCIAPDYVLCTKAVREELVPALINCLEEF-YGKNPQESEDLGRIINEKH--FNRLK---ALLSSGKVAVGGQT-- 309
Cdd:cd07102 252 FNSGQSCCSIERIYVHESIYDAFVEAFVAVVKGYkLGDPLDPSTTLGPVVSARAadFVRAQiadAIAKGARALIDGALfp 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 310 --DEKDKYIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFC 387
Cdd:cd07102 332 edKAGGAYLAPTVLTNVDHSMRVMREETFGPVVGIMKVKSDAEAIALMNDSEYGLTASVWTKDIARAEALGEQLETGTVF 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2119029253 388 SNDCImqmtlF---SLPFGGVGDSGMGMYHGRFSFDTFSHKRACML 430
Cdd:cd07102 412 MNRCD-----YldpALAWTGVKDSGRGVTLSRLGYDQLTRPKSYHL 452
|
|
| ALDH_ABALDH-YdcW |
cd07092 |
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD ... |
2-429 |
6.39e-64 |
|
Escherichia coli NAD+-dependent gamma-aminobutyraldehyde dehydrogenase YdcW-like; NAD+-dependent, tetrameric, gamma-aminobutyraldehyde dehydrogenase (ABALDH), YdcW of Escherichia coli K12, catalyzes the oxidation of gamma-aminobutyraldehyde to gamma-aminobutyric acid. ABALDH can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Pssm-ID: 143411 [Multi-domain] Cd Length: 450 Bit Score: 213.34 E-value: 6.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 2 SSTKEVAARL---REAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESIISEVLFTKNEI---VCAI 75
Cdd:cd07092 16 ASAADVDAAVaaaHAAFPSWRRTTPAERSKALLKLADAIEENAEELAALESRNTGKPLHLVRDDELPGAVDNFrffAGAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 76 NNLTEWMKPEYVEKTlvtkldTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLP 155
Cdd:cd07092 96 RTLEGPAAGEYLPGH------TSMIRREPIGVVAQIAPWNYPLMMAAWKIAPALAAGNTVVLKPSETTPLTTLLLAELAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 156 KYLDKDCFAVVCGGVKETTELL--EEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIA 233
Cdd:cd07092 170 EVLPPGVVNVVCGGGASAGDALvaHPRVRMVSLTGSVRTGKKVARAAADTLKRVHLELGGKAPVIVFDDADLDAAVAGIA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 234 WARFLNMGQTCIAPDYVLCTKAVREELVPALIN-CLEEFYGKNPQESEDLGRIINEKHFNRLKALLS----SGKVAVGG- 307
Cdd:cd07092 250 TAGYYNAGQDCTAACRVYVHESVYDEFVAALVEaVSAIRVGDPDDEDTEMGPLNSAAQRERVAGFVErapaHARVLTGGr 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 308 QTDEKDKYIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFC 387
Cdd:cd07092 330 RAEGPGYFYEPTVVAGVAQDDEIVQEEIFGPVVTVQPFDDEDEAIELANDVEYGLASSVWTRDVGRAMRLSARLDFGTVW 409
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2119029253 388 SNDCIMQMTlfSLPFGGVGDSGMGMYHGRFSFDTFSHKRACM 429
Cdd:cd07092 410 VNTHIPLAA--EMPHGGFKQSGYGKDLSIYALEDYTRIKHVM 449
|
|
| ALDH_F5_SSADH_GabD |
cd07103 |
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; ... |
13-411 |
1.56e-63 |
|
Mitochondrial succinate-semialdehyde dehydrogenase and ALDH family members 5A1 and 5F1-like; Succinate-semialdehyde dehydrogenase, mitochondrial (SSADH, GabD, EC=1.2.1.24) catalyzes the NAD+-dependent oxidation of succinate semialdehyde (SSA) to succinate. This group includes the human aldehyde dehydrogenase family 5 member A1 (ALDH5A1) which is a mitochondrial homotetramer that converts SSA to succinate in the last step of 4-aminobutyric acid (GABA) catabolism. This CD also includes the Arabidopsis SSADH gene product ALDH5F1. Mutations in this gene result in the accumulation of H2O2, suggesting a role in plant defense against the environmental stress of elevated reactive oxygen species.
Pssm-ID: 143421 [Multi-domain] Cd Length: 451 Bit Score: 212.29 E-value: 1.56e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 13 EAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPnfesiISEvlfTKNEIVCAINNLtEWmkpeYVE---- 88
Cdd:cd07103 30 AAFKTWRKTTARERAAILRRWADLIRERAEDLARLLTLEQGKP-----LAE---ARGEVDYAASFL-EW----FAEearr 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 89 ---KTLVTKLDTC--FIKKEPFGVALIIGPWNYPIQLV---LTPfigAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LD 159
Cdd:cd07103 97 iygRTIPSPAPGKriLVIKQPVGVVAAITPWNFPAAMItrkIAP---ALAAGCTVVLKPAEETPLSALALAELAEEAgLP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 160 KDCFAVVCGGVKETTELLEE-----KfdyIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAW 234
Cdd:cd07103 174 AGVLNVVTGSPAEIGEALCAsprvrK---ISFTGSTAVGKLLMAQAADTVKRVSLELGGNAPFIVFDDADLDKAVDGAIA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 235 ARFLNMGQTCIAPDYVLCTKAVREELVPALINCLEEF-YGKNPQESEDLGRIINEKHFNRLKALLSS-----GKVAVGGQ 308
Cdd:cd07103 251 SKFRNAGQTCVCANRIYVHESIYDEFVEKLVERVKKLkVGNGLDEGTDMGPLINERAVEKVEALVEDavakgAKVLTGGK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 309 TDEKDKY-IAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSG--- 384
Cdd:cd07103 331 RLGLGGYfYEPTVLTDVTDDMLIMNEETFGPVAPIIPFDTEDEVIARANDTPYGLAAYVFTRDLARAWRVAEALEAGmvg 410
|
410 420 430
....*....|....*....|....*....|
gi 2119029253 385 ---GFCSNDCImqmtlfslPFGGVGDSGMG 411
Cdd:cd07103 411 intGLISDAEA--------PFGGVKESGLG 432
|
|
| ALDH_AldA-AAD23400 |
cd07106 |
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative ... |
7-416 |
1.58e-61 |
|
Streptomyces aureofaciens putative aldehyde dehydrogenase AldA (AAD23400)-like; Putative aldehyde dehydrogenase, AldA, from Streptomyces aureofaciens (locus AAD23400) and other similar sequences are present in this CD.
Pssm-ID: 143424 [Multi-domain] Cd Length: 446 Bit Score: 207.00 E-value: 1.58e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 7 VAARlREAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESIIsevlftknEIVCAINnlteWMK--- 83
Cdd:cd07106 25 VAAA-KAAFPGWSATPLEERRAALLAIADAIEANAEELARLLTLEQGKPLAEAQF--------EVGGAVA----WLRyta 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 84 -----PEYVEKTlvtklDTCFIKKE--PFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPK 156
Cdd:cd07106 92 sldlpDEVIEDD-----DTRRVELRrkPLGVVAAIVPWNFPLLLAAWKIAPALLAGNTVVLKPSPFTPLCTLKLGELAQE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 157 YLDKDCFAVVCGGvKETTELLEE--KFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAW 234
Cdd:cd07106 167 VLPPGVLNVVSGG-DELGPALTShpDIRKISFTGSTATGKKVMASAAKTLKRVTLELGGNDAAIVLPDVDIDAVAPKLFW 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 235 ARFLNMGQTCIAPDYVLCTKAVREELVPALINCLEEFY-GKNPQESEDLGRIINEKHFNRLKALLSS-----GKVAVGGQ 308
Cdd:cd07106 246 GAFINSGQVCAAIKRLYVHESIYDEFCEALVALAKAAVvGDGLDPGTTLGPVQNKMQYDKVKELVEDakakgAKVLAGGE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 309 TDEKDKY-IAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFC 387
Cdd:cd07106 326 PLDGPGYfIPPTIVDDPPEGSRIVDEEQFGPVLPVLKYSDEDEVIARANDSEYGLGASVWSSDLERAEAVARRLEAGTVW 405
|
410 420 430
....*....|....*....|....*....|.
gi 2119029253 388 SNdcimQMTLFS--LPFGGVGDSGMGMYHGR 416
Cdd:cd07106 406 IN----THGALDpdAPFGGHKQSGIGVEFGI 432
|
|
| ALDH_SaliADH |
cd07105 |
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2. ... |
99-426 |
1.11e-60 |
|
Salicylaldehyde dehydrogenase, DoxF-like; Salicylaldehyde dehydrogenase (DoxF, SaliADH, EC=1.2.1.65) involved in the upper naphthalene catabolic pathway of Pseudomonas strain C18 and other similar sequences are present in this CD.
Pssm-ID: 143423 [Multi-domain] Cd Length: 432 Bit Score: 204.35 E-value: 1.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 99 FIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSEL-----LPKyldkdcfavvcgGV--- 170
Cdd:cd07105 93 MVVKEPVGVVLGIAPWNAPVILGTRAIAYPLAAGNTVVLKASELSPRTHWLIGRVfheagLPK------------GVlnv 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 171 --------KETTELLEE----KFdyIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFL 238
Cdd:cd07105 161 vthspedaPEVVEALIAhpavRK--VNFTGSTRVGRIIAETAAKHLKPVLLELGGKAPAIVLEDADLDAAANAALFGAFL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 239 NMGQTCIAPDYVLCTKAVREELVPALINCLEEFygknPQESEDLGRIINEKHFNRLKALLSS-----GKVAVGGQTDEKD 313
Cdd:cd07105 239 NSGQICMSTERIIVHESIADEFVEKLKAAAEKL----FAGPVVLGSLVSAAAADRVKELVDDalskgAKLVVGGLADESP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 314 K--YIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGfcsndC 391
Cdd:cd07105 315 SgtSMPPTILDNVTPDMDIYSEESFGPVVSIIRVKDEEEAVRIANDSEYGLSAAVFTRDLARALAVAKRIESGA-----V 389
|
330 340 350
....*....|....*....|....*....|....*....
gi 2119029253 392 -IMQMTL---FSLPFGGVGDSGMGMYHGRFSFDTFSHKR 426
Cdd:cd07105 390 hINGMTVhdePTLPHGGVKSSGYGRFNGKWGIDEFTETK 428
|
|
| ALDH_GABALDH-PuuC |
cd07112 |
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase ... |
12-411 |
1.20e-60 |
|
Escherichia coli NADP+-dependent gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase PuuC-like; NADP+-dependent, gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase (GABALDH) PuuC of Escherichia coli which catalyzes the conversion of putrescine to 4-aminobutanoate and other similar sequences are present in this CD.
Pssm-ID: 143430 [Multi-domain] Cd Length: 462 Bit Score: 205.14 E-value: 1.20e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 12 REAFNSGK-TRTA-EFRLKQLKAMLNLMKEN--EGALLEALkkDLRKPnfesiISEVLFTknEIVCAINNLTeWmkpeYV 87
Cdd:cd07112 34 RRAFESGVwSRLSpAERKAVLLRLADLIEAHrdELALLETL--DMGKP-----ISDALAV--DVPSAANTFR-W----YA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 88 EktLVTKL----------DTCFIKKEPFGVALIIGPWNYPIQLV---LTPfigAVAAGNCAILKPSEVSPNSSQLLSEL- 153
Cdd:cd07112 100 E--AIDKVygevaptgpdALALITREPLGVVGAVVPWNFPLLMAawkIAP---ALAAGNSVVLKPAEQSPLTALRLAELa 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 154 ----LPKyldkDCFAVVCGGVKETTELL--EEKFDYIFFTGGTHVGKIIMTAAAK-HLTPVSLELGGKNPCYVDKSC-DI 225
Cdd:cd07112 175 leagLPA----GVLNVVPGFGHTAGEALglHMDVDALAFTGSTEVGRRFLEYSGQsNLKRVWLECGGKSPNIVFADApDL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 226 NNTAHRIAWARFLNMGQTCIAPDYVLCTKAVREELVPALINCLEEFYGKNPQE-SEDLGRIINEKHFNRLKALLSSGK-- 302
Cdd:cd07112 251 DAAAEAAAAGIFWNQGEVCSAGSRLLVHESIKDEFLEKVVAAAREWKPGDPLDpATRMGALVSEAHFDKVLGYIESGKae 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 303 ---VAVGG---QTDEKDKYIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTD-NKVVK 375
Cdd:cd07112 331 garLVAGGkrvLTETGGFFVEPTVFDGVTPDMRIAREEIFGPVLSVITFDSEEEAVALANDSVYGLAASVWTSDlSRAHR 410
|
410 420 430
....*....|....*....|....*....|....*....
gi 2119029253 376 dVLERTSSGGF---CSNDCIMQMtlfslPFGGVGDSGMG 411
Cdd:cd07112 411 -VARRLRAGTVwvnCFDEGDITT-----PFGGFKQSGNG 443
|
|
| ALDH_AAS00426 |
cd07109 |
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; ... |
12-423 |
3.69e-60 |
|
Uncharacterized Saccharopolyspora spinosa aldehyde dehydrogenase (AAS00426)-like; Uncharacterized aldehyde dehydrogenase of Saccharopolyspora spinosa (AAS00426) and other similar sequences, are present in this CD.
Pssm-ID: 143427 [Multi-domain] Cd Length: 454 Bit Score: 203.62 E-value: 3.69e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 12 REAFNSGKTR-TAEFRLKQLKAMLNLMKEN--EGALLEALkkDLRKPNFESiisevlftKNEIVCAINNLtewmkpEYVE 88
Cdd:cd07109 29 RRAFESGWLRlSPAERGRLLLRIARLIREHadELARLESL--DTGKPLTQA--------RADVEAAARYF------EYYG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 89 KTlVTKLD----------TCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY- 157
Cdd:cd07109 93 GA-ADKLHgetiplgpgyFVYTVREPHGVTGHIIPWNYPLQITGRSVAPALAAGNAVVVKPAEDAPLTALRLAELAEEAg 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 158 LDKDCFAVVCGGVKETTELLEE--KFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWA 235
Cdd:cd07109 172 LPAGALNVVTGLGAEAGAALVAhpGVDHISFTGSVETGIAVMRAAAENVVPVTLELGGKSPQIVFADADLEAALPVVVNA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 236 RFLNMGQTCIAPDYVLCTKAVREELVPALINCLEEFYGKNPQESEDLGRIINEKHFNRLKALL-----SSGKVAVGGQ-- 308
Cdd:cd07109 252 IIQNAGQTCSAGSRLLVHRSIYDEVLERLVERFRALRVGPGLEDPDLGPLISAKQLDRVEGFVararaRGARIVAGGRia 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 309 --TDEKDKYIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGgf 386
Cdd:cd07109 332 egAPAGGYFVAPTLLDDVPPDSRLAQEEIFGPVLAVMPFDDEAEAIALANGTDYGLVAGVWTRDGDRALRVARRLRAG-- 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 2119029253 387 csndcimQMTL--------FSLPFGGVGDSGMGMYHGRFSFDTFS 423
Cdd:cd07109 410 -------QVFVnnygagggIELPFGGVKKSGHGREKGLEALYNYT 447
|
|
| ALDH_F8_HMSADH |
cd07093 |
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase ... |
2-423 |
3.88e-60 |
|
Human aldehyde dehydrogenase family 8 member A1-like; In humans, the aldehyde dehydrogenase family 8 member A1 (ALDH8A1) protein functions to convert 9-cis-retinal to 9-cis-retinoic acid and has a preference for NAD+. Also included in this CD is the 2-hydroxymuconic semialdehyde dehydrogenase (HMSADH) which catalyzes the conversion of 2-hydroxymuconic semialdehyde to 4-oxalocrotonate, a step in the meta cleavage pathway of aromatic hydrocarbons in bacteria. Such HMSADHs seen here are: XylG of the TOL plasmid pWW0 of Pseudomonas putida, TomC of Burkholderia cepacia G4, and AphC of Comamonas testosterone.
Pssm-ID: 143412 [Multi-domain] Cd Length: 455 Bit Score: 203.57 E-value: 3.88e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 2 SSTKEVAARL---REAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPnfesiisEVLFTKNEIVCAINNL 78
Cdd:cd07093 16 GGAAEVDAAVaaaKEAFPGWSRMSPAERARILHKVADLIEARADELALLESLDTGKP-------ITLARTRDIPRAAANF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 79 ---TEWMKpeYVEKTLVTKLDTC--FIKKEPFGVALIIGPWNYPIQLvLTPFIG-AVAAGNCAILKPSEVSPNSSQLLSE 152
Cdd:cd07093 89 rffADYIL--QLDGESYPQDGGAlnYVLRQPVGVAGLITPWNLPLML-LTWKIApALAFGNTVVLKPSEWTPLTAWLLAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 153 L-----LPKyldkDCFAVVCGGVKETTELLEE--KFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDI 225
Cdd:cd07093 166 LaneagLPP----GVVNVVHGFGPEAGAALVAhpDVDLISFTGETATGRTIMRAAAPNLKPVSLELGGKNPNIVFADADL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 226 NNTAHRIAWARFLNMGQTCIAPDYVLCTKAVREELVPALINCLEEFYGKNP-QESEDLGRIINEKHFNRLK-----ALLS 299
Cdd:cd07093 242 DRAVDAAVRSSFSNNGEVCLAGSRILVQRSIYDEFLERFVERAKALKVGDPlDPDTEVGPLISKEHLEKVLgyvelARAE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 300 SGKVAVGGQTDEKDK-----YIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVV 374
Cdd:cd07093 322 GATILTGGGRPELPDleggyFVEPTVITGLDNDSRVAQEEIFGPVVTVIPFDDEEEAIELANDTPYGLAAYVWTRDLGRA 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2119029253 375 KDVLERTSSGGFCSNdCIMQMTLfSLPFGGVGDSGMGMYHGRFSFDTFS 423
Cdd:cd07093 402 HRVARRLEAGTVWVN-CWLVRDL-RTPFGGVKASGIGREGGDYSLEFYT 448
|
|
| ALDH_SNDH |
cd07118 |
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone ... |
102-423 |
1.26e-59 |
|
Gluconobacter oxydans L-sorbosone dehydrogenase-like; Included in this CD is the L-sorbosone dehydrogenase (SNDH) from Gluconobacter oxydans UV10. In G. oxydans, D-sorbitol is converted to 2-keto-L-gulonate (a precursor of L-ascorbic acid) in sequential oxidation steps catalyzed by a FAD-dependent, L-sorbose dehydrogenase and an NAD(P)+-dependent, L-sorbosone dehydrogenase.
Pssm-ID: 143436 [Multi-domain] Cd Length: 454 Bit Score: 202.18 E-value: 1.26e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 102 KEPFGVALIIGPWNYPIqLVLT---PFigAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFAVVCGGVKETTELL 177
Cdd:cd07118 117 REPIGVVGIITPWNFPF-LILSqklPF--ALAAGCTVVVKPSEFTSGTTLMLAELLIEAgLPAGVVNIVTGYGATVGQAM 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 178 EE--KFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTKA 255
Cdd:cd07118 194 TEhpDVDMVSFTGSTRVGKAIAAAAARNLKKVSLELGGKNPQIVFADADLDAAADAVVFGVYFNAGECCNSGSRLLVHES 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 256 VREELVPALINCLEEFYGKNP-QESEDLGRIINEKHFNRLKALLSSGK-----VAVGGQTDEKDK--YIAPTVLVDVKET 327
Cdd:cd07118 274 IADAFVAAVVARSRKVRVGDPlDPETKVGAIINEAQLAKITDYVDAGRaegatLLLGGERLASAAglFYQPTIFTDVTPD 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 328 DPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNdCIMQMTLfSLPFGGVGD 407
Cdd:cd07118 354 MAIAREEIFGPVLSVLTFDTVDEAIALANDTVYGLSAGVWSKDIDTALTVARRIRAGTVWVN-TFLDGSP-ELPFGGFKQ 431
|
330
....*....|....*.
gi 2119029253 408 SGMGMYHGRFSFDTFS 423
Cdd:cd07118 432 SGIGRELGRYGVEEYT 447
|
|
| ALDH_LactADH-AldA |
cd07088 |
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from ... |
2-380 |
4.41e-59 |
|
Escherichia coli lactaldehyde dehydrogenase AldA-like; Lactaldehyde dehydrogenase from Escherichia coli (AldA, LactADH, EC=1.2.1.22), an NAD(+)-dependent enzyme involved in the metabolism of L-fucose and L-rhamnose, and other similar sequences are present in this CD.
Pssm-ID: 143407 [Multi-domain] Cd Length: 468 Bit Score: 200.95 E-value: 4.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 2 SSTKEVAARL----REAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPnfesiISEvlfTKNEIVCAINN 77
Cdd:cd07088 31 AATAEDADRAvdaaEAAQKAWERLPAIERAAYLRKLADLIRENADELAKLIVEEQGKT-----LSL---ARVEVEFTADY 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 78 L---TEW---MKPEYVEKTlvTKLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLS 151
Cdd:cd07088 103 IdymAEWarrIEGEIIPSD--RPNENIFIFKVPIGVVAGILPWNFPFFLIARKLAPALVTGNTIVIKPSEETPLNALEFA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 152 ELLPKY-LDKDCFAVVCGGVKETTELL--EEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNT 228
Cdd:cd07088 181 ELVDEAgLPAGVLNIVTGRGSVVGDALvaHPKVGMISLTGSTEAGQKIMEAAAENITKVSLELGGKAPAIVMKDADLDLA 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 229 AHRIAWARFLNMGQTCIAPDYVLCTKAVREELVPALINCLEEFYGKNP-QESEDLGRIINEKHFNRLKALL-----SSGK 302
Cdd:cd07088 261 VKAIVDSRIINCGQVCTCAERVYVHEDIYDEFMEKLVEKMKAVKVGDPfDAATDMGPLVNEAALDKVEEMVeraveAGAT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 303 VAVGGQTDEKDK--YIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLER 380
Cdd:cd07088 341 LLTGGKRPEGEKgyFYEPTVLTNVRQDMEIVQEEIFGPVLPVVKFSSLDEAIELANDSEYGLTSYIYTENLNTAMRATNE 420
|
|
| ALDH_BenzADH-like |
cd07104 |
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, ... |
100-426 |
9.44e-57 |
|
ALDH subfamily: NAD(P)+-dependent benzaldehyde dehydrogenase II, vanillin dehydrogenase, p-hydroxybenzaldehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD(P)+-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) involved in the oxidation of benzyl alcohol to benzoate; p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes the oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid; vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid as seen in Pseudomonas putida KT2440; and other related sequences.
Pssm-ID: 143422 [Multi-domain] Cd Length: 431 Bit Score: 193.90 E-value: 9.44e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 100 IKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLL-SEL-----LPKYLdkdcFAVVCGGVKET 173
Cdd:cd07104 94 VRRVPLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDSRTPVTGGLLiAEIfeeagLPKGV----LNVVPGGGSEI 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 174 TELL--EEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVL 251
Cdd:cd07104 170 GDALveHPRVRMISFTGSTAVGRHIGELAGRHLKKVALELGGNNPLIVLDDADLDLAVSAAAFGAFLHQGQICMAAGRIL 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 252 CTKAVREELVPALINCLEEF-YGkNPQESE-DLGRIINEKHFNRLKALLSS-----GKVAVGGQTDekDKYIAPTVLVDV 324
Cdd:cd07104 250 VHESVYDEFVEKLVAKAKALpVG-DPRDPDtVIGPLINERQVDRVHAIVEDavaagARLLTGGTYE--GLFYQPTVLSDV 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 325 KETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDcimqMTL---FSLP 401
Cdd:cd07104 327 TPDMPIFREEIFGPVAPVIPFDDDEEAVELANDTEYGLSAAVFTRDLERAMAFAERLETGMVHIND----QTVndePHVP 402
|
330 340
....*....|....*....|....*
gi 2119029253 402 FGGVGDSGMGMYHGRFSFDTFSHKR 426
Cdd:cd07104 403 FGGVKASGGGRFGGPASLEEFTEWQ 427
|
|
| ALDH_MGR_2402 |
cd07108 |
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent ... |
101-426 |
4.02e-56 |
|
Magnetospirillum NAD(P)+-dependent aldehyde dehydrogenase MSR-1-like; NAD(P)+-dependent aldehyde dehydrogenase of Magnetospirillum gryphiswaldense MSR-1 (MGR_2402) , and other similar sequences, are present in this CD.
Pssm-ID: 143426 Cd Length: 457 Bit Score: 192.96 E-value: 4.02e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 101 KKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKYLDKDCFAVVCGGVKETTELLEE- 179
Cdd:cd07108 114 VREPLGVVGAILPWNAPLMLAALKIAPALVAGNTVVLKAAEDAPLAVLLLAEILAQVLPAGVLNVITGYGEECGAALVDh 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 180 -KFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHR-IAWARFLNMGQTCIAPDYVLCTKAVR 257
Cdd:cd07108 194 pDVDKVTFTGSTEVGKIIYRAAADRLIPVSLELGGKSPMIVFPDADLDDAVDGaIAGMRFTRQGQSCTAGSRLFVHEDIY 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 258 EELVPALINCLEEFYGKNP-QESEDLGRIINEKHFNRLKALLSSG------KVAVGGQ-----TDEKDKYIAPTVLVDVK 325
Cdd:cd07108 274 DAFLEKLVAKLSKLKIGDPlDEATDIGAIISEKQFAKVCGYIDLGlstsgaTVLRGGPlpgegPLADGFFVQPTIFSGVD 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 326 ETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCIMQMTlfSLPFGGV 405
Cdd:cd07108 354 NEWRLAREEIFGPVLCAIPWKDEDEVIAMANDSHYGLAAYVWTRDLGRALRAAHALEAGWVQVNQGGGQQP--GQSYGGF 431
|
330 340
....*....|....*....|....*
gi 2119029253 406 GDSGMGMyhgRFSF----DTFSHKR 426
Cdd:cd07108 432 KQSGLGR---EASLegmlEHFTQKK 453
|
|
| ALDH_y4uC |
cd07149 |
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; ... |
5-411 |
3.16e-55 |
|
Uncharacterized ALDH (y4uC) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (ORF name y4uC) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143467 [Multi-domain] Cd Length: 453 Bit Score: 190.50 E-value: 3.16e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 5 KEVAARLREAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPnfesiiseVLFTKNEIVCAINNLT---EW 81
Cdd:cd07149 24 EKAIAAAKEGAKEMKSLPAYERAEILERAAQLLEERREEFARTIALEAGKP--------IKDARKEVDRAIETLRlsaEE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 82 MKPEYVEktlVTKLD--------TCFIKKEPFGVALIIGPWNYPIQLV---LTPfigAVAAGNCAILKPSEVSPNSSQLL 150
Cdd:cd07149 96 AKRLAGE---TIPFDaspggegrIGFTIREPIGVVAAITPFNFPLNLVahkVGP---AIAAGNAVVLKPASQTPLSALKL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 151 SELLPK-YLDKDCFAVVCGGVKET-TELLEEK-FDYIFFTGGTHVGKIIMTAAAkhLTPVSLELGGKNPCYVDKSCDINN 227
Cdd:cd07149 170 AELLLEaGLPKGALNVVTGSGETVgDALVTDPrVRMISFTGSPAVGEAIARKAG--LKKVTLELGSNAAVIVDADADLEK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 228 TAHRIAWARFLNMGQTCIAPDYVLCTKAVREELVPALINCLEEFYGKNPQESE-DLGRIINEKHFNRLKALLSS-----G 301
Cdd:cd07149 248 AVERCVSGAFANAGQVCISVQRIFVHEDIYDEFLERFVAATKKLVVGDPLDEDtDVGPMISEAEAERIEEWVEEaveggA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 302 KVAVGGQTDEKdkYIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERT 381
Cdd:cd07149 328 RLLTGGKRDGA--ILEPTVLTDVPPDMKVVCEEVFAPVVSLNPFDTLDEAIAMANDSPYGLQAGVFTNDLQKALKAAREL 405
|
410 420 430
....*....|....*....|....*....|
gi 2119029253 382 SSGGFCSNDcIMQMTLFSLPFGGVGDSGMG 411
Cdd:cd07149 406 EVGGVMIND-SSTFRVDHMPYGGVKESGTG 434
|
|
| ALDH_VaniDH_like |
cd07150 |
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved ... |
102-427 |
6.14e-55 |
|
Pseudomonas putida vanillin dehydrogenase-like; Vanillin dehydrogenase (Vdh, VaniDH) involved in the metabolism of ferulic acid and other related sequences are included in this CD. The E. coli vanillin dehydrogenase (LigV) preferred NAD+ to NADP+ and exhibited a broad substrate preference, including vanillin, benzaldehyde, protocatechualdehyde, m-anisaldehyde, and p-hydroxybenzaldehyde.
Pssm-ID: 143468 [Multi-domain] Cd Length: 451 Bit Score: 189.85 E-value: 6.14e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 102 KEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFAVVCGGVKETTELL--E 178
Cdd:cd07150 117 RRPLGVVAGITPFNYPLILATKKVAFALAAGNTVVLKPSEETPVIGLKIAEIMEEAgLPKGVFNVVTGGGAEVGDELvdD 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 179 EKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTKAVRE 258
Cdd:cd07150 197 PRVRMVTFTGSTAVGREIAEKAGRHLKKITLELGGKNPLIVLADADLDYAVRAAAFGAFMHQGQICMSASRIIVEEPVYD 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 259 ELVPALINCLEEFYGKNP-QESEDLGRIINEKHFNRLK-----ALLSSGKVAVGGQTDekDKYIAPTVLVDVKETDPVMQ 332
Cdd:cd07150 277 EFVKKFVARASKLKVGDPrDPDTVIGPLISPRQVERIKrqvedAVAKGAKLLTGGKYD--GNFYQPTVLTDVTPDMRIFR 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 333 EEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCIMqMTLFSLPFGGVGDSGMGM 412
Cdd:cd07150 355 EETFGPVTSVIPAKDAEEALELANDTEYGLSAAILTNDLQRAFKLAERLESGMVHINDPTI-LDEAHVPFGGVKASGFGR 433
|
330
....*....|....*
gi 2119029253 413 YHGRFSFDTFSHKRA 427
Cdd:cd07150 434 EGGEWSMEEFTELKW 448
|
|
| ALDH_CddD_SSP0762 |
cd07138 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase ... |
7-422 |
1.77e-54 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid, and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and other similar sequences, are included in this CD.
Pssm-ID: 143456 [Multi-domain] Cd Length: 466 Bit Score: 188.87 E-value: 1.77e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 7 VAARlREAFNS-GKTRTAEfRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESIISEVLFTKNEIVCAINNLTEWMKPE 85
Cdd:cd07138 42 VAAA-RRAFPAwSATSVEE-RAALLERIAEAYEARADELAQAITLEMGAPITLARAAQVGLGIGHLRAAADALKDFEFEE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 86 YVEKTLVTKldtcfikkEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFA 164
Cdd:cd07138 120 RRGNSLVVR--------EPIGVCGLITPWNWPLNQIVLKVAPALAAGCTVVLKPSEVAPLSAIILAEILDEAgLPAGVFN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 165 VVCGGVKETTELLEE--KFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQ 242
Cdd:cd07138 192 LVNGDGPVVGEALSAhpDVDMVSFTGSTRAGKRVAEAAADTVKRVALELGGKSANIILDDADLEKAVPRGVAACFANSGQ 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 243 TCIAPDYVLCTKAVREELVPALINCLEEFYGKNPQESED-LGRIINEKHFNRLKALLSSG-----KVAVGG----QTDEK 312
Cdd:cd07138 272 SCNAPTRMLVPRSRYAEAEEIAAAAAEAYVVGDPRDPATtLGPLASAAQFDRVQGYIQKGieegaRLVAGGpgrpEGLER 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 313 DKYIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDci 392
Cdd:cd07138 352 GYFVKPTVFADVTPDMTIAREEIFGPVLSIIPYDDEDEAIAIANDTPYGLAGYVWSADPERARAVARRLRAGQVHING-- 429
|
410 420 430
....*....|....*....|....*....|..
gi 2119029253 393 mqmTLFSL--PFGGVGDSGMGMYHGRFSFDTF 422
Cdd:cd07138 430 ---AAFNPgaPFGGYKQSGNGREWGRYGLEEF 458
|
|
| ALDH_CddD-AldA-like |
cd07089 |
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric ... |
8-423 |
3.45e-54 |
|
Rhodococcus ruber 6-oxolauric acid dehydrogenase-like and related proteins; The 6-oxolauric acid dehydrogenase (CddD) from Rhodococcus ruber SC1 which converts 6-oxolauric acid to dodecanedioic acid; and the aldehyde dehydrogenase (locus SSP0762) from Staphylococcus saprophyticus subsp. saprophyticus ATCC 15305 and also, the Mycobacterium tuberculosis H37Rv ALDH AldA (locus Rv0768) sequence; and other similar sequences, are included in this CD.
Pssm-ID: 143408 [Multi-domain] Cd Length: 459 Bit Score: 187.84 E-value: 3.45e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 8 AARlrEAFNSGKTRT-AEFRLKQLKAMLnlmkenegALLEALKKDLRkpnfESIISEV-----LFTKNEIVCAINNLTEW 81
Cdd:cd07089 27 AAR--RAFDTGDWSTdAEERARCLRQLH--------EALEARKEELR----ALLVAEVgapvmTARAMQVDGPIGHLRYF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 82 --MKPEY------VEKTLVTKLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSEL 153
Cdd:cd07089 93 adLADSFpwefdlPVPALRGGPGRRVVRREPVGVVAAITPWNFPFFLNLAKLAPALAAGNTVVLKPAPDTPLSALLLGEI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 154 -----LPKyldkDCFAVVCGGVKETTELL--EEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDIN 226
Cdd:cd07089 173 iaetdLPA----GVVNVVTGSDNAVGEALttDPRVDMVSFTGSTAVGRRIMAQAAATLKRVLLELGGKSANIVLDDADLA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 227 NTAHRIAWARFLNMGQTCIAPDYVLCTKAVREELVPALINCLEEFYGKNPQESED-LGRIINEKHFNRLKALLSSGK--- 302
Cdd:cd07089 249 AAAPAAVGVCMHNAGQGCALTTRLLVPRSRYDEVVEALAAAFEALPVGDPADPGTvMGPLISAAQRDRVEGYIARGRdeg 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 303 ---VAVGGQTDEKDK--YIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDV 377
Cdd:cd07089 329 arlVTGGGRPAGLDKgfYVEPTLFADVDNDMRIAQEEIFGPVLVVIPYDDDDEAVRIANDSDYGLSGGVWSADVDRAYRV 408
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2119029253 378 LERTSSGGFCSNDCIMQMTlfSLPFGGVGDSGMGMYHGRFSFDTFS 423
Cdd:cd07089 409 ARRIRTGSVGINGGGGYGP--DAPFGGYKQSGLGRENGIEGLEEFL 452
|
|
| PLN02278 |
PLN02278 |
succinic semialdehyde dehydrogenase |
4-411 |
7.20e-54 |
|
succinic semialdehyde dehydrogenase
Pssm-ID: 215157 [Multi-domain] Cd Length: 498 Bit Score: 187.98 E-value: 7.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 4 TKEVAARLREAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESIisevlftkNEIVCAINNLtEWMK 83
Cdd:PLN02278 64 TNDAIASAHDAFPSWSKLTASERSKILRRWYDLIIANKEDLAQLMTLEQGKPLKEAI--------GEVAYGASFL-EYFA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 84 PE----YVEKTLVTKLDT-CFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSEL-LPKY 157
Cdd:PLN02278 135 EEakrvYGDIIPSPFPDRrLLVLKQPVGVVGAITPWNFPLAMITRKVGPALAAGCTVVVKPSELTPLTALAAAELaLQAG 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 158 LDKDCFAVVCGGVKET-TELLE-EKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWA 235
Cdd:PLN02278 215 IPPGVLNVVMGDAPEIgDALLAsPKVRKITFTGSTAVGKKLMAGAAATVKRVSLELGGNAPFIVFDDADLDVAVKGALAS 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 236 RFLNMGQTCIAPDYVLCTKAVREELVPALINCLEEF-YGKNPQESEDLGRIINEKHFNRLKAL----LSSG-KVAVGGQ- 308
Cdd:PLN02278 295 KFRNSGQTCVCANRILVQEGIYDKFAEAFSKAVQKLvVGDGFEEGVTQGPLINEAAVQKVESHvqdaVSKGaKVLLGGKr 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 309 TDEKDKYIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCS 388
Cdd:PLN02278 375 HSLGGTFYEPTVLGDVTEDMLIFREEVFGPVAPLTRFKTEEEAIAIANDTEAGLAAYIFTRDLQRAWRVSEALEYGIVGV 454
|
410 420
....*....|....*....|...
gi 2119029253 389 NDCIMQMTlfSLPFGGVGDSGMG 411
Cdd:PLN02278 455 NEGLISTE--VAPFGGVKQSGLG 475
|
|
| ALDH_F10_BADH |
cd07110 |
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in ... |
12-424 |
9.71e-54 |
|
Arabidopsis betaine aldehyde dehydrogenase 1 and 2, ALDH family 10A8 and 10A9-like; Present in this CD are the Arabidopsis betaine aldehyde dehydrogenase (BADH) 1 (chloroplast) and 2 (mitochondria), also known as, aldehyde dehydrogenase family 10 member A8 and aldehyde dehydrogenase family 10 member A9, respectively, and are putative dehydration- and salt-inducible BADHs (EC 1.2.1.8) that catalyze the oxidation of betaine aldehyde to the compatible solute glycine betaine.
Pssm-ID: 143428 [Multi-domain] Cd Length: 456 Bit Score: 186.79 E-value: 9.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 12 REAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESIISevlfTKNEIVC----AinNLTEWMKPeYV 87
Cdd:cd07110 29 RRAFPRWKKTTGAERAKYLRAIAEGVRERREELAELEARDNGKPLDEAAWD----VDDVAGCfeyyA--DLAEQLDA-KA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 88 EKTLVTKLD--TCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSEL-----LPKyldk 160
Cdd:cd07110 102 ERAVPLPSEdfKARVRREPVGVVGLITPWNFPLLMAAWKVAPALAAGCTVVLKPSELTSLTELELAEIaaeagLPP---- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 161 DCFAVVCGGVKETTELLEE--KFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFL 238
Cdd:cd07110 178 GVLNVVTGTGDEAGAPLAAhpGIDKISFTGSTATGSQVMQAAAQDIKPVSLELGGKSPIIVFDDADLEKAVEWAMFGCFW 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 239 NMGQTCIAPDYVLCTKAVREELVPALINCLEEFYGKNPQESE-DLGRIINEKHFNRLKALLSSGK-----VAVGG---QT 309
Cdd:cd07110 258 NNGQICSATSRLLVHESIADAFLERLATAAEAIRVGDPLEEGvRLGPLVSQAQYEKVLSFIARGKeegarLLCGGrrpAH 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 310 DEKDKYIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGF--- 386
Cdd:cd07110 338 LEKGYFIAPTVFADVPTDSRIWREEIFGPVLCVRSFATEDEAIALANDSEYGLAAAVISRDAERCDRVAEALEAGIVwin 417
|
410 420 430
....*....|....*....|....*....|....*...
gi 2119029253 387 CSNDCIMQmtlfsLPFGGVGDSGMGMYHGRFSFDTFSH 424
Cdd:cd07110 418 CSQPCFPQ-----APWGGYKRSGIGRELGEWGLDNYLE 450
|
|
| ALDH_SSADH1_GabD1 |
cd07100 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde ... |
6-422 |
1.38e-53 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 1-like; Succinate-semialdehyde dehydrogenase 1 (SSADH1, GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde (SSA) to succinate. SSADH activity in Mycobacterium tuberculosis (Mtb) is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731). The Mtb GabD1 SSADH1 reportedly is an enzyme of the gamma-aminobutyrate shunt, which forms a functional link between two TCA half-cycles by converting alpha-ketoglutarate to succinate.
Pssm-ID: 143418 [Multi-domain] Cd Length: 429 Bit Score: 185.36 E-value: 1.38e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 6 EVAARLREAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESIiSEVlftknEIVCAI-----NNLTE 80
Cdd:cd07100 3 AALDRAHAAFLAWRKTSFAERAALLRKLADLLRERKDELARLITLEMGKPIAEAR-AEV-----EKCAWIcryyaENAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 81 WMKPEYVEktlvTKLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LD 159
Cdd:cd07100 77 FLADEPIE----TDAGKAYVRYEPLGVVLGIMPWNFPFWQVFRFAAPNLMAGNTVLLKHASNVPGCALAIEELFREAgFP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 160 KDCFAVVCGGVKETTELLEEkfDYI---FFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWAR 236
Cdd:cd07100 153 EGVFQNLLIDSDQVEAIIAD--PRVrgvTLTGSERAGRAVAAEAGKNLKKSVLELGGSDPFIVLDDADLDKAVKTAVKGR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 237 FLNMGQTCIAPDYVLCTKAVREELVPALINCLEEFYGKNP-QESEDLGRIINEKHFNRL-----KALLSSGKVAVGGQTD 310
Cdd:cd07100 231 LQNAGQSCIAAKRFIVHEDVYDEFLEKFVEAMAALKVGDPmDEDTDLGPLARKDLRDELheqveEAVAAGATLLLGGKRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 311 EKDK-YIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSN 389
Cdd:cd07100 311 DGPGaFYPPTVLTDVTPGMPAYDEELFGPVAAVIKVKDEEEAIALANDSPFGLGGSVFTTDLERAERVARRLEAGMVFIN 390
|
410 420 430
....*....|....*....|....*....|...
gi 2119029253 390 DciMQMTLFSLPFGGVGDSGMGMYHGRFSFDTF 422
Cdd:cd07100 391 G--MVKSDPRLPFGGVKRSGYGRELGRFGIREF 421
|
|
| ALDH_F1-2_Ald2-like |
cd07091 |
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD ... |
98-411 |
2.19e-53 |
|
ALDH subfamily: ALDH families 1and 2, including 10-formyltetrahydrofolate dehydrogenase, NAD+-dependent retinal dehydrogenase 1 and related proteins; ALDH subfamily which includes the NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36), also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1), in humans, a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism. 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1), in humans, a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. Also included in this subfamily is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial, homotetramers that oxidize acetaldehyde and glycolaldehyde, as well as, the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde. Also included is the AldA aldehyde dehydrogenase of Aspergillus nidulans (locus AN0554), the aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) of Saccharomyces cerevisiae, and other similar sequences.
Pssm-ID: 143410 Cd Length: 476 Bit Score: 186.26 E-value: 2.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 98 CFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFAVVCGGVKETTEL 176
Cdd:cd07091 135 AYTRREPIGVCGQIIPWNFPLLMLAWKLAPALAAGNTVVLKPAEQTPLSALYLAELIKEAgFPPGVVNIVPGFGPTAGAA 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 177 LEE--KFDYIFFTGGTHVGKIIMTAAAK-HLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCT 253
Cdd:cd07091 215 ISShmDVDKIAFTGSTAVGRTIMEAAAKsNLKKVTLELGGKSPNIVFDDADLDKAVEWAAFGIFFNQGQCCCAGSRIFVQ 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 254 KAVREELVPALINCLEEFYGKNPQESEDL-GRIINEKHFNRLKALLSSGK------VAVGGQTDEKDKYIAPTVLVDVKE 326
Cdd:cd07091 295 ESIYDEFVEKFKARAEKRVVGDPFDPDTFqGPQVSKAQFDKILSYIESGKkegatlLTGGERHGSKGYFIQPTVFTDVKD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 327 TDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGF---CSNDCIMQMtlfslPFG 403
Cdd:cd07091 375 DMKIAKEEIFGPVVTILKFKTEDEVIERANDTEYGLAAGVFTKDINKALRVSRALKAGTVwvnTYNVFDAAV-----PFG 449
|
....*...
gi 2119029253 404 GVGDSGMG 411
Cdd:cd07091 450 GFKQSGFG 457
|
|
| ALDH_AldH-CAJ73105 |
cd07131 |
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; ... |
12-427 |
1.56e-52 |
|
Uncharacterized Candidatus kuenenia aldehyde dehydrogenase AldH (CAJ73105)-like; Uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105) and similar sequences with similarity to alpha-aminoadipic semialdehyde dehydrogenase (AASADH, human ALDH7A1, EC=1.2.1.31), Arabidopsis ALDH7B4, and Streptomyces clavuligerus delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH) are included in this CD.
Pssm-ID: 143449 [Multi-domain] Cd Length: 478 Bit Score: 184.09 E-value: 1.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 12 REAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFEsiisevlfTKNEIVCAINnLTEW-------MKP 84
Cdd:cd07131 47 REAFPEWRKVPAPRRAEYLFRAAELLKKRKEELARLVTREMGKPLAE--------GRGDVQEAID-MAQYaagegrrLFG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 85 EYVEKTLVTKLdtCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCF 163
Cdd:cd07131 118 ETVPSELPNKD--AMTRRQPIGVVALITPWNFPVAIPSWKIFPALVCGNTVVFKPAEDTPACALKLVELFAEAgLPPGVV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 164 AVVCGGVKETTELLEE--KFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMG 241
Cdd:cd07131 196 NVVHGRGEEVGEALVEhpDVDVVSFTGSTEVGERIGETCARPNKRVALEMGGKNPIIVMDDADLDLALEGALWSAFGTTG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 242 QTCIAPDYVLCTKAVREELVPALINCLEEFYGKNPQESE-DLGRIINEKHFNRL-----------KALLSSGKVAVGGQT 309
Cdd:cd07131 276 QRCTATSRLIVHESVYDEFLKRFVERAKRLRVGDGLDEEtDMGPLINEAQLEKVlnyneigkeegATLLLGGERLTGGGY 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 310 dEKDKYIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSG-GFCS 388
Cdd:cd07131 356 -EKGYFVEPTVFTDVTPDMRIAQEEIFGPVVALIEVSSLEEAIEIANDTEYGLSSAIYTEDVNKAFRARRDLEAGiTYVN 434
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2119029253 389 NDCIMQMTlfSLPFGGVGDSGMGmyH---GRFSFDTFSHKRA 427
Cdd:cd07131 435 APTIGAEV--HLPFGGVKKSGNG--HreaGTTALDAFTEWKA 472
|
|
| PRK10090 |
PRK10090 |
aldehyde dehydrogenase A; Provisional |
99-370 |
2.57e-51 |
|
aldehyde dehydrogenase A; Provisional
Pssm-ID: 182233 [Multi-domain] Cd Length: 409 Bit Score: 179.16 E-value: 2.57e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 99 FIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFAVVCGGVKETTELL 177
Cdd:PRK10090 66 LLFKRALGVTTGILPWNFPFFLIARKMAPALLTGNTIVIKPSEFTPNNAIAFAKIVDEIgLPKGVFNLVLGRGETVGQEL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 178 --EEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTKA 255
Cdd:PRK10090 146 agNPKVAMVSMTGSVSAGEKIMAAAAKNITKVCLELGGKAPAIVMDDADLDLAVKAIVDSRVINSGQVCNCAERVYVQKG 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 256 VREELVPALINCLEEFYGKNPQESE--DLGRIINEKHFNRLKALLSSG-----KVAVGGQTDEKDKYI-APTVLVDVKET 327
Cdd:PRK10090 226 IYDQFVNRLGEAMQAVQFGNPAERNdiAMGPLINAAALERVEQKVARAveegaRVALGGKAVEGKGYYyPPTLLLDVRQE 305
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2119029253 328 DPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTD 370
Cdd:PRK10090 306 MSIMHEETFGPVLPVVAFDTLEEAIAMANDSDYGLTSSIYTQN 348
|
|
| ALDH_HMSADH_HapE |
cd07115 |
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic ... |
99-427 |
8.24e-51 |
|
Pseudomonas fluorescens 4-hydroxymuconic semialdehyde dehydrogenase-like; 4-hydroxymuconic semialdehyde dehydrogenase (HapE, EC=1.2.1.61) of Pseudomonas fluorescens ACB involved in 4-hydroxyacetophenone degradation, and putative hydroxycaproate semialdehyde dehydrogenase (ChnE) of Brachymonas petroleovorans involved in cyclohexane metabolism, and other similar sequences, are present in this CD.
Pssm-ID: 143433 [Multi-domain] Cd Length: 453 Bit Score: 178.79 E-value: 8.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 99 FIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFAVVCGGVKETTELL 177
Cdd:cd07115 112 YTVREPVGVVGAIVPWNFPLMFAAWKVAPALAAGNTVVLKPAELTPLSALRIAELMAEAgFPAGVLNVVTGFGEVAGAAL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 178 EE--KFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTKA 255
Cdd:cd07115 192 VEhpDVDKITFTGSTAVGRKIMQGAAGNLKRVSLELGGKSANIVFADADLDAAVRAAATGIFYNQGQMCTAGSRLLVHES 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 256 VREELVPALINCLEEFYGKNPQE-SEDLGRIINEKHFNRLKALLSSGK------VAVGGQTDEKDKYIAPTVLVDVKETD 328
Cdd:cd07115 272 IYDEFLERFTSLARSLRPGDPLDpKTQMGPLVSQAQFDRVLDYVDVGReegarlLTGGKRPGARGFFVEPTIFAAVPPEM 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 329 PVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNdcIMQMTLFSLPFGGVGDS 408
Cdd:cd07115 352 RIAQEEIFGPVVSVMRFRDEEEALRIANGTEYGLAAGVWTRDLGRAHRVAAALKAGTVWIN--TYNRFDPGSPFGGYKQS 429
|
330
....*....|....*....
gi 2119029253 409 GMGMYHGRFSFDTFSHKRA 427
Cdd:cd07115 430 GFGREMGREALDEYTEVKS 448
|
|
| ALDH_F21_LactADH-like |
cd07094 |
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related ... |
99-411 |
1.19e-50 |
|
ALDH subfamily: NAD+-dependent, lactaldehyde dehydrogenase, ALDH family 21 A1, and related proteins; ALDH subfamily which includes Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123), and NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) and like sequences.
Pssm-ID: 143413 [Multi-domain] Cd Length: 453 Bit Score: 178.40 E-value: 1.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 99 FIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELL-PKYLDKDCFAVVCGGVKETTELL 177
Cdd:cd07094 118 WTIREPVGVVLAITPFNFPLNLVAHKLAPAIATGCPVVLKPASKTPLSALELAKILvEAGVPEGVLQVVTGEREVLGDAF 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 178 --EEKFDYIFFTGGTHVGKIIMTAAAKhlTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTKA 255
Cdd:cd07094 198 aaDERVAMLSFTGSAAVGEALRANAGG--KRIALELGGNAPVIVDRDADLDAAIEALAKGGFYHAGQVCISVQRIYVHEE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 256 VREELVPALINCLEEFYGKNP-QESEDLGRIINEKHFNRL-----KALLSSGKVAVGGQTDekDKYIAPTVLVDVKETDP 329
Cdd:cd07094 276 LYDEFIEAFVAAVKKLKVGDPlDEDTDVGPLISEEAAERVerwveEAVEAGARLLCGGERD--GALFKPTVLEDVPRDTK 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 330 VMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCimqmTLF---SLPFGGVG 406
Cdd:cd07094 354 LSTEETFGPVVPIIRYDDFEEAIRIANSTDYGLQAGIFTRDLNVAFKAAEKLEVGGVMVNDS----SAFrtdWMPFGGVK 429
|
....*
gi 2119029253 407 DSGMG 411
Cdd:cd07094 430 ESGVG 434
|
|
| ALDH_DhaS |
cd07114 |
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized ... |
98-423 |
1.62e-50 |
|
Uncharacterized Candidatus pelagibacter aldehyde dehydrogenase, DhaS-like; Uncharacterized aldehyde dehydrogenase from Candidatus pelagibacter (DhaS) and other related sequences are present in this CD.
Pssm-ID: 143432 [Multi-domain] Cd Length: 457 Bit Score: 178.13 E-value: 1.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 98 CFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSEL-----LPKYLdkdcFAVVCGGVKE 172
Cdd:cd07114 113 NFTRREPLGVVAAITPWNSPLLLLAKKLAPALAAGNTVVLKPSEHTPASTLELAKLaeeagFPPGV----VNVVTGFGPE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 173 TTELLEE--KFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYV 250
Cdd:cd07114 189 TGEALVEhpLVAKIAFTGGTETGRHIARAAAENLAPVTLELGGKSPNIVFDDADLDAAVNGVVAGIFAAAGQTCVAGSRL 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 251 LCTKAVREELVPALIncleEFYGK----NPQESE-DLGRIINEKHFNRLKALLSSGK-----VAVGGQ---TDEKDK--Y 315
Cdd:cd07114 269 LVQRSIYDEFVERLV----ARARAirvgDPLDPEtQMGPLATERQLEKVERYVARAReegarVLTGGErpsGADLGAgyF 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 316 IAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDciMQM 395
Cdd:cd07114 345 FEPTILADVTNDMRIAQEEVFGPVLSVIPFDDEEEAIALANDSEYGLAAGIWTRDLARAHRVARAIEAGTVWVNT--YRA 422
|
330 340
....*....|....*....|....*...
gi 2119029253 396 TLFSLPFGGVGDSGMGMYHGRFSFDTFS 423
Cdd:cd07114 423 LSPSSPFGGFKDSGIGRENGIEAIREYT 450
|
|
| BADH |
TIGR01804 |
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes ... |
5-423 |
2.38e-50 |
|
betaine-aldehyde dehydrogenase; Under osmotic stress, betaine aldehyde dehydrogenase oxidizes glycine betaine aldehyde into the osmoprotectant glycine betaine, via the second of two oxidation steps from exogenously supplied choline or betaine aldehyde. This choline-glycine betaine synthesis pathway can be found in gram-positive and gram-negative bacteria. In Escherichia coli, betaine aldehyde dehydrogenase (betB) is osmotically co-induced with choline dehydrogenase (betA) in the presence of choline. These dehydrogenases are located in a betaine gene cluster with the upstream choline transporter (betT) and transcriptional regulator (betI). Similar to E.coli, betaine synthesis in Staphylococcus xylosus is also influenced by osmotic stress and the presence of choline with genes localized in a functionally equivalent gene cluster. Organization of the betaine gene cluster in Sinorhizobium meliloti and Bacillus subtilis differs from that of E.coli by the absence of upstream choline transporter and transcriptional regulator homologues. Additionally, B.subtilis co-expresses a type II alcohol dehydrogenase with betaine aldehyde dehydrogenase instead of choline dehydrogenase as in E.coli, St.xylosus, and Si.meliloti. Betaine aldehyde dehydrogenase is a member of the aldehyde dehydrogenase family (pfam00171). [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 200131 [Multi-domain] Cd Length: 467 Bit Score: 178.08 E-value: 2.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 5 KEVAARLReAFNSGKTRTAEFRLKQLKAMLNLMKENEGAL--LEALkkDLRKPNFESIISEVlftkNEIVCAIN---NLT 79
Cdd:TIGR01804 39 RAIAAARR-AQGEWAAMSPMERGRILRRAADLIRERNEELakLETL--DTGKTLQETIVADM----DSGADVFEffaGLA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 80 EWMKPEYVEktlVTKLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-L 158
Cdd:TIGR01804 112 PALNGEIIP---LGGPSFAYTIREPLGVCVGIGAWNYPLQIASWKIAPALAAGNAMVFKPSENTPLTALKVAEIMEEAgL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 159 DKDCFAVVCGGVKETTELLEEK--FDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWAR 236
Cdd:TIGR01804 189 PKGVFNVVQGDGAEVGPLLVNHpdVAKVSFTGGVPTGKKIMAAAAGHLKHVTMELGGKSPLIVFDDADLESAVDGAMLGN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 237 FLNMGQTCIAPDYVLCTKAVREELVPALINCLEEFYGKNP-QESEDLGRIINEKHFNRLKALLSSGK-----VAVGGQTD 310
Cdd:TIGR01804 269 FFSAGQVCSNGTRVFVHKKIKERFLARLVERTERIKLGDPfDEATEMGPLISAAHRDKVLSYIEKGKaegatLATGGGRP 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 311 EKDK-----YIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGG 385
Cdd:TIGR01804 349 ENVGlqngfFVEPTVFADCTDDMTIVREEIFGPVMTVLTFSDEDEVIARANDTEYGLAGGVFTADLGRAHRVADQLEAGT 428
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2119029253 386 FCSND---CIMQMtlfslPFGGVGDSGMGMYHGRFSFDTFS 423
Cdd:TIGR01804 429 VWINTynlYPAEA-----PFGGYKQSGIGRENGKAALAHYT 464
|
|
| ALDH_F9_TMBADH |
cd07090 |
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, ... |
99-424 |
4.50e-50 |
|
NAD+-dependent 4-trimethylaminobutyraldehyde dehydrogenase, ALDH family 9A1; NAD+-dependent, 4-trimethylaminobutyraldehyde dehydrogenase (TMABADH, EC=1.2.1.47), also known as aldehyde dehydrogenase family 9 member A1 (ALDH9A1) in humans, is a cytosolic tetramer which catalyzes the oxidation of gamma-aminobutyraldehyde involved in 4-aminobutyric acid (GABA) biosynthesis and also oxidizes betaine aldehyde (gamma-trimethylaminobutyraldehyde) which is involved in carnitine biosynthesis.
Pssm-ID: 143409 [Multi-domain] Cd Length: 457 Bit Score: 176.73 E-value: 4.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 99 FIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFAVVCGGvKETTELL 177
Cdd:cd07090 111 YTRREPLGVCAGIGAWNYPIQIASWKSAPALACGNAMVYKPSPFTPLTALLLAEILTEAgLPDGVFNVVQGG-GETGQLL 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 178 EEKFDY--IFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTKA 255
Cdd:cd07090 190 CEHPDVakVSFTGSVPTGKKVMSAAAKGIKHVTLELGGKSPLIIFDDADLENAVNGAMMANFLSQGQVCSNGTRVFVQRS 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 256 VREELVPALINCLEEFYGKNP-QESEDLGRIINEKHFNRLKALLSSGK-----VAVGGQ-TDEKDK-----YIAPTVLVD 323
Cdd:cd07090 270 IKDEFTERLVERTKKIRIGDPlDEDTQMGALISEEHLEKVLGYIESAKqegakVLCGGErVVPEDGlengfYVSPCVLTD 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 324 VKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDciMQMTLFSLPFG 403
Cdd:cd07090 350 CTDDMTIVREEIFGPVMSILPFDTEEEVIRRANDTTYGLAAGVFTRDLQRAHRVIAQLQAGTCWINT--YNISPVEVPFG 427
|
330 340
....*....|....*....|.
gi 2119029253 404 GVGDSGMGMYHGRFSFDTFSH 424
Cdd:cd07090 428 GYKQSGFGRENGTAALEHYTQ 448
|
|
| ALDH_PhpJ |
cd07146 |
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative ... |
99-415 |
7.19e-50 |
|
Streptomyces putative phosphonoformaldehyde dehydrogenase PhpJ-like; Putative phosphonoformaldehyde dehydrogenase (PhpJ), an aldehyde dehydrogenase homolog reportedly involved in the biosynthesis of phosphinothricin tripeptides in Streptomyces viridochromogenes DSM 40736, and similar sequences are included in this CD.
Pssm-ID: 143464 [Multi-domain] Cd Length: 451 Bit Score: 176.01 E-value: 7.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 99 FIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFAVVCGGVKETTELL 177
Cdd:cd07146 115 FTLREPLGVVLAITPFNHPLNQVAHKIAPAIAANNRIVLKPSEKTPLSAIYLADLLYEAgLPPDMLSVVTGEPGEIGDEL 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 178 --EEKFDYIFFTGGTHVGKIIM-TAAAKHLTpvsLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTK 254
Cdd:cd07146 195 itHPDVDLVTFTGGVAVGKAIAaTAGYKRQL---LELGGNDPLIVMDDADLERAATLAVAGSYANSGQRCTAVKRILVHE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 255 AVREELVPALINCLEEF-YGKNPQESEDLGRIINEK---HFNR--LKALLSSGKVAVGGQTDekDKYIAPTVLVDVKETD 328
Cdd:cd07146 272 SVADEFVDLLVEKSAALvVGDPMDPATDMGTVIDEEaaiQIENrvEEAIAQGARVLLGNQRQ--GALYAPTVLDHVPPDA 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 329 PVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDcIMQMTLFSLPFGGVGDS 408
Cdd:cd07146 350 ELVTEETFGPVAPVIRVKDLDEAIAISNSTAYGLSSGVCTNDLDTIKRLVERLDVGTVNVNE-VPGFRSELSPFGGVKDS 428
|
....*..
gi 2119029253 409 GMGMYHG 415
Cdd:cd07146 429 GLGGKEG 435
|
|
| ALDH_BenzADH |
cd07152 |
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II ... |
104-426 |
8.07e-50 |
|
NAD-dependent benzaldehyde dehydrogenase II-like; NAD-dependent, benzaldehyde dehydrogenase II (XylC, BenzADH, EC=1.2.1.28) is involved in the oxidation of benzyl alcohol to benzoate. In Acinetobacter calcoaceticus, this process is carried out by the chromosomally encoded, benzyl alcohol dehydrogenase (xylB) and benzaldehyde dehydrogenase II (xylC) enzymes; whereas in Pseudomonas putida they are encoded by TOL plasmids.
Pssm-ID: 143470 [Multi-domain] Cd Length: 443 Bit Score: 175.94 E-value: 8.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 104 PFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSS-----QLLSEL-LPKYLdkdcFAVVCGGVkETTELL 177
Cdd:cd07152 110 PLGVVGVISPFNFPLILAMRSVAPALALGNAVVLKPDPRTPVSGgvviaRLFEEAgLPAGV----LHVLPGGA-DAGEAL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 178 EE--KFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTKA 255
Cdd:cd07152 185 VEdpNVAMISFTGSTAVGRKVGEAAGRHLKKVSLELGGKNALIVLDDADLDLAASNGAWGAFLHQGQICMAAGRHLVHES 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 256 VREELVPALINCLEEFYGKNPQESE-DLGRIINEKHFNRLKALLSS-----GKVAVGGQTDekDKYIAPTVLVDVKETDP 329
Cdd:cd07152 265 VADAYTAKLAAKAKHLPVGDPATGQvALGPLINARQLDRVHAIVDDsvaagARLEAGGTYD--GLFYRPTVLSGVKPGMP 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 330 VMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSND------CIMqmtlfslPFG 403
Cdd:cd07152 343 AFDEEIFGPVAPVTVFDSDEEAVALANDTEYGLSAGIISRDVGRAMALADRLRTGMLHINDqtvndePHN-------PFG 415
|
330 340
....*....|....*....|....
gi 2119029253 404 GVGDSGMGMYHG-RFSFDTFSHKR 426
Cdd:cd07152 416 GMGASGNGSRFGgPANWEEFTQWQ 439
|
|
| ALDH_AldA-Rv0768 |
cd07139 |
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis ... |
97-422 |
8.10e-50 |
|
Mycobacterium tuberculosis aldehyde dehydrogenase AldA-like; The Mycobacterium tuberculosis NAD+-dependent, aldehyde dehydrogenase PDB structure, 3B4W, and the Mycobacterium tuberculosis H37Rv aldehyde dehydrogenase AldA (locus Rv0768) sequence, as well as the Rhodococcus rhodochrous ALDH involved in haloalkane catabolism, and other similar sequences, are included in this CD.
Pssm-ID: 143457 [Multi-domain] Cd Length: 471 Bit Score: 176.61 E-value: 8.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 97 TCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSEL-----LPKYLdkdcFAVVCGGVk 171
Cdd:cd07139 130 HVLVRREPVGVVAAIVPWNAPLFLAALKIAPALAAGCTVVLKPSPETPLDAYLLAEAaeeagLPPGV----VNVVPADR- 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 172 ETTELLEEK--FDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDY 249
Cdd:cd07139 205 EVGEYLVRHpgVDKVSFTGSTAAGRRIAAVCGERLARVTLELGGKSAAIVLDDADLDAAVPGLVPASLMNNGQVCVALTR 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 250 VLCTKAVREELVPALINCLEEFYGKNP-QESEDLGRIINEKHFNRLKALLSSGK------VAVGGQTDEKDK--YIAPTV 320
Cdd:cd07139 285 ILVPRSRYDEVVEALAAAVAALKVGDPlDPATQIGPLASARQRERVEGYIAKGRaegarlVTGGGRPAGLDRgwFVEPTL 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 321 LVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNdciMQMTLFSL 400
Cdd:cd07139 365 FADVDNDMRIAQEEIFGPVLSVIPYDDEDDAVRIANDSDYGLSGSVWTADVERGLAVARRIRTGTVGVN---GFRLDFGA 441
|
330 340
....*....|....*....|..
gi 2119029253 401 PFGGVGDSGMGMYHGRFSFDTF 422
Cdd:cd07139 442 PFGGFKQSGIGREGGPEGLDAY 463
|
|
| ALDH_ALD2-YMR170C |
cd07144 |
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent ... |
12-427 |
2.90e-49 |
|
Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c)-like; NAD(P)+-dependent Saccharomyces cerevisiae aldehyde dehydrogenase 2 (YMR170c, ALD5, EC=1.2.1.5) and other similar sequences, are present in this CD.
Pssm-ID: 143462 Cd Length: 484 Bit Score: 175.29 E-value: 2.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 12 REAFNSGKTR-TAEFRLKQLKAMLNLMKENEGAL--LEALkkDLRKP---NFESIISEVLFTKNeiVCA-----INNLTE 80
Cdd:cd07144 55 RKAFESWWSKvTGEERGELLDKLADLVEKNRDLLaaIEAL--DSGKPyhsNALGDLDEIIAVIR--YYAgwadkIQGKTI 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 81 WMKPEYVEKTLvtkldtcfikKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LD 159
Cdd:cd07144 131 PTSPNKLAYTL----------HEPYGVCGQIIPWNYPLAMAAWKLAPALAAGNTVVIKPAENTPLSLLYFANLVKEAgFP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 160 KDCFAVVCGGVKETTELLEE--KFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARF 237
Cdd:cd07144 201 PGVVNIIPGYGAVAGSALAEhpDVDKIAFTGSTATGRLVMKAAAQNLKAVTLECGGKSPALVFEDADLDQAVKWAAAGIM 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 238 LNMGQTCIAPDYVLCTKAVREELVPALINCLEEFY--GKNPQESEDLGRIINEKHFNRLKALLSSG-----KVAVGG--- 307
Cdd:cd07144 281 YNSGQNCTATSRIYVQESIYDKFVEKFVEHVKQNYkvGSPFDDDTVVGPQVSKTQYDRVLSYIEKGkkegaKLVYGGeka 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 308 -QTDEKDKYIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGF 386
Cdd:cd07144 361 pEGLGKGYFIPPTIFTDVPQDMRIVKEEIFGPVVVISKFKTYEEAIKKANDTTYGLAAAVFTKDIRRAHRVARELEAGMV 440
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2119029253 387 ---CSNDCIMQMtlfslPFGGVGDSGMGMYHGRFSFDTFSHKRA 427
Cdd:cd07144 441 winSSNDSDVGV-----PFGGFKMSGIGRELGEYGLETYTQTKA 479
|
|
| ALDH_LactADH_F420-Bios |
cd07145 |
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, ... |
85-411 |
3.37e-49 |
|
Methanocaldococcus jannaschii NAD+-dependent lactaldehyde dehydrogenase-like; NAD+-dependent, lactaldehyde dehydrogenase (EC=1.2.1.22) involved the biosynthesis of coenzyme F(420) in Methanocaldococcus jannaschii through the oxidation of lactaldehyde to lactate and generation of NAPH, and similar sequences are included in this CD.
Pssm-ID: 143463 [Multi-domain] Cd Length: 456 Bit Score: 174.46 E-value: 3.37e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 85 EYVEKTLVtkldtcFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCF 163
Cdd:cd07145 110 EYNERRIA------FTVREPIGVVGAITPFNFPANLFAHKIAPAIAVGNSVVVKPSSNTPLTAIELAKILEEAgLPPGVI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 164 AVVCGGVKET-TELLE-EKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMG 241
Cdd:cd07145 184 NVVTGYGSEVgDEIVTnPKVNMISFTGSTAVGLLIASKAGGTGKKVALELGGSDPMIVLKDADLERAVSIAVRGRFENAG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 242 QTCIAPDYVLCTKAVREELVPALINCLEEFYGKNP-QESEDLGRIINEKHFNRL-----KALLSSGKVAVGGQTDEKdKY 315
Cdd:cd07145 264 QVCNAVKRILVEEEVYDKFLKLLVEKVKKLKVGDPlDESTDLGPLISPEAVERMenlvnDAVEKGGKILYGGKRDEG-SF 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 316 IAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTD-NKVVKdVLERTSSGGFCSNDCimq 394
Cdd:cd07145 343 FPPTVLENDTPDMIVMKEEVFGPVLPIAKVKDDEEAVEIANSTEYGLQASVFTNDiNRALK-VARELEAGGVVINDS--- 418
|
330 340
....*....|....*....|
gi 2119029253 395 mTLF---SLPFGGVGDSGMG 411
Cdd:cd07145 419 -TRFrwdNLPFGGFKKSGIG 437
|
|
| PRK13473 |
PRK13473 |
aminobutyraldehyde dehydrogenase; |
97-413 |
7.33e-49 |
|
aminobutyraldehyde dehydrogenase;
Pssm-ID: 237391 Cd Length: 475 Bit Score: 173.94 E-value: 7.33e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 97 TCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKYLDKDCFAVVCGGVKETTEL 176
Cdd:PRK13473 131 TSMIRRDPVGVVASIAPWNYPLMMAAWKLAPALAAGNTVVLKPSEITPLTALKLAELAADILPPGVLNVVTGRGATVGDA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 177 L--EEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTK 254
Cdd:PRK13473 211 LvgHPKVRMVSLTGSIATGKHVLSAAADSVKRTHLELGGKAPVIVFDDADLDAVVEGIRTFGYYNAGQDCTAACRIYAQR 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 255 AVREELVPALINCLEEF-YGKNPQESEDLGRIINEKHFNRLKAL------LSSGKVAVGGQT-DEKDKYIAPTVLVDVKE 326
Cdd:PRK13473 291 GIYDDLVAKLAAAVATLkVGDPDDEDTELGPLISAAHRDRVAGFverakaLGHIRVVTGGEApDGKGYYYEPTLLAGARQ 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 327 TDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCIMqmtLFS-LPFGGV 405
Cdd:PRK13473 371 DDEIVQREVFGPVVSVTPFDDEDQAVRWANDSDYGLASSVWTRDVGRAHRVSARLQYGCTWVNTHFM---LVSeMPHGGQ 447
|
330
....*....|..
gi 2119029253 406 GDSG----MGMY 413
Cdd:PRK13473 448 KQSGygkdMSLY 459
|
|
| ALDH_F6_MMSDH |
cd07085 |
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate ... |
1-359 |
2.12e-48 |
|
Methylmalonate semialdehyde dehydrogenase and ALDH family members 6A1 and 6B2; Methylmalonate semialdehyde dehydrogenase (MMSDH, EC=1.2.1.27) [acylating] from Bacillus subtilis is involved in valine metabolism and catalyses the NAD+- and CoA-dependent oxidation of methylmalonate semialdehyde into propionyl-CoA. Mitochondrial human MMSDH ALDH6A1 and Arabidopsis MMSDH ALDH6B2 are also present in this CD.
Pssm-ID: 143404 [Multi-domain] Cd Length: 478 Bit Score: 172.70 E-value: 2.12e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 1 MSSTKEVAARL---REAFN-----SGKTRTA-EFRLKQL-----KAMLNLMKENEGALLEALKKDLRKpnfeSIisEVLf 66
Cdd:cd07085 34 LATAEEVDAAVaaaKAAFPawsatPVLKRQQvMFKFRQLleenlDELARLITLEHGKTLADARGDVLR----GL--EVV- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 67 tknEIVCAINNLtewMKPEYVEKtlVTKLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNS 146
Cdd:cd07085 107 ---EFACSIPHL---LKGEYLEN--VARGIDTYSYRQPLGVVAGITPFNFPAMIPLWMFPMAIACGNTFVLKPSERVPGA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 147 SQLLSELLPKY-LDKDCFAVVCGGVKETTELLEE-KFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCD 224
Cdd:cd07085 179 AMRLAELLQEAgLPDGVLNVVHGGKEAVNALLDHpDIKAVSFVGSTPVGEYIYERAAANGKRVQALGGAKNHAVVMPDAD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 225 INNTAHRIAWARFLNMGQTCIAPDYVLCTKAVREELVPALINCLEEF-YGKNPQESEDLGRIINEKHFNRLKALLSSG-- 301
Cdd:cd07085 259 LEQTANALVGAAFGAAGQRCMALSVAVAVGDEADEWIPKLVERAKKLkVGAGDDPGADMGPVISPAAKERIEGLIESGve 338
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119029253 302 ---KVAVGGQTDEKDKY-----IAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHE 359
Cdd:cd07085 339 egaKLVLDGRGVKVPGYengnfVGPTILDNVTPDMKIYKEEIFGPVLSIVRVDTLDEAIAIINANP 404
|
|
| ALDH_BADH-GbsA |
cd07119 |
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is ... |
12-423 |
1.07e-47 |
|
Bacillus subtilis NAD+-dependent betaine aldehyde dehydrogenase-like; Included in this CD is the NAD+-dependent, betaine aldehyde dehydrogenase (BADH, GbsA, EC=1.2.1.8) of Bacillus subtilis involved in the synthesis of the osmoprotectant glycine betaine from choline or glycine betaine aldehyde.
Pssm-ID: 143437 Cd Length: 482 Bit Score: 170.95 E-value: 1.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 12 REAFNSGKTR--TAEFRLKQLKAMLNLMKENEGAL--LEALkkDLRKPNFESIIsevlftknEIVCAINNLtewmkpEYV 87
Cdd:cd07119 45 RRAFDSGEWPhlPAQERAALLFRIADKIREDAEELarLETL--NTGKTLRESEI--------DIDDVANCF------RYY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 88 EKtLVTKLD----------TCFIKKEPFGVALIIGPWNYPI-QLV--LTPfigAVAAGNCAILKPSEVSPNSSQLLSELL 154
Cdd:cd07119 109 AG-LATKETgevydvpphvISRTVREPVGVCGLITPWNYPLlQAAwkLAP---ALAAGNTVVIKPSEVTPLTTIALFELI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 155 PKY-LDKDCFAVVCGGVKETTELLEE--KFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHR 231
Cdd:cd07119 185 EEAgLPAGVVNLVTGSGATVGAELAEspDVDLVSFTGGTATGRSIMRAAAGNVKKVALELGGKNPNIVFADADFETAVDQ 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 232 IAWARFLNMGQTCIAPDYVLCTKAVREELVPALINCLEEFYGKNPQESE-DLGRIINEKHFNRLKALLSSG-----KVAV 305
Cdd:cd07119 265 ALNGVFFNAGQVCSAGSRLLVEESIHDKFVAALAERAKKIKLGNGLDADtEMGPLVSAEHREKVLSYIQLGkeegaRLVC 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 306 GGQ--TD---EKDKYIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLER 380
Cdd:cd07119 345 GGKrpTGdelAKGYFVEPTIFDDVDRTMRIVQEEIFGPVLTVERFDTEEEAIRLANDTPYGLAGAVWTKDIARANRVARR 424
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2119029253 381 TSSGGFCSNDciMQMTLFSLPFGGVGDSGMGMYHGRFSFDTFS 423
Cdd:cd07119 425 LRAGTVWIND--YHPYFAEAPWGGYKQSGIGRELGPTGLEEYQ 465
|
|
| ALDH_SSADH2_GabD2 |
cd07101 |
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde ... |
104-416 |
1.16e-47 |
|
Mycobacterium tuberculosis succinate-semialdehyde dehydrogenase 2-like; Succinate-semialdehyde dehydrogenase 2 (SSADH2) and similar proteins are in this CD. SSADH1 (GabD1, EC=1.2.1.16) catalyzes the NADP(+)-dependent oxidation of succinate semialdehyde to succinate. SSADH activity in Mycobacterium tuberculosis is encoded by both gabD1 (Rv0234c) and gabD2 (Rv1731), however ,the Vmax of GabD1 was shown to be much higher than that of GabD2, and GabD2 (SSADH2) is likely to serve physiologically as a dehydrogenase for a different aldehyde(s).
Pssm-ID: 143419 [Multi-domain] Cd Length: 454 Bit Score: 170.18 E-value: 1.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 104 PFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFAVVCGGVKETTELLEEKFD 182
Cdd:cd07101 118 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTALTALWAVELLIEAgLPRDLWQVVTGPGSEVGGAIVDNAD 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 183 YIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTKAVREELVP 262
Cdd:cd07101 198 YVMFTGSTATGRVVAERAGRRLIGCSLELGGKNPMIVLEDADLDKAAAGAVRACFSNAGQLCVSIERIYVHESVYDEFVR 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 263 ALINCLEEF-YGKNPQESEDLGRIINEKHFNRLK-----ALLSSGKVAVGGQT--DEKDKYIAPTVLVDVKETDPVMQEE 334
Cdd:cd07101 278 RFVARTRALrLGAALDYGPDMGSLISQAQLDRVTahvddAVAKGATVLAGGRArpDLGPYFYEPTVLTGVTEDMELFAEE 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 335 IFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDcIMQMTLFSL--PFGGVGDSGMGM 412
Cdd:cd07101 358 TFGPVVSIYRVADDDEAIELANDTDYGLNASVWTRDGARGRRIAARLRAGTVNVNE-GYAAAWASIdaPMGGMKDSGLGR 436
|
....
gi 2119029253 413 YHGR 416
Cdd:cd07101 437 RHGA 440
|
|
| ALDH_F11_NP-GAPDH |
cd07082 |
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family ... |
3-411 |
1.23e-47 |
|
NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase and ALDH family 11; NADP+-dependent non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase (NP-GAPDH, EC=1.2.1.9) catalyzes the irreversible oxidation of glyceraldehyde 3-phosphate to 3-phosphoglycerate generating NADPH for biosynthetic reactions. This CD also includes the Arabidopsis thaliana osmotic-stress-inducible ALDH family 11, ALDH11A3 and similar sequences. In autotrophic eukaryotes, NP-GAPDH generates NADPH for biosynthetic processes from photosynthetic glyceraldehyde-3-phosphate exported from the chloroplast and catalyzes one of the classic glycolytic bypass reactions unique to plants.
Pssm-ID: 143401 [Multi-domain] Cd Length: 473 Bit Score: 170.83 E-value: 1.23e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 3 STKEVAARLREAFNSGK----TRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESIiSEVLFTKNEIVCAINNL 78
Cdd:cd07082 36 SALEILEAAETAYDAGRgwwpTMPLEERIDCLHKFADLLKENKEEVANLLMWEIGKTLKDAL-KEVDRTIDYIRDTIEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 79 TEwMKPEYV--EKTLVTKLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPK 156
Cdd:cd07082 115 KR-LDGDSLpgDWFPGTKGKIAQVRREPLGVVLAIGPFNYPLNLTVSKLIPALIMGNTVVFKPATQGVLLGIPLAEAFHD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 157 Y-LDKDCFAVVCGGVKETTELLEE--KFDYIFFTGGTHVGKIIMTAAAKhlTPVSLELGGKNPCYVDKSCDINNTAHRIA 233
Cdd:cd07082 194 AgFPKGVVNVVTGRGREIGDPLVThgRIDVISFTGSTEVGNRLKKQHPM--KRLVLELGGKDPAIVLPDADLELAAKEIV 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 234 WARFLNMGQTCIAPDYVLCTKAVREELVPALINCLEEFYGKNPQESE-DLGRIINEKHFNRLKALL----SSGKVAVGGQ 308
Cdd:cd07082 272 KGALSYSGQRCTAIKRVLVHESVADELVELLKEEVAKLKVGMPWDNGvDITPLIDPKSADFVEGLIddavAKGATVLNGG 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 309 TDEKDKYIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTD-NKVVK--DVLE------ 379
Cdd:cd07082 352 GREGGNLIYPTLLDPVTPDMRLAWEEPFGPVLPIIRVNDIEEAIELANKSNYGLQASIFTKDiNKARKlaDALEvgtvni 431
|
410 420 430
....*....|....*....|....*....|....
gi 2119029253 380 --RTSSGgfcsNDcimqmtlfSLPFGGVGDSGMG 411
Cdd:cd07082 432 nsKCQRG----PD--------HFPFLGRKDSGIG 453
|
|
| PLN02467 |
PLN02467 |
betaine aldehyde dehydrogenase |
98-424 |
4.29e-47 |
|
betaine aldehyde dehydrogenase
Pssm-ID: 215260 [Multi-domain] Cd Length: 503 Bit Score: 169.91 E-value: 4.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 98 CFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFAVVCGGVKETTEL 176
Cdd:PLN02467 145 GYVLKEPLGVVGLITPWNYPLLMATWKVAPALAAGCTAVLKPSELASVTCLELADICREVgLPPGVLNVVTGLGTEAGAP 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 177 L--EEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTK 254
Cdd:PLN02467 225 LasHPGVDKIAFTGSTATGRKIMTAAAQMVKPVSLELGGKSPIIVFDDVDLDKAVEWAMFGCFWTNGQICSATSRLLVHE 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 255 AVREELVPALINCLEEFYGKNPQEsED--LGRIINEKHFNRLKALLSSGK-----VAVGG---QTDEKDKYIAPTVLVDV 324
Cdd:PLN02467 305 RIASEFLEKLVKWAKNIKISDPLE-EGcrLGPVVSEGQYEKVLKFISTAKsegatILCGGkrpEHLKKGFFIEPTIITDV 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 325 KETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGF---CSNDCIMQmtlfsLP 401
Cdd:PLN02467 384 TTSMQIWREEVFGPVLCVKTFSTEDEAIELANDSHYGLAGAVISNDLERCERVSEAFQAGIVwinCSQPCFCQ-----AP 458
|
330 340
....*....|....*....|...
gi 2119029253 402 FGGVGDSGMGMYHGRFSFDTFSH 424
Cdd:PLN02467 459 WGGIKRSGFGRELGEWGLENYLS 481
|
|
| ALDH_PutA-P5CDH-RocA |
cd07124 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate ... |
103-411 |
9.12e-47 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, RocA; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), RocA: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. The proline catabolic enzymes, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). In this CD, monofunctional enzyme sequences such as seen in the Bacillus subtilis RocA P5CDH are also present. These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis.
Pssm-ID: 143442 Cd Length: 512 Bit Score: 169.33 E-value: 9.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 103 EPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFAVVCGGVKETTELLEE-- 179
Cdd:cd07124 165 RPLGVGAVISPWNFPLAILAGMTTAALVTGNTVVLKPAEDTPVIAAKLVEILEEAgLPPGVVNFLPGPGEEVGDYLVEhp 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 180 KFDYIFFTGGTHVGKIIMTAAAK------HLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCT 253
Cdd:cd07124 245 DVRFIAFTGSREVGLRIYERAAKvqpgqkWLKRVIAEMGGKNAIIVDEDADLDEAAEGIVRSAFGFQGQKCSACSRVIVH 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 254 KAVREELVPALINCLEEFYGKNPQESE-DLGRIINEKHFNRLK----ALLSSGKVAVGGQTDEKDK---YIAPTVLVDVK 325
Cdd:cd07124 325 ESVYDEFLERLVERTKALKVGDPEDPEvYMGPVIDKGARDRIRryieIGKSEGRLLLGGEVLELAAegyFVQPTIFADVP 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 326 ETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCIMQMTLFSLPFGGV 405
Cdd:cd07124 405 PDHRLAQEEIFGPVLAVIKAKDFDEALEIANDTEYGLTGGVFSRSPEHLERARREFEVGNLYANRKITGALVGRQPFGGF 484
|
....*.
gi 2119029253 406 GDSGMG 411
Cdd:cd07124 485 KMSGTG 490
|
|
| PRK03137 |
PRK03137 |
1-pyrroline-5-carboxylate dehydrogenase; Provisional |
103-370 |
4.19e-46 |
|
1-pyrroline-5-carboxylate dehydrogenase; Provisional
Pssm-ID: 179543 Cd Length: 514 Bit Score: 167.42 E-value: 4.19e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 103 EPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFAVVCGGVKETTELLEE-- 179
Cdd:PRK03137 170 IPLGVGVVISPWNFPFAIMAGMTLAAIVAGNTVLLKPASDTPVIAAKFVEVLEEAgLPAGVVNFVPGSGSEVGDYLVDhp 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 180 KFDYIFFTGGTHVGKIIMTAAAK------HLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCT 253
Cdd:PRK03137 250 KTRFITFTGSREVGLRIYERAAKvqpgqiWLKRVIAEMGGKDAIVVDEDADLDLAAESIVASAFGFSGQKCSACSRAIVH 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 254 KAVREELVPALINCLEEFYGKNPQESEDLGRIINEKHFNRLKALL----SSGKVAVGGQTDEKDKY-IAPTVLVDVKETD 328
Cdd:PRK03137 330 EDVYDEVLEKVVELTKELTVGNPEDNAYMGPVINQASFDKIMSYIeigkEEGRLVLGGEGDDSKGYfIQPTIFADVDPKA 409
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2119029253 329 PVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTD 370
Cdd:PRK03137 410 RIMQEEIFGPVVAFIKAKDFDHALEIANNTEYGLTGAVISNN 451
|
|
| ALDH_KGSADH-YcbD |
cd07097 |
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; ... |
99-411 |
2.41e-45 |
|
Bacillus subtilis NADP+-dependent alpha-ketoglutaric semialdehyde dehydrogenase ycbD-like; Kinetic studies of the Bacillus subtilis ALDH-like ycbD protein, which is involved in d-glucarate/d-galactarate utilization, reveal that it is a NADP+-dependent, alpha-ketoglutaric semialdehyde dehydrogenase (KGSADH). KGSADHs (EC 1.2.1.26) catalyze the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. Interestingly, the NADP+-dependent, tetrameric, 2,5-dioxopentanoate dehydrogenase (EC=1.2.1.26), an enzyme involved in the catabolic pathway for D-arabinose in Sulfolobus solfataricus, also clusters in this group. This CD shows a distant phylogenetic relationship to the Azospirillum brasilense KGSADH-II (-III) group.
Pssm-ID: 143415 [Multi-domain] Cd Length: 473 Bit Score: 164.34 E-value: 2.41e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 99 FIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFAVVCG-GVKETTEL 176
Cdd:cd07097 130 ETTREPLGVVGLITPWNFPIAIPAWKIAPALAYGNTVVFKPAELTPASAWALVEILEEAgLPAGVFNLVMGsGSEVGQAL 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 177 LE-EKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTKA 255
Cdd:cd07097 210 VEhPDVDAVSFTGSTAVGRRIAAAAAARGARVQLEMGGKNPLVVLDDADLDLAVECAVQGAFFSTGQRCTASSRLIVTEG 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 256 VREELVPALINCLEEF-YGKNPQESEDLGRIINEKHFNRLKALLSSG-----KVAVGGQT-DEKDK--YIAPTVLVDVKE 326
Cdd:cd07097 290 IHDRFVEALVERTKALkVGDALDEGVDIGPVVSERQLEKDLRYIEIArsegaKLVYGGERlKRPDEgyYLAPALFAGVTN 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 327 TDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGgfcsndciMQM-------TLFS 399
Cdd:cd07097 370 DMRIAREEIFGPVAAVIRVRDYDEALAIANDTEFGLSAGIVTTSLKHATHFKRRVEAG--------VVMvnlptagVDYH 441
|
330
....*....|..
gi 2119029253 400 LPFGGVGDSGMG 411
Cdd:cd07097 442 VPFGGRKGSSYG 453
|
|
| ABALDH |
TIGR03374 |
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1. ... |
85-431 |
7.71e-45 |
|
1-pyrroline dehydrogenase; Members of this protein family are 1-pyrroline dehydrogenase (1.5.1.35), also called gamma-aminobutyraldehyde dehydrogenase. This enzyme can follow putrescine transaminase (EC 2.6.1.82) for a two-step conversion of putrescine to gamma-aminobutyric acid (GABA). The member from Escherichia coli is characterized as a homotetramer that binds one NADH per momomer. This enzyme belongs to the medium-chain aldehyde dehydrogenases, and is quite similar in sequence to the betaine aldehyde dehydrogenase (EC 1.2.1.8) family.
Pssm-ID: 132417 Cd Length: 472 Bit Score: 163.25 E-value: 7.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 85 EYVEKtlvtklDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKYLDKDCFA 164
Cdd:TIGR03374 124 EYLEG------HTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVVN 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 165 VVCGGVKETTELL--EEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQ 242
Cdd:TIGR03374 198 ILFGRGKTVGDPLtgHEKVRMVSLTGSIATGEHILSHTAPSIKRTHMELGGKAPVIVFDDADIDAVVEGVRTFGFYNAGQ 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 243 TCIAPDYVLCTKAVREELVPALINCLEEFYGKNPQ-ESEDLGRIINEKHFNRLKALLSSGK------VAVGG-QTDEKDK 314
Cdd:TIGR03374 278 DCTAACRIYAQRGIYDTLVEKLGAAVATLKSGAPDdESTELGPLSSLAHLERVMKAVEEAKalghikVITGGeKRKGNGY 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 315 YIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCIMQ 394
Cdd:TIGR03374 358 YFAPTLLAGAKQDDAIVQKEVFGPVVSITSFDDEEQVVNWANDSQYGLASSVWTKDVGRAHRLSARLQYGCTWVNTHFML 437
|
330 340 350
....*....|....*....|....*....|....*..
gi 2119029253 395 MTlfSLPFGGVGDSGMGMYHGRFSFDTFSHKRACMLR 431
Cdd:TIGR03374 438 VS--EMPHGGQKLSGYGKDMSLYGLEDYTVVRHIMVK 472
|
|
| ALDH_HBenzADH |
cd07151 |
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, ... |
100-423 |
1.44e-44 |
|
NADP+-dependent p-hydroxybenzaldehyde dehydrogenase-like; NADP+-dependent, p-hydroxybenzaldehyde dehydrogenase (PchA, HBenzADH) which catalyzes oxidation of p-hydroxybenzaldehyde to p-hydroxybenzoic acid and other related sequences are included in this CD.
Pssm-ID: 143469 [Multi-domain] Cd Length: 465 Bit Score: 162.09 E-value: 1.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 100 IKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLL-SEL-----LPKYLdkdcFAVVCGGVKET 173
Cdd:cd07151 126 VYREPLGVVGVISPWNFPLHLSMRSVAPALALGNAVVLKPASDTPITGGLLlAKIfeeagLPKGV----LNVVVGAGSEI 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 174 TELLEEKF--DYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVL 251
Cdd:cd07151 202 GDAFVEHPvpRLISFTGSTPVGRHIGELAGRHLKKVALELGGNNPFVVLEDADIDAAVNAAVFGKFLHQGQICMAINRII 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 252 CTKAVREELVPALINCLEEFYGKNPQESEDL-GRIINEKHFNRLKALLSSGK-----VAVGGQTDekDKYIAPTVLVDVK 325
Cdd:cd07151 282 VHEDVYDEFVEKFVERVKALPYGDPSDPDTVvGPLINESQVDGLLDKIEQAVeegatLLVGGEAE--GNVLEPTVLSDVT 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 326 ETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCIMQMTLFsLPFGGV 405
Cdd:cd07151 360 NDMEIAREEIFGPVAPIIKADDEEEALELANDTEYGLSGAVFTSDLERGVQFARRIDAGMTHINDQPVNDEPH-VPFGGE 438
|
330
....*....|....*...
gi 2119029253 406 GDSGMGMYHGRFSFDTFS 423
Cdd:cd07151 439 KNSGLGRFNGEWALEEFT 456
|
|
| ALDH_AldA_AN0554 |
cd07143 |
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde ... |
99-431 |
2.04e-44 |
|
Aspergillus nidulans aldehyde dehydrogenase, AldA (AN0554)-like; NAD(P)+-dependent aldehyde dehydrogenase (AldA) of Aspergillus nidulans (locus AN0554), and other similar sequences, are present in this CD.
Pssm-ID: 143461 Cd Length: 481 Bit Score: 162.31 E-value: 2.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 99 FIKKEPFGVALIIGPWNYPIqLVLTPFIG-AVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFAVVCGGVKETTEL 176
Cdd:cd07143 139 YTRHEPIGVCGQIIPWNFPL-LMCAWKIApALAAGNTIVLKPSELTPLSALYMTKLIPEAgFPPGVINVVSGYGRTCGNA 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 177 LEE--KFDYIFFTGGTHVGKIIMTAAAK-HLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCT 253
Cdd:cd07143 218 ISShmDIDKVAFTGSTLVGRKVMEAAAKsNLKKVTLELGGKSPNIVFDDADLESAVVWTAYGIFFNHGQVCCAGSRIYVQ 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 254 KAVREELVPALINCLEEFYGKNP-QESEDLGRIINEKHFNRLKALLSSGK-----VAVGGQTDEKDKY-IAPTVLVDVKE 326
Cdd:cd07143 298 EGIYDKFVKRFKEKAKKLKVGDPfAEDTFQGPQVSQIQYERIMSYIESGKaegatVETGGKRHGNEGYfIEPTIFTDVTE 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 327 TDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTD-NKVVK--DVLERTSSGGFCSNdcimqMTLFSLPFG 403
Cdd:cd07143 378 DMKIVKEEIFGPVVAVIKFKTEEEAIKRANDSTYGLAAAVFTNNiNNAIRvaNALKAGTVWVNCYN-----LLHHQVPFG 452
|
330 340
....*....|....*....|....*...
gi 2119029253 404 GVGDSGMGMYHGRFSFDTFSHKRACMLR 431
Cdd:cd07143 453 GYKQSGIGRELGEYALENYTQIKAVHIN 480
|
|
| ALDH_PADH_NahF |
cd07113 |
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, ... |
97-431 |
1.53e-43 |
|
Escherichia coli NAD+-dependent phenylacetaldehyde dehydrogenase PadA-like; NAD+-dependent, homodimeric, phenylacetaldehyde dehydrogenase (PADH, EC=1.2.1.39) PadA of Escherichia coli involved in the catabolism of 2-phenylethylamine, and other related sequences, are present in this CD. Also included is the Pseudomonas fluorescens ST StyD PADH involved in styrene catabolism, the Sphingomonas sp. LB126 FldD protein involved in fluorene degradation, and the Novosphingobium aromaticivorans NahF salicylaldehyde dehydrogenase involved in the NAD+-dependent conversion of salicylaldehyde to salicylate.
Pssm-ID: 143431 Cd Length: 477 Bit Score: 159.53 E-value: 1.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 97 TCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFAVVCGGVKETTE 175
Cdd:cd07113 135 TAFTRREPVGVVAGIVPWNFSVMIAVWKIGAALATGCTIVIKPSEFTPLTLLRVAELAKEAgIPDGVLNVVNGKGAVGAQ 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 176 LLEE-KFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTK 254
Cdd:cd07113 215 LISHpDVAKVSFTGSVATGKKIGRQAASDLTRVTLELGGKNAAAFLKDADIDWVVEGLLTAGFLHQGQVCAAPERFYVHR 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 255 AVREELVPALINCLEEFYGKNP-QESEDLGRIINEKHFNRLKALL-----SSGKVAVGGQT-DEKDKYIAPTVLVDVKET 327
Cdd:cd07113 295 SKFDELVTKLKQALSSFQVGSPmDESVMFGPLANQPHFDKVCSYLddaraEGDEIVRGGEAlAGEGYFVQPTLVLARSAD 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 328 DPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNdcimqMTLF---SLPFGG 404
Cdd:cd07113 375 SRLMREETFGPVVSFVPYEDEEELIQLINDTPFGLTASVWTNNLSKALRYIPRIEAGTVWVN-----MHTFldpAVPFGG 449
|
330 340
....*....|....*....|....*..
gi 2119029253 405 VGDSGMGMYHGRFSFDTFSHKRACMLR 431
Cdd:cd07113 450 MKQSGIGREFGSAFIDDYTELKSVMIR 476
|
|
| ALDH_F2BC |
cd07142 |
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the ... |
12-427 |
3.51e-43 |
|
Arabidosis aldehyde dehydrogenase family 2 B4, B7, C4-like; Included in this CD is the Arabidosis aldehyde dehydrogenase family 2 members B4 and B7 (EC=1.2.1.3), which are mitochondrial homotetramers that oxidize acetaldehyde and glycolaldehyde, but not L-lactaldehyde. Also in this group, is the Arabidosis cytosolic, homotetramer ALDH2C4 (EC=1.2.1.3), an enzyme involved in the oxidation of sinapalehyde and coniferaldehyde.
Pssm-ID: 143460 Cd Length: 476 Bit Score: 158.81 E-value: 3.51e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 12 REAFNSGK--TRTAEFRLKQLKAMLNLMKEN--EGALLEALkkDLRKPNFESIISEV-----LFTKNE-IVCAINNLTEW 81
Cdd:cd07142 51 RKAFDEGPwpRMTGYERSRILLRFADLLEKHadELAALETW--DNGKPYEQARYAEVplaarLFRYYAgWADKIHGMTLP 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 82 MKPEYVEKTLvtkldtcfikKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDK 160
Cdd:cd07142 129 ADGPHHVYTL----------HEPIGVVGQIIPWNFPLLMFAWKVGPALACGNTIVLKPAEQTPLSALLAAKLAAEAgLPD 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 161 DCFAVVCG-GVKETTELLEEK-FDYIFFTGGTHVGKIIMTAAAK-HLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARF 237
Cdd:cd07142 199 GVLNIVTGfGPTAGAAIASHMdVDKVAFTGSTEVGKIIMQLAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALF 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 238 LNMGQTCIAPDYVLCTKAVREELVP-ALINCLEEFYGKNPQESEDLGRIINEKHFNRLKALLSSGK------VAVGGQTD 310
Cdd:cd07142 279 FNQGQCCCAGSRTFVHESIYDEFVEkAKARALKRVVGDPFRKGVEQGPQVDKEQFEKILSYIEHGKeegatlITGGDRIG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 311 EKDKYIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVkDVLERTSSGGFCSND 390
Cdd:cd07142 359 SKGYYIQPTIFSDVKDDMKIARDEIFGPVQSILKFKTVDEVIKRANNSKYGLAAGVFSKNIDTA-NTLSRALKAGTVWVN 437
|
410 420 430
....*....|....*....|....*....|....*..
gi 2119029253 391 CIMQMTLfSLPFGGVGDSGMGMYHGRFSFDTFSHKRA 427
Cdd:cd07142 438 CYDVFDA-SIPFGGYKMSGIGREKGIYALNNYLQVKA 473
|
|
| gabD2 |
PRK09407 |
succinic semialdehyde dehydrogenase; Reviewed |
104-415 |
8.04e-43 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 236501 [Multi-domain] Cd Length: 524 Bit Score: 158.50 E-value: 8.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 104 PFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLpkY---LDKDCFAVVCGGVKETTELLEEK 180
Cdd:PRK09407 154 PKGVVGVISPWNYPLTLAVSDAIPALLAGNAVVLKPDSQTPLTALAAVELL--YeagLPRDLWQVVTGPGPVVGTALVDN 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 181 FDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTKAVREEL 260
Cdd:PRK09407 232 ADYLMFTGSTATGRVLAEQAGRRLIGFSLELGGKNPMIVLDDADLDKAAAGAVRACFSNAGQLCISIERIYVHESIYDEF 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 261 VPALINCLEEF-YGKNPQESEDLGRIINEKHFNRLKA----LLSSG-KVAVGGQT--DEKDKYIAPTVLVDVKETDPVMQ 332
Cdd:PRK09407 312 VRAFVAAVRAMrLGAGYDYSADMGSLISEAQLETVSAhvddAVAKGaTVLAGGKArpDLGPLFYEPTVLTGVTPDMELAR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 333 EEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCIMQmTLFSL--PFGGVGDSGM 410
Cdd:PRK09407 392 EETFGPVVSVYPVADVDEAVERANDTPYGLNASVWTGDTARGRAIAARIRAGTVNVNEGYAA-AWGSVdaPMGGMKDSGL 470
|
....*
gi 2119029253 411 GMYHG 415
Cdd:PRK09407 471 GRRHG 475
|
|
| ALDH_ACDHII_AcoD-like |
cd07559 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus ... |
102-411 |
1.81e-42 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II and Staphylococcus aureus AldA1 (SACOL0154)-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane, as well as, the uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences.
Pssm-ID: 143471 [Multi-domain] Cd Length: 480 Bit Score: 156.74 E-value: 1.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 102 KEPFGVALIIGPWNYPIQLV---LTPfigAVAAGNCAILKPSEVSPNSSQLLSELLPKYLDKDCFAVVCG-GVKETTELL 177
Cdd:cd07559 134 HEPLGVVGQIIPWNFPLLMAawkLAP---ALAAGNTVVLKPASQTPLSILVLMELIGDLLPKGVVNVVTGfGSEAGKPLA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 178 EEK-FDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYV-----DKSCDINNTAHRIAWARFLNMGQTCIAPDYVL 251
Cdd:cd07559 211 SHPrIAKLAFTGSTTVGRLIMQYAAENLIPVTLELGGKSPNIFfddamDADDDFDDKAEEGQLGFAFNQGEVCTCPSRAL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 252 CTKAVREELVPALINCLEEFYGKNPQESED-LGRIINEKHFNRLKALLSSGK-----VAVGGQ-----TDEKDKYIAPTV 320
Cdd:cd07559 291 VQESIYDEFIERAVERFEAIKVGNPLDPETmMGAQVSKDQLEKILSYVDIGKeegaeVLTGGErltlgGLDKGYFYEPTL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 321 LVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTD-NKVVKdvLERTSSGGFCSNDCIMQMTLFS 399
Cdd:cd07559 371 IKGGNNDMRIFQEEIFGPVLAVITFKDEEEAIAIANDTEYGLGGGVWTRDiNRALR--VARGIQTGRVWVNCYHQYPAHA 448
|
330
....*....|..
gi 2119029253 400 lPFGGVGDSGMG 411
Cdd:cd07559 449 -PFGGYKKSGIG 459
|
|
| ALDH_F7_AASADH-like |
cd07086 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH ... |
104-428 |
2.13e-42 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase and related proteins; ALDH subfamily which includes the NAD+-dependent, alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as Antiquitin-1, ALDH7A1, ALDH7B or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), and other similar sequences, such as the uncharacterized aldehyde dehydrogenase of Candidatus kuenenia AldH (locus CAJ73105).
Pssm-ID: 143405 [Multi-domain] Cd Length: 478 Bit Score: 156.57 E-value: 2.13e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 104 PFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKYLDKD-----CFAVVCGGvKETTELLE 178
Cdd:cd07086 133 PLGVVGVITAFNFPVAVPGWNAAIALVCGNTVVWKPSETTPLTAIAVTKILAEVLEKNglppgVVNLVTGG-GDGGELLV 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 179 --EKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTKAV 256
Cdd:cd07086 212 hdPRVPLVSFTGSTEVGRRVGETVARRFGRVLLELGGNNAIIVMDDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESV 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 257 REELVPALINCLEEFYGKNPQESE-DLGRIINEKHFNR-LKAL----LSSGKVAVGGQT---DEKDKYIAPTVLVDVKET 327
Cdd:cd07086 292 YDEFLERLVKAYKQVRIGDPLDEGtLVGPLINQAAVEKyLNAIeiakSQGGTVLTGGKRidgGEPGNYVEPTIVTGVTDD 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 328 DPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSggfcsnDC-IMQMTLFS------L 400
Cdd:cd07086 372 ARIVQEETFAPILYVIKFDSLEEAIAINNDVPQGLSSSIFTEDLREAFRWLGPKGS------DCgIVNVNIPTsgaeigG 445
|
330 340
....*....|....*....|....*...
gi 2119029253 401 PFGGVGDSGMGMYHGRFSFDTFSHKRAC 428
Cdd:cd07086 446 AFGGEKETGGGRESGSDAWKQYMRRSTC 473
|
|
| D1pyr5carbox2 |
TIGR01237 |
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of ... |
104-411 |
4.02e-42 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase, group 2, putative; This enzyme is the second of two in the degradation of proline to glutamate. This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch may be associated with proline dehydrogenase (the other enzyme of the pathway from proline to glutamate) but have not been demonstrated experimentally. The branches are not as closely related to each other as some distinct aldehyde dehydrogenases are to some; separate models were built to let each model describe a set of equivalogs. [Energy metabolism, Amino acids and amines]
Pssm-ID: 200087 [Multi-domain] Cd Length: 511 Bit Score: 156.56 E-value: 4.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 104 PFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFAVVCGGVKETTELL--EEK 180
Cdd:TIGR01237 167 PTGVTVVISPWNFPFAIMVGMTVAPIVTGNCVVLKPAEAAPVIAAKFVEILEEAgLPKGVVQFVPGSGSEVGDYLvdHPK 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 181 FDYIFFTGGTHVGKIIMTAAAK------HLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTK 254
Cdd:TIGR01237 247 TSLITFTGSREVGTRIFERAAKvqpgqkHLKRVIAEMGGKDTVIVDEDADIELAAQSAFTSAFGFAGQKCSAGSRAVVHE 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 255 AVREELVPALINCLEEF-YGKNPQESEDLGRIINEKHFNRLKALL----SSGKVAVGGQTDEKDKY-IAPTVLVDVKETD 328
Cdd:TIGR01237 327 KVYDEVVERFVEITESLkVGPPDSADVYVGPVIDQKSFNKIMEYIeigkAEGRLVSGGCGDDSKGYfIGPTIFADVDRKA 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 329 PVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCIMQMTLFSLPFGGVGDS 408
Cdd:TIGR01237 407 RLAQEEIFGPVVAFIRASDFDEALEIANNTEYGLTGGVISNNRDHINRAKAEFEVGNLYFNRNITGAIVGYQPFGGFKMS 486
|
...
gi 2119029253 409 GMG 411
Cdd:TIGR01237 487 GTD 489
|
|
| ALDH_StaphAldA1 |
cd07117 |
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; ... |
12-411 |
6.05e-42 |
|
Uncharacterized Staphylococcus aureus AldA1 (SACOL0154) aldehyde dehydrogenase-like; Uncharacterized aldehyde dehydrogenase from Staphylococcus aureus (AldA1, locus SACOL0154) and other similar sequences are present in this CD.
Pssm-ID: 143435 Cd Length: 475 Bit Score: 155.31 E-value: 6.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 12 REAFNSGKTRTAEFRLKQLKAMLNLMKENEG--ALLEALkkDLRKPNFESiisevlfTKNEIVCAINNLTEWMKPEYVEK 89
Cdd:cd07117 48 QEAFKTWRKTTVAERANILNKIADIIDENKEllAMVETL--DNGKPIRET-------RAVDIPLAADHFRYFAGVIRAEE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 90 TLVTKLDTCF---IKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKYLDKDCFAVV 166
Cdd:cd07117 119 GSANMIDEDTlsiVLREPIGVVGQIIPWNFPFLMAAWKLAPALAAGNTVVIKPSSTTSLSLLELAKIIQDVLPKGVVNIV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 167 CG-GVKETTELLEEK-FDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTC 244
Cdd:cd07117 199 TGkGSKSGEYLLNHPgLDKLAFTGSTEVGRDVAIAAAKKLIPATLELGGKSANIIFDDANWDKALEGAQLGILFNQGQVC 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 245 IAPDYVLCTKAVREELVPALINCLEEFYGKNPQESE-DLGRIINEKHFNRLK-----ALLSSGKVAVGGQ---TDEKDK- 314
Cdd:cd07117 279 CAGSRIFVQEGIYDEFVAKLKEKFENVKVGNPLDPDtQMGAQVNKDQLDKILsyvdiAKEEGAKILTGGHrltENGLDKg 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 315 -YIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTD-NKVVKdvLERTSSGGFCSNDCI 392
Cdd:cd07117 359 fFIEPTLIVNVTNDMRVAQEEIFGPVATVIKFKTEDEVIDMANDSEYGLGGGVFTKDiNRALR--VARAVETGRVWVNTY 436
|
410
....*....|....*....
gi 2119029253 393 MQMTLFSlPFGGVGDSGMG 411
Cdd:cd07117 437 NQIPAGA-PFGGYKKSGIG 454
|
|
| ALDH_F1AB_F2_RALDH1 |
cd07141 |
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent ... |
98-423 |
1.18e-41 |
|
NAD+-dependent retinal dehydrogenase 1, ALDH families 1A, 1B, and 2-like; NAD+-dependent retinal dehydrogenase 1 (RALDH 1, ALDH1, EC=1.2.1.36) also known as aldehyde dehydrogenase family 1 member A1 (ALDH1A1) in humans, is a homotetrameric, cytosolic enzyme that catalyzes the oxidation of retinaldehyde to retinoic acid. Human ALDH1B1 and ALDH2 are also in this cluster; both are mitochrondrial homotetramers which play important roles in acetaldehyde oxidation; ALDH1B1 in response to UV light exposure and ALDH2 during ethanol metabolism.
Pssm-ID: 143459 Cd Length: 481 Bit Score: 154.43 E-value: 1.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 98 CFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSEL-------------LPKYldkdcfA 164
Cdd:cd07141 139 TYTRHEPVGVCGQIIPWNFPLLMAAWKLAPALACGNTVVLKPAEQTPLTALYLASLikeagfppgvvnvVPGY------G 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 165 VVCGGVKETtellEEKFDYIFFTGGTHVGKIIMTAAAK-HLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQT 243
Cdd:cd07141 213 PTAGAAISS----HPDIDKVAFTGSTEVGKLIQQAAGKsNLKRVTLELGGKSPNIVFADADLDYAVEQAHEALFFNMGQC 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 244 CIAPDYVLCTKAVREELVPALINCLEEFYGKNPQESE-DLGRIINEKHFNRLKALLSSGK------VAVGGQTDEKDKYI 316
Cdd:cd07141 289 CCAGSRTFVQESIYDEFVKRSVERAKKRVVGNPFDPKtEQGPQIDEEQFKKILELIESGKkegaklECGGKRHGDKGYFI 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 317 APTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNdcIMQMT 396
Cdd:cd07141 369 QPTVFSDVTDDMRIAKEEIFGPVQQIFKFKTIDEVIERANNTTYGLAAAVFTKDIDKAITFSNALRAGTVWVN--CYNVV 446
|
330 340
....*....|....*....|....*..
gi 2119029253 397 LFSLPFGGVGDSGMGMYHGRFSFDTFS 423
Cdd:cd07141 447 SPQAPFGGYKMSGNGRELGEYGLQEYT 473
|
|
| ALDH_PsfA-ACA09737 |
cd07120 |
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the ... |
100-423 |
4.31e-41 |
|
Pseudomonas putida aldehyde dehydrogenase PsfA (ACA09737)-like; Included in this CD is the aldehyde dehydrogenase (PsfA, locus ACA09737) of Pseudomonas putida involved in furoic acid metabolism. Transcription of psfA was induced in response to 2-furoic acid, furfuryl alcohol, and furfural.
Pssm-ID: 143438 [Multi-domain] Cd Length: 455 Bit Score: 152.50 E-value: 4.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 100 IKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSP--NS--SQLLSELlpKYLDKDCFAVVCGGVKETTE 175
Cdd:cd07120 113 VLREPMGVAGIIVPWNSPVVLLVRSLAPALAAGCTVVVKPAGQTAqiNAaiIRILAEI--PSLPAGVVNLFTESGSEGAA 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 176 LLEE--KFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCT 253
Cdd:cd07120 191 HLVAspDVDVISFTGSTATGRAIMAAAAPTLKRLGLELGGKTPCIVFDDADLDAALPKLERALTIFAGQFCMAGSRVLVQ 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 254 KAVREELVPALINCLEEF-YGKNPQESEDLGRIINEKHFNRL-----KALLSSGKVAV-GGQTDE---KDKYIAPTvLVD 323
Cdd:cd07120 271 RSIADEVRDRLAARLAAVkVGPGLDPASDMGPLIDRANVDRVdrmveRAIAAGAEVVLrGGPVTEglaKGAFLRPT-LLE 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 324 VKETD-PVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDcimQMTLFS-LP 401
Cdd:cd07120 350 VDDPDaDIVQEEIFGPVLTLETFDDEAEAVALANDTDYGLAASVWTRDLARAMRVARAIRAGTVWIND---WNKLFAeAE 426
|
330 340
....*....|....*....|..
gi 2119029253 402 FGGVGDSGMGMYHGRFSFDTFS 423
Cdd:cd07120 427 EGGYRQSGLGRLHGVAALEDFI 448
|
|
| gabD |
PRK11241 |
NADP-dependent succinate-semialdehyde dehydrogenase I; |
8-411 |
1.13e-40 |
|
NADP-dependent succinate-semialdehyde dehydrogenase I;
Pssm-ID: 183050 [Multi-domain] Cd Length: 482 Bit Score: 151.98 E-value: 1.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 8 AARLREAFNSG-------KTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESiisevlftKNEIVCAINnLTE 80
Cdd:PRK11241 47 ADETRAAIDAAnralpawRALTAKERANILRRWFNLMMEHQDDLARLMTLEQGKPLAEA--------KGEISYAAS-FIE 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 81 WMKPE----YVEKTLVTKLDTCFIK-KEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLP 155
Cdd:PRK11241 118 WFAEEgkriYGDTIPGHQADKRLIViKQPIGVTAAITPWNFPAAMITRKAGPALAAGCTMVLKPASQTPFSALALAELAI 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 156 KY-LDKDCFAVVCGGVKE-----TTELLEEKFDyifFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTA 229
Cdd:PRK11241 198 RAgIPAGVFNVVTGSAGAvggelTSNPLVRKLS---FTGSTEIGRQLMEQCAKDIKKVSLELGGNAPFIVFDDADLDKAV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 230 HRIAWARFLNMGQTCIAPDYVLCTKAVREELVPALINCLEEFY-GKNPQESEDLGRIINEKHFNRLK-----ALLSSGKV 303
Cdd:PRK11241 275 EGALASKFRNAGQTCVCANRLYVQDGVYDRFAEKLQQAVSKLHiGDGLEKGVTIGPLIDEKAVAKVEehiadALEKGARV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 304 AVGGQTDEKD-KYIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTS 382
Cdd:PRK11241 355 VCGGKAHELGgNFFQPTILVDVPANAKVAKEETFGPLAPLFRFKDEADVIAQANDTEFGLAAYFYARDLSRVFRVGEALE 434
|
410 420 430
....*....|....*....|....*....|....*
gi 2119029253 383 SG------GFCSNDCImqmtlfslPFGGVGDSGMG 411
Cdd:PRK11241 435 YGivgintGIISNEVA--------PFGGIKASGLG 461
|
|
| ALDH_F21_RNP123 |
cd07147 |
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) ... |
98-411 |
1.79e-40 |
|
Aldehyde dehydrogenase family 21A1-like; Aldehyde dehydrogenase ALDH21A1 (gene name RNP123) was first described in the moss Tortula ruralis and is believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and ALDH21A1 expression represents a unique stress tolerance mechanism. So far, of plants, only the bryophyte sequence has been observed, but similar protein sequences from bacteria and archaea are also present in this CD.
Pssm-ID: 143465 [Multi-domain] Cd Length: 452 Bit Score: 150.86 E-value: 1.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 98 CFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFAVV-CGgvKETTE 175
Cdd:cd07147 117 GLVRRFPIGPVSAITPFNFPLNLVAHKVAPAIAAGCPFVLKPASRTPLSALILGEVLAETgLPKGAFSVLpCS--RDDAD 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 176 LL--EEKFDYIFFTGGTHVGKIIMTAAAKHltPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCT 253
Cdd:cd07147 195 LLvtDERIKLLSFTGSPAVGWDLKARAGKK--KVVLELGGNAAVIVDSDADLDFAAQRIIFGAFYQAGQSCISVQRVLVH 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 254 KAVREELVPALINCLEEFYGKNP-QESEDLGRIINEKHFNRLKALLSS-----GKVAVGGQTDEKdkYIAPTVLVDVKET 327
Cdd:cd07147 273 RSVYDEFKSRLVARVKALKTGDPkDDATDVGPMISESEAERVEGWVNEavdagAKLLTGGKRDGA--LLEPTILEDVPPD 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 328 DPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTD-NKVVK--DVLErtsSGGFCSNDcIMQMTLFSLPFGG 404
Cdd:cd07147 351 MEVNCEEVFGPVVTVEPYDDFDEALAAVNDSKFGLQAGVFTRDlEKALRawDELE---VGGVVIND-VPTFRVDHMPYGG 426
|
....*..
gi 2119029253 405 VGDSGMG 411
Cdd:cd07147 427 VKDSGIG 433
|
|
| ALDH_PhdK-like |
cd07107 |
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain ... |
9-415 |
7.55e-40 |
|
Nocardioides 2-carboxybenzaldehyde dehydrogenase, PhdK-like; Nocardioides sp. strain KP72-carboxybenzaldehyde dehydrogenase (PhdK), an enzyme involved in phenanthrene degradation, and other similar sequences, are present in this CD.
Pssm-ID: 143425 [Multi-domain] Cd Length: 456 Bit Score: 149.06 E-value: 7.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 9 ARLREAFNSGKTRTAEFRLKQLKAMLNLMKEN--EGALLEALkkDLRKPnfesiISEVLFTKNEIVCAIN---NLTEWMK 83
Cdd:cd07107 26 AAARAAFPEWRATTPLERARMLRELATRLREHaeELALIDAL--DCGNP-----VSAMLGDVMVAAALLDyfaGLVTELK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 84 PEYVEktlVTKLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKYLDKDCF 163
Cdd:cd07107 99 GETIP---VGGRNLHYTLREPYGVVARIVAFNHPLMFAAAKIAAPLAAGNTVVVKPPEQAPLSALRLAELAREVLPPGVF 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 164 AVVCGGVKETTELLEEKFDY--IFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHriAWARFLNM- 240
Cdd:cd07107 176 NILPGDGATAGAALVRHPDVkrIALIGSVPTGRAIMRAAAEGIKHVTLELGGKNALIVFPDADPEAAAD--AAVAGMNFt 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 241 --GQTCIAPDYVLCTKAVREELVPALINCLEEFYGKNP-QESEDLGRIINEKHFNRLKALLSSGK------VAVGGQTD- 310
Cdd:cd07107 254 wcGQSCGSTSRLFVHESIYDEVLARVVERVAAIKVGDPtDPATTMGPLVSRQQYDRVMHYIDSAKregarlVTGGGRPEg 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 311 ---EKDKYIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFC 387
Cdd:cd07107 334 palEGGFYVEPTVFADVTPGMRIAREEIFGPVLSVLRWRDEAEMVAQANGVEYGLTAAIWTNDISQAHRTARRVEAGYVW 413
|
410 420
....*....|....*....|....*...
gi 2119029253 388 SNDciMQMTLFSLPFGGVGDSGMGMYHG 415
Cdd:cd07107 414 ING--SSRHFLGAPFGGVKNSGIGREEC 439
|
|
| ALDH_F1L_FTFDH |
cd07140 |
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate ... |
98-411 |
4.83e-39 |
|
10-formyltetrahydrofolate dehydrogenase, ALDH family 1L; 10-formyltetrahydrofolate dehydrogenase (FTHFDH, EC=1.5.1.6), also known as aldehyde dehydrogenase family 1 member L1 (ALDH1L1) in humans, is a multi-domain homotetramer with an N-terminal formyl transferase domain and a C-terminal ALDH domain. FTHFDH catalyzes an NADP+-dependent dehydrogenase reaction resulting in the conversion of 10-formyltetrahydrofolate to tetrahydrofolate and CO2. The ALDH domain is also capable of the oxidation of short chain aldehydes to their corresponding acids.
Pssm-ID: 143458 [Multi-domain] Cd Length: 486 Bit Score: 147.64 E-value: 4.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 98 CFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFAVVCGGVKETTEL 176
Cdd:cd07140 141 TLTKREPIGVCGIVIPWNYPLMMLAWKMAACLAAGNTVVLKPAQVTPLTALKFAELTVKAgFPKGVINILPGSGSLVGQR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 177 LEEKFDY--IFFTGGTHVGKIIMTAAAK-HLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCT 253
Cdd:cd07140 221 LSDHPDVrkLGFTGSTPIGKHIMKSCAVsNLKKVSLELGGKSPLIIFADCDMDKAVRMGMSSVFFNKGENCIAAGRLFVE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 254 KAVREELVPALINCLEEFYGKNPQE-SEDLGRIINEKHFNRL-----KALLSSGKVAVGG-QTDEKDKYIAPTVLVDVKE 326
Cdd:cd07140 301 ESIHDEFVRRVVEEVKKMKIGDPLDrSTDHGPQNHKAHLDKLveyceRGVKEGATLVYGGkQVDRPGFFFEPTVFTDVED 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 327 TDPVMQEEIFGPILPIVDVEN--IDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNdcIMQMTLFSLPFGG 404
Cdd:cd07140 381 HMFIAKEESFGPIMIISKFDDgdVDGVLQRANDTEYGLASGVFTKDINKALYVSDKLEAGTVFVN--TYNKTDVAAPFGG 458
|
....*..
gi 2119029253 405 VGDSGMG 411
Cdd:cd07140 459 FKQSGFG 465
|
|
| PLN02766 |
PLN02766 |
coniferyl-aldehyde dehydrogenase |
102-427 |
9.15e-38 |
|
coniferyl-aldehyde dehydrogenase
Pssm-ID: 215410 [Multi-domain] Cd Length: 501 Bit Score: 144.19 E-value: 9.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 102 KEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPnssqlLSELLPKYLDKDC------FAVVCG-----GV 170
Cdd:PLN02766 156 KEPIGVVGHIIPWNFPSTMFFMKVAPALAAGCTMVVKPAEQTP-----LSALFYAHLAKLAgvpdgvINVVTGfgptaGA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 171 KETTELleeKFDYIFFTGGTHVGKIIMTAAAK-HLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDY 249
Cdd:PLN02766 231 AIASHM---DVDKVSFTGSTEVGRKIMQAAATsNLKQVSLELGGKSPLLIFDDADVDMAVDLALLGIFYNKGEICVASSR 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 250 VLCTKAVREELVPALINCLEEFYGKNPQESE-DLGRIINEKHFNRLKALLSSGK-----VAVGGQ-TDEKDKYIAPTVLV 322
Cdd:PLN02766 308 VYVQEGIYDEFVKKLVEKAKDWVVGDPFDPRaRQGPQVDKQQFEKILSYIEHGKregatLLTGGKpCGDKGYYIEPTIFT 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 323 DVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVlERTSSGGFCSNDCIMQMTLfSLPF 402
Cdd:PLN02766 388 DVTEDMKIAQDEIFGPVMSLMKFKTVEEAIKKANNTKYGLAAGIVTKDLDVANTV-SRSIRAGTIWVNCYFAFDP-DCPF 465
|
330 340
....*....|....*....|....*
gi 2119029253 403 GGVGDSGMGMYHGRFSFDTFSHKRA 427
Cdd:PLN02766 466 GGYKMSGFGRDQGMDALDKYLQVKS 490
|
|
| ALDH_SGSD_AstD |
cd07095 |
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate ... |
12-409 |
4.34e-37 |
|
N-succinylglutamate 5-semialdehyde dehydrogenase, AstD-like; N-succinylglutamate 5-semialdehyde dehydrogenase or succinylglutamic semialdehyde dehydrogenase (SGSD, E. coli AstD, EC=1.2.1.71) involved in L-arginine degradation via the arginine succinyltransferase (AST) pathway and catalyzes the NAD+-dependent reduction of succinylglutamate semialdehyde into succinylglutamate.
Pssm-ID: 143414 [Multi-domain] Cd Length: 431 Bit Score: 140.87 E-value: 4.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 12 REAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESIiSEVLFTKNEIVCAINnltewmkpEYVEKTL 91
Cdd:cd07095 10 RAAFPGWAALSLEERAAILRRFAELLKANKEELARLISRETGKPLWEAQ-TEVAAMAGKIDISIK--------AYHERTG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 92 VTKLDTCFIK----KEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELL-PKYLDKDCFAVV 166
Cdd:cd07095 81 ERATPMAQGRavlrHRPHGVMAVFGPFNFPGHLPNGHIVPALLAGNTVVFKPSELTPAVAELMVELWeEAGLPPGVLNLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 167 CGGvKETTELL--EEKFDYIFFTGGTHVGKIIMTAAAKHltP---VSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMG 241
Cdd:cd07095 161 QGG-RETGEALaaHEGIDGLLFTGSAATGLLLHRQFAGR--PgkiLALEMGGNNPLVVWDVADIDAAAYLIVQSAFLTAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 242 QTC------IAPDyvlctKAVREELVPALINCLEEFYGKNPQESED-LGRIINEKHFNRLkALLSSGKVAVGGQT----- 309
Cdd:cd07095 238 QRCtcarrlIVPD-----GAVGDAFLERLVEAAKRLRIGAPDAEPPfMGPLIIAAAAARY-LLAQQDLLALGGEPllame 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 310 --DEKDKYIAPTvLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFC 387
Cdd:cd07095 312 rlVAGTAFLSPG-IIDVTDAADVPDEEIFGPLLQVYRYDDFDEAIALANATRFGLSAGLLSDDEALFERFLARIRAGIVN 390
|
410 420
....*....|....*....|....*
gi 2119029253 388 SNdcimQMTLFS---LPFGGVGDSG 409
Cdd:cd07095 391 WN----RPTTGAsstAPFGGVGLSG 411
|
|
| PRK13252 |
PRK13252 |
betaine aldehyde dehydrogenase; Provisional |
101-411 |
1.63e-36 |
|
betaine aldehyde dehydrogenase; Provisional
Pssm-ID: 183918 Cd Length: 488 Bit Score: 140.40 E-value: 1.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 101 KKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSEL-----LPKYLdkdcFAVVcGGVKETTE 175
Cdd:PRK13252 139 RREPLGVCAGIGAWNYPIQIACWKSAPALAAGNAMIFKPSEVTPLTALKLAEIyteagLPDGV----FNVV-QGDGRVGA 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 176 LLEE--KFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCT 253
Cdd:PRK13252 214 WLTEhpDIAKVSFTGGVPTGKKVMAAAAASLKEVTMELGGKSPLIVFDDADLDRAADIAMLANFYSSGQVCTNGTRVFVQ 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 254 KAVREELVPALINCLEEFYGKNPQ-ESEDLGRIINEKHFNRLKALLSSGK-----VAVGGQ--TDE---KDKYIAPTVLV 322
Cdd:PRK13252 294 KSIKAAFEARLLERVERIRIGDPMdPATNFGPLVSFAHRDKVLGYIEKGKaegarLLCGGErlTEGgfaNGAFVAPTVFT 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 323 DVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTD----NKVVkDVLErtssGGFC----SNDCIMQ 394
Cdd:PRK13252 374 DCTDDMTIVREEIFGPVMSVLTFDDEDEVIARANDTEYGLAAGVFTADlsraHRVI-HQLE----AGICwintWGESPAE 448
|
330
....*....|....*..
gi 2119029253 395 MtlfslPFGGVGDSGMG 411
Cdd:PRK13252 449 M-----PVGGYKQSGIG 460
|
|
| PLN02466 |
PLN02466 |
aldehyde dehydrogenase family 2 member |
103-427 |
4.40e-36 |
|
aldehyde dehydrogenase family 2 member
Pssm-ID: 215259 [Multi-domain] Cd Length: 538 Bit Score: 139.94 E-value: 4.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 103 EPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFAVVCG-GVKETTELLEE- 179
Cdd:PLN02466 194 EPIGVAGQIIPWNFPLLMFAWKVGPALACGNTIVLKTAEQTPLSALYAAKLLHEAgLPPGVLNVVSGfGPTAGAALASHm 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 180 KFDYIFFTGGTHVGKIIMTAAAK-HLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTKAVRE 258
Cdd:PLN02466 274 DVDKLAFTGSTDTGKIVLELAAKsNLKPVTLELGGKSPFIVCEDADVDKAVELAHFALFFNQGQCCCAGSRTFVHERVYD 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 259 ELV-PALINCLEEFYGKNPQESEDLGRIINEKHFNRLKALLSSGK------VAVGGQTDEKDKYIAPTVLVDVKETDPVM 331
Cdd:PLN02466 354 EFVeKAKARALKRVVGDPFKKGVEQGPQIDSEQFEKILRYIKSGVesgatlECGGDRFGSKGYYIQPTVFSNVQDDMLIA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 332 QEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYsTDNKVVKDVLERTSSGGFCSNDCimqMTLF--SLPFGGVGDSG 409
Cdd:PLN02466 434 QDEIFGPVQSILKFKDLDEVIRRANNTRYGLAAGVF-TQNLDTANTLSRALRVGTVWVNC---FDVFdaAIPFGGYKMSG 509
|
330
....*....|....*...
gi 2119029253 410 MGMYHGRFSFDTFSHKRA 427
Cdd:PLN02466 510 IGREKGIYSLNNYLQVKA 527
|
|
| PRK09847 |
PRK09847 |
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional |
12-411 |
8.56e-36 |
|
gamma-glutamyl-gamma-aminobutyraldehyde dehydrogenase; Provisional
Pssm-ID: 182108 [Multi-domain] Cd Length: 494 Bit Score: 138.49 E-value: 8.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 12 REAFNSGK-TRTAEFRLKQ-LKAMLNLMKEN--EGALLEALkkDLRKPNFESIisevlftKNEIVCAINNL---TEWMKP 84
Cdd:PRK09847 67 RGVFERGDwSLSSPAKRKAvLNKLADLMEAHaeELALLETL--DTGKPIRHSL-------RDDIPGAARAIrwyAEAIDK 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 85 EYVEKTLVTKLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCF 163
Cdd:PRK09847 138 VYGEVATTSSHELAMIVREPVGVIAAIVPWNFPLLLTCWKLGPALAAGNSVILKPSEKSPLSAIRLAGLAKEAgLPDGVL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 164 AVVCGGVKETTELL--EEKFDYIFFTGGTHVGKIIMT-AAAKHLTPVSLELGGKNPCYVDKSC-DINNTAHRIAWARFLN 239
Cdd:PRK09847 218 NVVTGFGHEAGQALsrHNDIDAIAFTGSTRTGKQLLKdAGDSNMKRVWLEAGGKSANIVFADCpDLQQAASATAAGIFYN 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 240 MGQTCIAPDYVLCTKAVREELVPALINCLEEFYGKNPQE-SEDLGRIINEKHFNRLKALL----SSGKVAVGGQTDEKDK 314
Cdd:PRK09847 298 QGQVCIAGTRLLLEESIADEFLALLKQQAQNWQPGHPLDpATTMGTLIDCAHADSVHSFIregeSKGQLLLDGRNAGLAA 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 315 YIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGG-FCSNDCIM 393
Cdd:PRK09847 378 AIGPTIFVDVDPNASLSREEIFGPVLVVTRFTSEEQALQLANDSQYGLGAAVWTRDLSRAHRMSRRLKAGSvFVNNYNDG 457
|
410
....*....|....*...
gi 2119029253 394 QMTlfsLPFGGVGDSGMG 411
Cdd:PRK09847 458 DMT---VPFGGYKQSGNG 472
|
|
| ALDH_P5CDH |
cd07083 |
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH ... |
14-411 |
3.24e-33 |
|
ALDH subfamily NAD+-dependent delta(1)-pyrroline-5-carboxylate dehydrogenase-like; ALDH subfamily of the NAD+-dependent, delta(1)-pyrroline-5-carboxylate dehydrogenases (P5CDH, EC=1.5.1.12). The proline catabolic enzymes, proline dehydrogenase and P5CDH catalyze the two-step oxidation of proline to glutamate. P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA). These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes. Monofunctional enzyme sequences such as those seen in the Bacillus RocA P5CDH are also present in this subfamily as well as the human ALDH4A1 P5CDH and the Drosophila Aldh17 P5CDH.
Pssm-ID: 143402 [Multi-domain] Cd Length: 500 Bit Score: 131.55 E-value: 3.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 14 AFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESI--ISEVL-FTKNEIVCAInnltEWMKPEYVEKT 90
Cdd:cd07083 67 AFKTWKDWPQEDRARLLLKAADLLRRRRRELIATLTYEVGKNWVEAIddVAEAIdFIRYYARAAL----RLRYPAVEVVP 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 91 LVTKLDTCFIKkePFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSE----VSPNSSQLLSE--LLPKYLDkdcFA 164
Cdd:cd07083 143 YPGEDNESFYV--GLGAGVVISPWNFPVAIFTGMIVAPVAVGNTVIAKPAEdavvVGYKVFEIFHEagFPPGVVQ---FL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 165 VVCGGVKETTELLEEKFDYIFFTGGTHVGKIIMTAAAKHLT------PVSLELGGKNPCYVDKSCDINNTAHRIAWARFL 238
Cdd:cd07083 218 PGVGEEVGAYLTEHERIRGINFTGSLETGKKIYEAAARLAPgqtwfkRLYVETGGKNAIIVDETADFELVVEGVVVSAFG 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 239 NMGQTCIAPDYVLCTKAVREELVPALINCLEEFYGKNPQESE-DLGRIINEKHFNRLKALL----SSGKVAVGGQTDEKD 313
Cdd:cd07083 298 FQGQKCSAASRLILTQGAYEPVLERLLKRAERLSVGPPEENGtDLGPVIDAEQEAKVLSYIehgkNEGQLVLGGKRLEGE 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 314 KY-IAPTVLVDVKETDPVMQEEIFGPILPIVDVENID--EAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSND 390
Cdd:cd07083 378 GYfVAPTVVEEVPPKARIAQEEIFGPVLSVIRYKDDDfaEALEVANSTPYGLTGGVYSRKREHLEEARREFHVGNLYINR 457
|
410 420
....*....|....*....|.
gi 2119029253 391 CIMQMTLFSLPFGGVGDSGMG 411
Cdd:cd07083 458 KITGALVGVQPFGGFKLSGTN 478
|
|
| ALDH_F16 |
cd07111 |
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 ... |
94-416 |
5.88e-31 |
|
Aldehyde dehydrogenase family 16A1-like; Uncharacterized aldehyde dehydrogenase family 16 member A1 (ALDH16A1) and other related sequences are present in this CD. The active site cysteine and glutamate residues are not conserved in the human ALDH16A1 protein sequence.
Pssm-ID: 143429 [Multi-domain] Cd Length: 480 Bit Score: 124.82 E-value: 5.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 94 KLDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFAVVCGGVKE 172
Cdd:cd07111 137 LLDTELAGWKPVGVVGQIVPWNFPLLMLAWKICPALAMGNTVVLKPAEYTPLTALLFAEICAEAgLPPGVLNIVTGNGSF 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 173 TTELLEE-KFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVL 251
Cdd:cd07111 217 GSALANHpGVDKVAFTGSTEVGRALRRATAGTGKKLSLELGGKSPFIVFDDADLDSAVEGIVDAIWFNQGQVCCAGSRLL 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 252 CTKAVREELVPALINCLEEFYGKNP-QESEDLGRIINEKHFNRLKALLSSGKvAVGGQTDEKDK-------YIAPTVLVD 323
Cdd:cd07111 297 VQESVAEELIRKLKERMSHLRVGDPlDKAIDMGAIVDPAQLKRIRELVEEGR-AEGADVFQPGAdlpskgpFYPPTLFTN 375
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 324 VKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNdcimQMTLF--SLP 401
Cdd:cd07111 376 VPPASRIAQEEIFGPVLVVLTFRTAKEAVALANNTPYGLAASVWSENLSLALEVALSLKAGVVWIN----GHNLFdaAAG 451
|
330
....*....|....*
gi 2119029253 402 FGGVGDSGMGMYHGR 416
Cdd:cd07111 452 FGGYRESGFGREGGK 466
|
|
| ALDH_PutA-P5CDH |
cd07125 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the ... |
9-412 |
1.03e-29 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, PutA; The proline catabolic enzymes of the aldehyde dehydrogenase (ALDH) protein superfamily, proline dehydrogenase and Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, (EC=1.5.1.12 )), catalyze the two-step oxidation of proline to glutamate; P5CDH catalyzes the oxidation of glutamate semialdehyde, utilizing NAD+ as the electron acceptor. In some bacteria, the two enzymes are fused into the bifunctional flavoenzyme, proline utilization A (PutA) These enzymes play important roles in cellular redox control, superoxide generation, and apoptosis. In certain prokaryotes such as Escherichia coli, PutA is also a transcriptional repressor of the proline utilization genes.
Pssm-ID: 143443 [Multi-domain] Cd Length: 518 Bit Score: 121.53 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 9 ARLREAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKpNFESIISEVlftkNEIV--C------AINNLTE 80
Cdd:cd07125 76 AIAAAAFAGWSATPVEERAEILEKAADLLEANRGELIALAAAEAGK-TLADADAEV----REAIdfCryyaaqARELFSD 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 81 WMKPEYVEKtlvtkLDTcfIKKEPFGVALIIGPWNYPIQLvltpFIG----AVAAGNCAILKPSEVSPNSSQLLSELL-- 154
Cdd:cd07125 151 PELPGPTGE-----LNG--LELHGRGVFVCISPWNFPLAI----FTGqiaaALAAGNTVIAKPAEQTPLIAARAVELLhe 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 155 ---PKYLdkdCFAVVCGGVKETTELLE-EKFDYIFFTGGTHVGKIIMTAAAKH---LTPVSLELGGKNPCYVDKSCDINN 227
Cdd:cd07125 220 agvPRDV---LQLVPGDGEEIGEALVAhPRIDGVIFTGSTETAKLINRALAERdgpILPLIAETGGKNAMIVDSTALPEQ 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 228 -TAHRIAWArFLNMGQTCIAPDyVLCTKA-VREELVPALINCLEEFYGKNPQE-SEDLGRIINEKHFNRLKAL--LSSGK 302
Cdd:cd07125 297 aVKDVVQSA-FGSAGQRCSALR-LLYLQEeIAERFIEMLKGAMASLKVGDPWDlSTDVGPLIDKPAGKLLRAHteLMRGE 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 303 ---VAVGGQTDEKDKYIAPTVLVDVKetDPVMQEEIFGPILPIV--DVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDV 377
Cdd:cd07125 375 awlIAPAPLDDGNGYFVAPGIIEIVG--IFDLTTEVFGPILHVIrfKAEDLDEAIEDINATGYGLTLGIHSRDEREIEYW 452
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 2119029253 378 LERTSSGGFCSNDCI------MQmtlfslPFGGVGDSGMGM 412
Cdd:cd07125 453 RERVEAGNLYINRNItgaivgRQ------PFGGWGLSGTGP 487
|
|
| ALDH_ACDHII-AcoD |
cd07116 |
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is ... |
103-432 |
1.38e-28 |
|
Ralstonia eutrophus NAD+-dependent acetaldehyde dehydrogenase II-like; Included in this CD is the NAD+-dependent, acetaldehyde dehydrogenase II (AcDHII, AcoD, EC=1.2.1.3) from Ralstonia (Alcaligenes) eutrophus H16 involved in the catabolism of acetoin and ethanol, and similar proteins, such as, the dimeric dihydrolipoamide dehydrogenase of the acetoin dehydrogenase enzyme system of Klebsiella pneumonia. Also included are sequences similar to the NAD+-dependent chloroacetaldehyde dehydrogenases (AldA and AldB) of Xanthobacter autotrophicus GJ10 which are involved in the degradation of 1,2-dichloroethane. These proteins apparently require RpoN factors for expression.
Pssm-ID: 143434 [Multi-domain] Cd Length: 479 Bit Score: 117.94 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 103 EPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKYLDKDCFAVVCGGVKETTELL--EEK 180
Cdd:cd07116 135 EPLGVVGQIIPWNFPLLMATWKLAPALAAGNCVVLKPAEQTPASILVLMELIGDLLPPGVVNVVNGFGLEAGKPLasSKR 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 181 FDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNP------------CYVDKSCDinntahriAWARF-LNMGQTCIAP 247
Cdd:cd07116 215 IAKVAFTGETTTGRLIMQYASENIIPVTLELGGKSPniffadvmdaddAFFDKALE--------GFVMFaLNQGEVCTCP 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 248 DYVLCTKAVREELVPALINCLEEFYGKNPQESED-LGRIINEKHFNRLKALLSSGK-----VAVGGQ-----TDEKDKYI 316
Cdd:cd07116 287 SRALIQESIYDRFMERALERVKAIKQGNPLDTETmIGAQASLEQLEKILSYIDIGKeegaeVLTGGErnelgGLLGGGYY 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 317 APTVLVDVKETDpVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTD-NKVVKdvLERTSSGGFCSNDCiMQM 395
Cdd:cd07116 367 VPTTFKGGNKMR-IFQEEIFGPVLAVTTFKDEEEALEIANDTLYGLGAGVWTRDgNTAYR--MGRGIQAGRVWTNC-YHL 442
|
330 340 350
....*....|....*....|....*....|....*..
gi 2119029253 396 TLFSLPFGGVGDSGMGMYHGRFSFDTFSHKRaCMLRS 432
Cdd:cd07116 443 YPAHAAFGGYKQSGIGRENHKMMLDHYQQTK-NLLVS 478
|
|
| ALDH_RL0313 |
cd07148 |
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ... |
99-412 |
3.37e-27 |
|
Uncharacterized ALDH ( RL0313) with similarity to Tortula ruralis aldehyde dehydrogenase ALDH21A1; Uncharacterized aldehyde dehydrogenase (locus RL0313) with sequence similarity to the moss Tortula ruralis aldehyde dehydrogenase ALDH21A1 (RNP123) believed to play an important role in the detoxification of aldehydes generated in response to desiccation- and salinity-stress, and similar sequences are included in this CD.
Pssm-ID: 143466 [Multi-domain] Cd Length: 455 Bit Score: 113.67 E-value: 3.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 99 FIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKD-CFAVVCGgvKETTEL 176
Cdd:cd07148 119 FTTREPIGVVVAISAFNHPLNLIVHQVAPAIAAGCPVIVKPALATPLSCLAFVDLLHEAgLPEGwCQAVPCE--NAVAEK 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 177 L--EEKFDYIFFTGGTHVGKIIMTAAAKHlTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTK 254
Cdd:cd07148 197 LvtDPRVAFFSFIGSARVGWMLRSKLAPG-TRCALEHGGAAPVIVDRSADLDAMIPPLVKGGFYHAGQVCVSVQRVFVPA 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 255 AVREELVPALINCLEEFYGKNPQESE-DLGRIINEKHFNRL-----KALLSSGKVAVGGQTDEKDKYiAPTVLVDVKETD 328
Cdd:cd07148 276 EIADDFAQRLAAAAEKLVVGDPTDPDtEVGPLIRPREVDRVeewvnEAVAAGARLLCGGKRLSDTTY-APTVLLDPPRDA 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 329 PVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDcimqMTLFS---LPFGGV 405
Cdd:cd07148 355 KVSTQEIFGPVVCVYSYDDLDEAIAQANSLPVAFQAAVFTKDLDVALKAVRRLDATAVMVND----HTAFRvdwMPFAGR 430
|
....*..
gi 2119029253 406 GDSGMGM 412
Cdd:cd07148 431 RQSGYGT 437
|
|
| gabD1 |
PRK09406 |
succinic semialdehyde dehydrogenase; Reviewed |
99-411 |
1.59e-25 |
|
succinic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181826 [Multi-domain] Cd Length: 457 Bit Score: 108.67 E-value: 1.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 99 FIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFAVVCGGVKETTELL 177
Cdd:PRK09406 118 YVRYQPLGVVLAVMPWNFPLWQVVRFAAPALMAGNVGLLKHASNVPQTALYLADLFRRAgFPDGCFQTLLVGSGAVEAIL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 178 -EEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTKAV 256
Cdd:PRK09406 198 rDPRVAAATLTGSEPAGRAVAAIAGDEIKKTVLELGGSDPFIVMPSADLDRAAETAVTARVQNNGQSCIAAKRFIVHADV 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 257 REELVPALINCLEEFYGKNP-QESEDLGRIINEKHFNRLKALL-----SSGKVAVGGQTDEKDK-YIAPTVLVDVKETDP 329
Cdd:PRK09406 278 YDAFAEKFVARMAALRVGDPtDPDTDVGPLATEQGRDEVEKQVddavaAGATILCGGKRPDGPGwFYPPTVITDITPDMR 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 330 VMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDciMQMTLFSLPFGGVGDSG 409
Cdd:PRK09406 358 LYTEEVFGPVASLYRVADIDEAIEIANATTFGLGSNAWTRDEAEQERFIDDLEAGQVFING--MTVSYPELPFGGVKRSG 435
|
..
gi 2119029253 410 MG 411
Cdd:PRK09406 436 YG 437
|
|
| astD |
PRK09457 |
succinylglutamic semialdehyde dehydrogenase; Reviewed |
12-409 |
2.93e-25 |
|
succinylglutamic semialdehyde dehydrogenase; Reviewed
Pssm-ID: 181873 Cd Length: 487 Bit Score: 108.12 E-value: 2.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 12 REAFNSGKTRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESIiSEVLFTKNEIVCAINnltewmkpEYVEKTL 91
Cdd:PRK09457 47 RAAFPAWARLSFEERQAIVERFAALLEENKEELAEVIARETGKPLWEAA-TEVTAMINKIAISIQ--------AYHERTG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 92 VTKLD----TCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKY-LDKDCFAVV 166
Cdd:PRK09457 118 EKRSEmadgAAVLRHRPHGVVAVFGPYNFPGHLPNGHIVPALLAGNTVVFKPSELTPWVAELTVKLWQQAgLPAGVLNLV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 167 CGGvKETTELL--EEKFDYIFFTGGTHVGKIIMTAAAKHltP---VSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMG 241
Cdd:PRK09457 198 QGG-RETGKALaaHPDIDGLLFTGSANTGYLLHRQFAGQ--PekiLALEMGGNNPLVIDEVADIDAAVHLIIQSAFISAG 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 242 QTCiapdyvlcTKAvREELVP------ALINCLEEFYGK------NPQESEDLGRIINEKHFNRLKA----LLSSGKVAV 305
Cdd:PRK09457 275 QRC--------TCA-RRLLVPqgaqgdAFLARLVAVAKRltvgrwDAEPQPFMGAVISEQAAQGLVAaqaqLLALGGKSL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 306 --GGQTDEKDKYIAPTvLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSS 383
Cdd:PRK09457 346 leMTQLQAGTGLLTPG-IIDVTGVAELPDEEYFGPLLQVVRYDDFDEAIRLANNTRFGLSAGLLSDDREDYDQFLLEIRA 424
|
410 420 430
....*....|....*....|....*....|....*
gi 2119029253 384 G---------GFCSndcimqmtlfSLPFGGVGDSG 409
Cdd:PRK09457 425 GivnwnkpltGASS----------AAPFGGVGASG 449
|
|
| PRK13968 |
PRK13968 |
putative succinate semialdehyde dehydrogenase; Provisional |
88-422 |
2.01e-24 |
|
putative succinate semialdehyde dehydrogenase; Provisional
Pssm-ID: 184426 [Multi-domain] Cd Length: 462 Bit Score: 105.33 E-value: 2.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 88 EKTLVTKlDTCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELlpkYLDKDCFAVVC 167
Cdd:PRK13968 111 EPTLVEN-QQAVIEYRPLGTILAIMPWNFPLWQVMRGAVPILLAGNGYLLKHAPNVMGCAQLIAQV---FKDAGIPQGVY 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 168 GGVKETTE-----LLEEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQ 242
Cdd:PRK13968 187 GWLNADNDgvsqmINDSRIAAVTVTGSVRAGAAIGAQAGAALKKCVLELGGSDPFIVLNDADLELAVKAAVAGRYQNTGQ 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 243 TCIAPDYVLCTKAVREELVPALINCLEEFYGKNP-QESEDLGRII-----NEKHfNRLKALLSSG-KVAVGGQTDE-KDK 314
Cdd:PRK13968 267 VCAAAKRFIIEEGIASAFTERFVAAAAALKMGDPrDEENALGPMArfdlrDELH-HQVEATLAEGaRLLLGGEKIAgAGN 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 315 YIAPTVLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSG-----GFCSN 389
Cdd:PRK13968 346 YYAPTVLANVTPEMTAFREELFGPVAAITVAKDAEHALELANDSEFGLSATIFTTDETQARQMAARLECGgvfinGYCAS 425
|
330 340 350
....*....|....*....|....*....|...
gi 2119029253 390 DCimqmtlfSLPFGGVGDSGMGMYHGRFSFDTF 422
Cdd:PRK13968 426 DA-------RVAFGGVKKSGFGRELSHFGLHEF 451
|
|
| PLN02419 |
PLN02419 |
methylmalonate-semialdehyde dehydrogenase [acylating] |
102-424 |
1.47e-23 |
|
methylmalonate-semialdehyde dehydrogenase [acylating]
Pssm-ID: 166060 [Multi-domain] Cd Length: 604 Bit Score: 103.67 E-value: 1.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 102 KEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKYLDKDCFAVVCGGVKETTELL--EE 179
Cdd:PLN02419 247 REPLGVCAGICPFNFPAMIPLWMFPVAVTCGNTFILKPSEKDPGASVILAELAMEAGLPDGVLNIVHGTNDTVNAIcdDE 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 180 KFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLC---TKAV 256
Cdd:PLN02419 327 DIRAVSFVGSNTAGMHIYARAAAKGKRIQSNMGAKNHGLVLPDANIDATLNALLAAGFGAAGQRCMALSTVVFvgdAKSW 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 257 REELVPAlINCLEEFYGKNPqeSEDLGRIINEKHFNRLKALLSSG-----KVAVGGQT-----DEKDKYIAPTVLVDVKE 326
Cdd:PLN02419 407 EDKLVER-AKALKVTCGSEP--DADLGPVISKQAKERICRLIQSGvddgaKLLLDGRDivvpgYEKGNFIGPTILSGVTP 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 327 TDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCI-MQMTLFSLPFGGV 405
Cdd:PLN02419 484 DMECYKEEIFGPVLVCMQANSFDEAISIINKNKYGNGAAIFTSSGAAARKFQMDIEAGQIGINVPIpVPLPFFSFTGNKA 563
|
330
....*....|....*....
gi 2119029253 406 GDSGMGMYHGRFSFDTFSH 424
Cdd:PLN02419 564 SFAGDLNFYGKAGVDFFTQ 582
|
|
| ALDH_F7_AASADH |
cd07130 |
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; ... |
104-356 |
3.93e-23 |
|
NAD+-dependent alpha-aminoadipic semialdehyde dehydrogenase, ALDH family members 7A1 and 7B; Alpha-aminoadipic semialdehyde dehydrogenase (AASADH, EC=1.2.1.31), also known as ALDH7A1, Antiquitin-1, ALDH7B, or delta-1-piperideine-6-carboxylate dehydrogenase (P6CDH), is a NAD+-dependent ALDH. Human ALDH7A1 is involved in the pipecolic acid pathway of lysine catabolism, catalyzing the oxidation of alpha-aminoadipic semialdehyde to alpha-aminoadipate. Arabidopsis thaliana ALDH7B4 appears to be an osmotic-stress-inducible ALDH gene encoding a turgor-responsive or stress-inducible ALDH. The Streptomyces clavuligerus P6CDH appears to be involved in cephamycin biosynthesis, catalyzing the second stage of the two-step conversion of lysine to alpha-aminoadipic acid. The ALDH7A1 enzyme and others in this group have been observed as tetramers, yet the bacterial P6CDH enzyme has been reported as a monomer.
Pssm-ID: 143448 Cd Length: 474 Bit Score: 101.90 E-value: 3.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 104 PFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSS----QLLSELLPKY-LDKDCFAVVCGGVKETTELLE 178
Cdd:cd07130 132 PLGVVGVITAFNFPVAVWGWNAAIALVCGNVVVWKPSPTTPLTAiavtKIVARVLEKNgLPGAIASLVCGGADVGEALVK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 179 EK-FDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTKAVR 257
Cdd:cd07130 212 DPrVPLVSFTGSTAVGRQVGQAVAARFGRSLLELGGNNAIIVMEDADLDLAVRAVLFAAVGTAGQRCTTTRRLIVHESIY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 258 EELVPALINCLEEFYGKNPQESEDL-GRIINEKHFNRLKALL-----SSGKVAVGGQ-TDEKDKYIAPTVlVDVKETDPV 330
Cdd:cd07130 292 DEVLERLKKAYKQVRIGDPLDDGTLvGPLHTKAAVDNYLAAIeeaksQGGTVLFGGKvIDGPGNYVEPTI-VEGLSDAPI 370
|
250 260
....*....|....*....|....*.
gi 2119029253 331 MQEEIFGPILPIVDVENIDEAIAFMN 356
Cdd:cd07130 371 VKEETFAPILYVLKFDTLEEAIAWNN 396
|
|
| ALDH_KGSADH-like |
cd07084 |
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant ... |
104-415 |
6.72e-22 |
|
ALDH subfamily: NAD(P)+-dependent alpha-ketoglutaric semialdehyde dehydrogenases and plant delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12-like; ALDH subfamily which includes the NAD(P)+-dependent, alpha-ketoglutaric semialdehyde dehydrogenases (KGSADH, EC 1.2.1.26); plant delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12 ), ALDH family 12; the N-terminal domain of the MaoC (monoamine oxidase C) dehydratase regulatory protein; and orthologs of MaoC, PaaZ and PaaN, which are putative ring-opening enzymes of the aerobic phenylacetic acid catabolic pathway.
Pssm-ID: 143403 [Multi-domain] Cd Length: 442 Bit Score: 97.69 E-value: 6.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 104 PFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPK--YLDKDCFAVVCGGVKETTELLEE-K 180
Cdd:cd07084 100 PYGPVLVIGAFNFPLWIPLLQLAGALAMGNPVIVKPHTAVSIVMQIMVRLLHYagLLPPEDVTLINGDGKTMQALLLHpN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 181 FDYIFFTGGTHVGKIImtAAAKHLTPVSLELGGKNPCYVDKSCD-INNTAHRIAWARFLNMGQTCIAPDYVLCTKAVREE 259
Cdd:cd07084 180 PKMVLFTGSSRVAEKL--ALDAKQARIYLELAGFNWKVLGPDAQaVDYVAWQCVQDMTACSGQKCTAQSMLFVPENWSKT 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 260 lvpALINCLEEFYGKNPQESEDLGRIINEKHFNRLKALLS-SGKVAVGGQTDEKDKYI--------APTVLVDVKETD-- 328
Cdd:cd07084 258 ---PLVEKLKALLARRKLEDLLLGPVQTFTTLAMIAHMENlLGSVLLFSGKELKNHSIpsiygacvASALFVPIDEILkt 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 329 -PVMQEEIFGPILPIVDVENIDEA--IAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGfcsndcimqMTLFSLPfgGV 405
Cdd:cd07084 335 yELVTEEIFGPFAIVVEYKKDQLAlvLELLERMHGSLTAAIYSNDPIFLQELIGNLWVAG---------RTYAILR--GR 403
|
330
....*....|
gi 2119029253 406 GDSGMGMYHG 415
Cdd:cd07084 404 TGVAPNQNHG 413
|
|
| PLN00412 |
PLN00412 |
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional |
26-411 |
1.79e-21 |
|
NADP-dependent glyceraldehyde-3-phosphate dehydrogenase; Provisional
Pssm-ID: 215110 [Multi-domain] Cd Length: 496 Bit Score: 96.75 E-value: 1.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 26 RLKQLKAMLNLMKENEGALLEALKKDLRKPNFESIiSEVLFTkneivcaiNNLTEWMKPEYVE-----KTLV-------- 92
Cdd:PLN00412 77 RAELLHKAAAILKEHKAPIAECLVKEIAKPAKDAV-TEVVRS--------GDLISYTAEEGVRilgegKFLVsdsfpgne 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 93 -TKLdtCFIKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSEL-----LPKYLdkdcFAVV 166
Cdd:PLN00412 148 rNKY--CLTSKIPLGVVLAIPPFNYPVNLAVSKIAPALIAGNAVVLKPPTQGAVAALHMVHCfhlagFPKGL----ISCV 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 167 CGGVKETTELLEEK--FDYIFFTGGtHVGKIIMTAAAkhLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTC 244
Cdd:PLN00412 222 TGKGSEIGDFLTMHpgVNCISFTGG-DTGIAISKKAG--MVPLQMELGGKDACIVLEDADLDLAAANIIKGGFSYSGQRC 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 245 IAPDYVLCTKAVREELVPALINCLEEFYGKNPQESEDLGRIINEKHFNRLKALL--SSGKVAVGGQTDEKD-KYIAPTVL 321
Cdd:PLN00412 299 TAVKVVLVMESVADALVEKVNAKVAKLTVGPPEDDCDITPVVSESSANFIEGLVmdAKEKGATFCQEWKREgNLIWPLLL 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 322 VDVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTD-NKVV--KDVLErtsSGGFCSN-------Dc 391
Cdd:PLN00412 379 DNVRPDMRIAWEEPFGPVLPVIRINSVEEGIHHCNASNFGLQGCVFTRDiNKAIliSDAME---TGTVQINsapargpD- 454
|
410 420
....*....|....*....|
gi 2119029253 392 imqmtlfSLPFGGVGDSGMG 411
Cdd:PLN00412 455 -------HFPFQGLKDSGIG 467
|
|
| D1pyr5carbox3 |
TIGR01238 |
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents ... |
103-411 |
3.80e-19 |
|
delta-1-pyrroline-5-carboxylate dehydrogenase (PutA C-terminal domain); This model represents one of several related branches of delta-1-pyrroline-5-carboxylate dehydrogenase. Members of this branch are the C-terminal domain of the PutA bifunctional proline dehydrogenase / delta-1-pyrroline-5-carboxylate dehydrogenase. [Energy metabolism, Amino acids and amines]
Pssm-ID: 273518 [Multi-domain] Cd Length: 500 Bit Score: 89.97 E-value: 3.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 103 EPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSP-NSSQLLSELLPKYLDKDCFAVVCGGVKETTELL--EE 179
Cdd:TIGR01238 159 ESRGVFVCISPWNFPLAIFTGQISAALAAGNTVIAKPAEQTSlIAYRAVELMQEAGFPAGTIQLLPGRGADVGAALtsDP 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 180 KFDYIFFTGGTHVGKIIMTAAAKHL-TPVSL--ELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTKAV 256
Cdd:TIGR01238 239 RIAGVAFTGSTEVAQLINQTLAQREdAPVPLiaETGGQNAMIVDSTALPEQVVRDVLRSAFDSAGQRCSALRVLCVQEDV 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 257 REELVPALINCLEEFYGKNP-QESEDLGRIINEK-------HFNRLKALLSSGKVAV--GGQTDEKDKYIAPTvLVDVKE 326
Cdd:TIGR01238 319 ADRVLTMIQGAMQELKVGVPhLLTTDVGPVIDAEakqnllaHIEHMSQTQKKIAQLTldDSRACQHGTFVAPT-LFELDD 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 327 TDPvMQEEIFGPILPIV--DVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSGGFCSNDCIMQMTLFSLPFGG 404
Cdd:TIGR01238 398 IAE-LSEEVFGPVLHVVryKARELDQIVDQINQTGYGLTMGVHSRIETTYRWIEKHARVGNCYVNRNQVGAVVGVQPFGG 476
|
....*..
gi 2119029253 405 VGDSGMG 411
Cdd:TIGR01238 477 QGLSGTG 483
|
|
| PLN02315 |
PLN02315 |
aldehyde dehydrogenase family 7 member |
104-356 |
2.58e-15 |
|
aldehyde dehydrogenase family 7 member
Pssm-ID: 177949 Cd Length: 508 Bit Score: 77.95 E-value: 2.58e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 104 PFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKYLDKD-----CFAVVCGGVKETTEL-L 177
Cdd:PLN02315 154 PLGIVGVITAFNFPCAVLGWNACIALVCGNCVVWKGAPTTPLITIAMTKLVAEVLEKNnlpgaIFTSFCGGAEIGEAIaK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 178 EEKFDYIFFTGGTHVGKIIMTAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTKAVR 257
Cdd:PLN02315 234 DTRIPLVSFTGSSKVGLMVQQTVNARFGKCLLELSGNNAIIVMDDADIQLAVRSVLFAAVGTAGQRCTTCRRLLLHESIY 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 258 EELVPALINCLEEFYGKNPQESEDL--------GRIINEKHFNRLKAllSSGKVAVGGQTDEKD-KYIAPTVlVDVKETD 328
Cdd:PLN02315 314 DDVLEQLLTVYKQVKIGDPLEKGTLlgplhtpeSKKNFEKGIEIIKS--QGGKILTGGSAIESEgNFVQPTI-VEISPDA 390
|
250 260
....*....|....*....|....*...
gi 2119029253 329 PVMQEEIFGPILPIVDVENIDEAIAFMN 356
Cdd:PLN02315 391 DVVKEELFGPVLYVMKFKTLEEAIEINN 418
|
|
| ALDH_F4-17_P5CDH |
cd07123 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1) ... |
120-409 |
2.77e-15 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH families 4 and 17; Delta(1)-pyrroline-5-carboxylate dehydrogenase (EC=1.5.1.12 ), families 4 and 17: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH), also known as ALDH4A1 in humans, is a mitochondrial homodimer involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Also included in this CD is the Aldh17 Drosophila melanogaster (Q9VUC0) P5CDH and similar sequences.
Pssm-ID: 143441 [Multi-domain] Cd Length: 522 Bit Score: 78.01 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 120 LVLTPF----IGA--VAA----GNCAILKPSEVSPNSSQLLSEL-----LPK----YLDKDCFAVVcggvkeTTELLEEK 180
Cdd:cd07123 175 YAVSPFnftaIGGnlAGApalmGNVVLWKPSDTAVLSNYLVYKIleeagLPPgvinFVPGDGPVVG------DTVLASPH 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 181 FDYIFFTGGTHVGKIIMTAAAKHLT-----P-VSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTK 254
Cdd:cd07123 249 LAGLHFTGSTPTFKSLWKQIGENLDryrtyPrIVGETGGKNFHLVHPSADVDSLVTATVRGAFEYQGQKCSAASRAYVPE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 255 AVREELVPALINCLEEFYGKNPQE-SEDLGRIINEKHFNRLKALL------SSGKVAVGGQTDEKDKY-IAPTVLVdvkE 326
Cdd:cd07123 329 SLWPEVKERLLEELKEIKMGDPDDfSNFMGAVIDEKAFDRIKGYIdhaksdPEAEIIAGGKCDDSVGYfVEPTVIE---T 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 327 TDP---VMQEEIFGPILPI--VDVENIDEAIAFMNRHEkPLALY--VYSTDNKVVKDVLE--RTSSGGFCSND-----CI 392
Cdd:cd07123 406 TDPkhkLMTEEIFGPVLTVyvYPDSDFEETLELVDTTS-PYALTgaIFAQDRKAIREATDalRNAAGNFYINDkptgaVV 484
|
330
....*....|....*..
gi 2119029253 393 MQMtlfslPFGGVGDSG 409
Cdd:cd07123 485 GQQ-----PFGGARASG 496
|
|
| PRK11905 |
PRK11905 |
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed |
103-417 |
4.39e-14 |
|
bifunctional proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 237018 [Multi-domain] Cd Length: 1208 Bit Score: 74.90 E-value: 4.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 103 EPFGVALIIGPWNYPiqlvLTPFIG----AVAAGNCAILKPSEVSP----NSSQLLSEL-LPKyldkDCFAVVCGGVKET 173
Cdd:PRK11905 675 KPLGPVVCISPWNFP----LAIFTGqiaaALVAGNTVLAKPAEQTPliaaRAVRLLHEAgVPK----DALQLLPGDGRTV 746
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 174 TELL--EEKFDYIFFTGGTHVGKIIMTAAAKHLT-PVSL--ELGGKNPCYVDKSC-------DINNTAhriawarFLNMG 241
Cdd:PRK11905 747 GAALvaDPRIAGVMFTGSTEVARLIQRTLAKRSGpPVPLiaETGGQNAMIVDSSAlpeqvvaDVIASA-------FDSAG 819
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 242 QTCIAPDyVLCT-KAVREELVPALINCLEEFYGKNPQE-SEDLGRIINEK-------HFNRLKALlssGK----VAVGGQ 308
Cdd:PRK11905 820 QRCSALR-VLCLqEDVADRVLTMLKGAMDELRIGDPWRlSTDVGPVIDAEaqanieaHIEAMRAA---GRlvhqLPLPAE 895
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 309 TdEKDKYIAPTVLvdvkETD--PVMQEEIFGPILPIV--DVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSG 384
Cdd:PRK11905 896 T-EKGTFVAPTLI----EIDsiSDLEREVFGPVLHVVrfKADELDRVIDDINATGYGLTFGLHSRIDETIAHVTSRIRAG 970
|
330 340 350
....*....|....*....|....*....|....*....
gi 2119029253 385 GFCSNDCIMQMTLFSLPFGGVGDSGMG------MYHGRF 417
Cdd:PRK11905 971 NIYVNRNIIGAVVGVQPFGGEGLSGTGpkaggpLYLGRL 1009
|
|
| putA |
PRK11809 |
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate ... |
104-411 |
6.34e-13 |
|
trifunctional transcriptional regulator/proline dehydrogenase/pyrroline-5-carboxylate dehydrogenase; Reviewed
Pssm-ID: 236989 [Multi-domain] Cd Length: 1318 Bit Score: 71.16 E-value: 6.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 104 PFGVALIIGPWNYPiqlvLTPFIG----AVAAGNCAILKPSEVSP----NSSQLLSE---------LLPkyldkdcfavv 166
Cdd:PRK11809 768 PLGPVVCISPWNFP----LAIFTGqvaaALAAGNSVLAKPAEQTPliaaQAVRILLEagvpagvvqLLP----------- 832
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 167 cgGVKET--TELL-EEKFDYIFFTGGTHVGKIIMTAAAKHL------TPVSLELGGKNPCYVDKSC-------DINNTAh 230
Cdd:PRK11809 833 --GRGETvgAALVaDARVRGVMFTGSTEVARLLQRNLAGRLdpqgrpIPLIAETGGQNAMIVDSSAlteqvvaDVLASA- 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 231 riawarFLNMGQTCIAPDyVLCTKA-VREELVPALINCLEEFYGKNPQE-SEDLGRIIN-------EKHFNRLKAllsSG 301
Cdd:PRK11809 910 ------FDSAGQRCSALR-VLCLQDdVADRTLKMLRGAMAECRMGNPDRlSTDIGPVIDaeakaniERHIQAMRA---KG 979
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 302 ----KVAVGGQTDEKD-KYIAPTVLvdvkETDPV--MQEEIFGPILPIVDV--ENIDEAIAFMNRHEKPLALYVYSTDNK 372
Cdd:PRK11809 980 rpvfQAARENSEDWQSgTFVPPTLI----ELDSFdeLKREVFGPVLHVVRYnrNQLDELIEQINASGYGLTLGVHTRIDE 1055
|
330 340 350
....*....|....*....|....*....|....*....
gi 2119029253 373 VVKDVLERTSSGGFCSNDCIMQMTLFSLPFGGVGDSGMG 411
Cdd:PRK11809 1056 TIAQVTGSAHVGNLYVNRNMVGAVVGVQPFGGEGLSGTG 1094
|
|
| ALDH_EutE |
cd07121 |
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), ... |
104-358 |
3.13e-11 |
|
Ethanolamine utilization protein EutE-like; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), converts acetaldehyde into acetyl-CoA. This CD is limited to such monofunctional enzymes as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium. Mutations in eutE abolish the ability to utilize ethanolamine as a carbon source.
Pssm-ID: 143439 [Multi-domain] Cd Length: 429 Bit Score: 64.95 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 104 PFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKyldkdcFAVVCGG-------VKE-TTE 175
Cdd:cd07121 97 PFGVIGAITPSTNPTETIINNSISMLAAGNAVVFNPHPGAKKVSAYAVELINK------AIAEAGGpdnlvvtVEEpTIE 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 176 LLEEKFDY-----IFFTGGTHVGKIIMTAAAKhltpvSLELGGKNP-CYVDKSCDINNTAHRI-AWARFLNmGQTCIAPD 248
Cdd:cd07121 171 TTNELMAHpdinlLVVTGGPAVVKAALSSGKK-----AIGAGAGNPpVVVDETADIEKAARDIvQGASFDN-NLPCIAEK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 249 YVLctkaVREELVPALINCLEE---FYGKNPQESEDL--------GRIINEKHFNRLKALLSSgkvAVGGQTDEKDKYIa 317
Cdd:cd07121 245 EVI----AVDSVADYLIAAMQRngaYVLNDEQAEQLLevvlltnkGATPNKKWVGKDASKILK---AAGIEVPADIRLI- 316
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2119029253 318 ptvLVDVKETDPVMQEEIFGPILPIVDVENIDEAIAFM------NRH 358
Cdd:cd07121 317 ---IVETDKDHPFVVEEQMMPILPVVRVKNFDEAIELAvelehgNRH 360
|
|
| PRK11904 |
PRK11904 |
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA; |
106-411 |
1.87e-10 |
|
bifunctional proline dehydrogenase/L-glutamate gamma-semialdehyde dehydrogenase PutA;
Pssm-ID: 237017 [Multi-domain] Cd Length: 1038 Bit Score: 63.29 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 106 GVALIIGPWNYPiqlvLTPFIG----AVAAGNCAILKPSEVSP----NSSQLLSE---------LLP---KYL------D 159
Cdd:PRK11904 686 GVFVCISPWNFP----LAIFLGqvaaALAAGNTVIAKPAEQTPliaaEAVKLLHEagipkdvlqLLPgdgATVgaaltaD 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 160 KDCFAVVcggvkettelleekfdyifFTGGTHVGKII-MTAAAKHLTPVSL--ELGGKNPCYVDKSC-------DINNTA 229
Cdd:PRK11904 762 PRIAGVA-------------------FTGSTETARIInRTLAARDGPIVPLiaETGGQNAMIVDSTAlpeqvvdDVVTSA 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 230 HRIAwarflnmGQTCIAPDyVLCtkaVREE----LVPALINCLEEFYGKNPQE-SEDLGRIIN-------EKHFNRLKA- 296
Cdd:PRK11904 823 FRSA-------GQRCSALR-VLF---VQEDiadrVIEMLKGAMAELKVGDPRLlSTDVGPVIDaeakanlDAHIERMKRe 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 297 --LLSSGKVAVGGqtdEKDKYIAPTvLVDVKETDpVMQEEIFGPILPIV--DVENIDEAIAFMNRHEKPLALYVYSTDNK 372
Cdd:PRK11904 892 arLLAQLPLPAGT---ENGHFVAPT-AFEIDSIS-QLEREVFGPILHVIryKASDLDKVIDAINATGYGLTLGIHSRIEE 966
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2119029253 373 VVKDVLERTSSGGFCSN-DCI-----MQmtlfslPFGGVGDSGMG 411
Cdd:PRK11904 967 TADRIADRVRVGNVYVNrNQIgavvgVQ------PFGGQGLSGTG 1005
|
|
| ALDH_PAD-PaaZ |
cd07127 |
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) ... |
79-379 |
2.67e-10 |
|
Phenylacetic acid degradation proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida)-like; Phenylacetic acid degradation (PAD) proteins PaaZ (Escherichia coli) and PaaN (Pseudomonas putida) are putative aromatic ring cleavage enzymes of the aerobic PA catabolic pathway. PaaZ mutants were defective for growth with PA as a sole carbon source due to interruption of the putative ring opening system. This CD is limited to bacterial monofunctional enzymes.
Pssm-ID: 143445 Cd Length: 549 Bit Score: 62.50 E-value: 2.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 79 TEWMKPEyvektlvTKLDTCFIKKE----PFGVALIIG-----PWN-YPiqlvltPFIGAVAAGNCAILKP--SEVSPN- 145
Cdd:cd07127 171 AEWEKPQ-------GKHDPLAMEKTftvvPRGVALVIGcstfpTWNgYP------GLFASLATGNPVIVKPhpAAILPLa 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 146 -SSQLLSELLPKY-LDKDCFAVVCGGVKE--TTEL-LEEKFDYIFFTGGTHVGKIIMTAAAKHLtpVSLELGGKNPCYVD 220
Cdd:cd07127 238 iTVQVAREVLAEAgFDPNLVTLAADTPEEpiAQTLaTRPEVRIIDFTGSNAFGDWLEANARQAQ--VYTEKAGVNTVVVD 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 221 KSCDINNTAHRIAWARFLNMGQTCIAPDYVLCTKA-VR--------EELVPALINCLEEFYGKNPQESEDLGRIINEKHF 291
Cdd:cd07127 316 STDDLKAMLRNLAFSLSLYSGQMCTTPQNIYVPRDgIQtddgrksfDEVAADLAAAIDGLLADPARAAALLGAIQSPDTL 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 292 NRLKALLSSGKVAVGGQTDEKDKYIAPTV----LVDVKETDPVM-QEEIFGPILPIVDVENIDEAIAFMN---RHEKPLA 363
Cdd:cd07127 396 ARIAEARQLGEVLLASEAVAHPEFPDARVrtplLLKLDASDEAAyAEERFGPIAFVVATDSTDHSIELAResvREHGAMT 475
|
330
....*....|....*.
gi 2119029253 364 LYVYSTDNKVVKDVLE 379
Cdd:cd07127 476 VGVYSTDPEVVERVQE 491
|
|
| ALDH_MaoC-N |
cd07128 |
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC ... |
106-378 |
5.65e-10 |
|
N-terminal domain of the monoamine oxidase C dehydratase; The N-terminal domain of the MaoC dehydratase, a monoamine oxidase regulatory protein. Orthologs of MaoC include PaaZ (Escherichia coli) and PaaN (Pseudomonas putida), which are putative ring-opening enzymes of the aerobic phenylacetic acid (PA) catabolic pathway. The C-terminal domain of MaoC has sequence similarity to enoyl-CoA hydratase. Also included in this CD is a novel Burkholderia xenovorans LB400 ALDH of the aerobic benzoate oxidation (box) pathway. This pathway involves first the synthesis of a CoA thio-esterified aromatic acid, with subsequent dihydroxylation and cleavage steps, yielding the CoA thio-esterified aliphatic aldehyde, 3,4-dehydroadipyl-CoA semialdehyde, which is further converted into its corresponding CoA acid by the Burkholderia LB400 ALDH.
Pssm-ID: 143446 [Multi-domain] Cd Length: 513 Bit Score: 61.52 E-value: 5.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 106 GVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLL------SELLPKyldkDCFAVVCGGVKETTELLEE 179
Cdd:cd07128 146 GVAVHINAFNFPVWGMLEKFAPALLAGVPVIVKPATATAYLTEAVvkdiveSGLLPE----GALQLICGSVGDLLDHLGE 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 180 kFDYIFFTGGTHVGKIIMT--AAAKHLTPVSLELGGKNPCYVdkSCDINNTAHriAWARFLN-----M----GQTCIAPD 248
Cdd:cd07128 222 -QDVVAFTGSAATAAKLRAhpNIVARSIRFNAEADSLNAAIL--GPDATPGTP--EFDLFVKevareMtvkaGQKCTAIR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 249 YVLCTKAVREELVPALINCLEEFYGKNP-QESEDLGRIINEKHFN----RLKALLSSGKVAVGGQTD--------EKDKY 315
Cdd:cd07128 297 RAFVPEARVDAVIEALKARLAKVVVGDPrLEGVRMGPLVSREQREdvraAVATLLAEAEVVFGGPDRfevvgadaEKGAF 376
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119029253 316 IAPTVLV--DVKETDPVMQEEIFGPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVL 378
Cdd:cd07128 377 FPPTLLLcdDPDAATAVHDVEAFGPVATLMPYDSLAEAIELAARGRGSLVASVVTNDPAFARELV 441
|
|
| PRK15398 |
PRK15398 |
aldehyde dehydrogenase; |
104-353 |
3.43e-09 |
|
aldehyde dehydrogenase;
Pssm-ID: 237956 Cd Length: 465 Bit Score: 58.76 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 104 PFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKyldkdcFAVVCGG-------VKETT-E 175
Cdd:PRK15398 129 PFGVIGAVTPSTNPTETIINNAISMLAAGNSVVFSPHPGAKKVSLRAIELLNE------AIVAAGGpenlvvtVAEPTiE 202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 176 LLEEKFDY-----IFFTGGTHVGKIIMTAAAKhltpvSLELGGKNP-CYVDKSCDINNTAHRI-AWARFLNmGQTCIAPD 248
Cdd:PRK15398 203 TAQRLMKHpgialLVVTGGPAVVKAAMKSGKK-----AIGAGAGNPpVVVDETADIEKAARDIvKGASFDN-NLPCIAEK 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 249 YVLctkaVREELVPALINCLEEF--YGKNPQESEDLGR--IINEKHFNR------LKALLSsgkvAVGGQTDEKDKYIap 318
Cdd:PRK15398 277 EVI----VVDSVADELMRLMEKNgaVLLTAEQAEKLQKvvLKNGGTVNKkwvgkdAAKILE----AAGINVPKDTRLL-- 346
|
250 260 270
....*....|....*....|....*....|....*
gi 2119029253 319 tvLVDVKETDPVMQEEIFGPILPIVDVENIDEAIA 353
Cdd:PRK15398 347 --IVETDANHPFVVTELMMPVLPVVRVKDVDEAIA 379
|
|
| PutA2 |
COG4230 |
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism]; |
103-343 |
9.05e-08 |
|
Delta 1-pyrroline-5-carboxylate dehydrogenase [Amino acid transport and metabolism];
Pssm-ID: 443374 [Multi-domain] Cd Length: 1156 Bit Score: 54.94 E-value: 9.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 103 EPFGVALIIGPWNYPiqlvLTPFIG----AVAAGNCAILKPSEVSP----NSSQLLSE---------LLP-------KYL 158
Cdd:COG4230 679 RGRGVFVCISPWNFP----LAIFTGqvaaALAAGNTVLAKPAEQTPliaaRAVRLLHEagvpadvlqLLPgdgetvgAAL 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 159 --DKDCFAVVcggvkettelleekfdyifFTGGTHVGKII-MTAAAKHLTPVSL--ELGGKNPCYVDKSC-------DIn 226
Cdd:COG4230 755 vaDPRIAGVA-------------------FTGSTETARLInRTLAARDGPIVPLiaETGGQNAMIVDSSAlpeqvvdDV- 814
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 227 ntahrIAWArFLNMGQTCIAPDyVLCtkaVREELVPALINCL----EEFYGKNPQE-SEDLGRIIN-------EKHFNRL 294
Cdd:COG4230 815 -----LASA-FDSAGQRCSALR-VLC---VQEDIADRVLEMLkgamAELRVGDPADlSTDVGPVIDaearanlEAHIERM 884
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2119029253 295 KAllsSGK-VAVGGQTDEKDK--YIAPTV--LVDVKEtdpvMQEEIFGPILPIV 343
Cdd:COG4230 885 RA---EGRlVHQLPLPEECANgtFVAPTLieIDSISD----LEREVFGPVLHVV 931
|
|
| ALDH_F12_P5CDH |
cd07126 |
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1) ... |
104-384 |
7.87e-07 |
|
Delta(1)-pyrroline-5-carboxylate dehydrogenase, ALDH family 12; Delta(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH, EC=1.5.1.12), family 12: a proline catabolic enzyme of the aldehyde dehydrogenase (ALDH) protein superfamily. P5CDH is a mitochondrial enzyme involved in proline degradation and catalyzes the NAD + -dependent conversion of P5C to glutamate. The P5CDH, ALDH12A1 gene, in Arabidopsis, has been identified as an osmotic-stress-inducible ALDH gene. This CD contains both Viridiplantae and Alveolata P5CDH sequences.
Pssm-ID: 143444 Cd Length: 489 Bit Score: 51.34 E-value: 7.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 104 PFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILK-PSEVSPNSSQLLSEL----LPKyldKDCFAVVCGGVKETTELLE 178
Cdd:cd07126 142 PYGPVAIITPFNFPLEIPALQLMGALFMGNKPLLKvDSKVSVVMEQFLRLLhlcgMPA---TDVDLIHSDGPTMNKILLE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 179 EKFDYIFFTGGTHV---------GKIIMTAAA---KHLTPVSLELGgknpcYVDKSCDINntahriAWArflNMGQTCIA 246
Cdd:cd07126 219 ANPRMTLFTGSSKVaerlalelhGKVKLEDAGfdwKILGPDVSDVD-----YVAWQCDQD------AYA---CSGQKCSA 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 247 PDYVLctkaVREELVPA-LINCLEEFYGKNPQESEDLGRII---NEKHFNRLKALLS--SGKVAVGGQ--TD-------- 310
Cdd:cd07126 285 QSILF----AHENWVQAgILDKLKALAEQRKLEDLTIGPVLtwtTERILDHVDKLLAipGAKVLFGGKplTNhsipsiyg 360
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119029253 311 --EKDKYIAPTVLVDVKETDPVMQEEIFGP--ILPIVDVENIDEAIAFMNRHEKPLALYVYSTDNKVVKDVLERTSSG 384
Cdd:cd07126 361 ayEPTAVFVPLEEIAIEENFELVTTEVFGPfqVVTEYKDEQLPLVLEALERMHAHLTAAVVSNDIRFLQEVLANTVNG 438
|
|
| ALDH_F20_ACDH_EutE-like |
cd07081 |
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and ... |
100-353 |
4.58e-06 |
|
Coenzyme A acylating aldehyde dehydrogenase (ACDH), Ethanolamine utilization protein EutE, and related proteins; Coenzyme A acylating aldehyde dehydrogenase (ACDH), an NAD+ and CoA-dependent acetaldehyde dehydrogenase, acetylating (EC=1.2.1.10), functions as a single enzyme (such as the Ethanolamine utilization protein, EutE, in Salmonella typhimurium) or as part of a multifunctional enzyme to convert acetaldehyde into acetyl-CoA. The E. coli aldehyde-alcohol dehydrogenase includes the functional domains, alcohol dehydrogenase (ADH), ACDH, and pyruvate-formate-lyase deactivase; and the Entamoeba histolytica aldehyde-alcohol dehydrogenase 2 (ALDH20A1) includes the functional domains ADH and ACDH, and may be critical enzymes in the fermentative pathway.
Pssm-ID: 143400 [Multi-domain] Cd Length: 439 Bit Score: 48.80 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 100 IKKEPFGVALIIGPWNYPIQLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLpkyLDKdcfAVVCGGVK-------- 171
Cdd:cd07081 91 IIAEPIGVVASITPSTNPTSTVIFKSLISLKTRNSIIFSPHPRAKKVTQRAATLL---LQA---AVAAGAPEnligwidn 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 172 ---ETTELLEEK--FDYIFFTGGTHVGKiimtAAAKHLTPVSLELGGKNPCYVDKSCDINNTAHRIAWARFLNMGQTCIA 246
Cdd:cd07081 165 psiELAQRLMKFpgIGLLLATGGPAVVK----AAYSSGKPAIGVGAGNTPVVIDETADIKRAVQSIVKSKTFDNGVICAS 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 247 PDYVLCTKAVREELvpalincLEEFYGKNpqesedlGRIINEKHFNRLKALL-------------SSGKVA--VGGQTDE 311
Cdd:cd07081 241 EQSVIVVDSVYDEV-------MRLFEGQG-------AYKLTAEELQQVQPVIlkngdvnrdivgqDAYKIAaaAGLKVPQ 306
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2119029253 312 KDKYIAPTVLVdVKETDPVMQEEIfGPILPIVDVENIDEAIA 353
Cdd:cd07081 307 ETRILIGEVTS-LAEHEPFAHEKL-SPVLAMYRAANFADADA 346
|
|
| ALDH_KGSADH |
cd07129 |
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) ... |
128-380 |
5.17e-06 |
|
Alpha-Ketoglutaric Semialdehyde Dehydrogenase; Alpha-Ketoglutaric Semialdehyde (KGSA) Dehydrogenase (KGSADH, EC 1.2.1.26) catalyzes the NAD(P)+-dependent conversion of KGSA to alpha-ketoglutarate. This CD contains such sequences as those seen in Azospirillum brasilense, KGSADH-II (D-glucarate/D-galactarate-inducible) and KGSADH-III (hydroxy-L-proline-inducible). Both show similar high substrate specificity for KGSA and different coenzyme specificity; KGSADH-II is NAD+-dependent and KGSADH-III is NADP+-dependent. Also included in this CD is the NADP(+)-dependent aldehyde dehydrogenase from Vibrio harveyi which catalyzes the oxidation of long-chain aliphatic aldehydes to acids.
Pssm-ID: 143447 [Multi-domain] Cd Length: 454 Bit Score: 48.69 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 128 AVAAGNCAILKPSEVSPNSSQLLSELLPKYLDKdC------FAVVCGGVKETTELLEE--KFDYIFFTGGTHVGKIIMTA 199
Cdd:cd07129 131 ALAAGCPVVVKAHPAHPGTSELVARAIRAALRA-TglpagvFSLLQGGGREVGVALVKhpAIKAVGFTGSRRGGRALFDA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 200 AAKHLT--PVSLELGGKNPCYVdkscdinnT----AHRI-AWAR-F-----LNMGQTCIAPDYVLCTKAVR-EELVPALI 265
Cdd:cd07129 210 AAARPEpiPFYAELGSVNPVFI--------LpgalAERGeAIAQgFvgsltLGAGQFCTNPGLVLVPAGPAgDAFIAALA 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 266 NCLEEFygknpqeseDLGRIINE---KHFNR-LKALLSSGKV--AVGGQTDEKDKYIAPTVL-VDVKE--TDPVMQEEIF 336
Cdd:cd07129 282 EALAAA---------PAQTMLTPgiaEAYRQgVEALAAAPGVrvLAGGAAAEGGNQAAPTLFkVDAAAflADPALQEEVF 352
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2119029253 337 GPILPIVDVENIDEAIAFMNRHEKPLALYVYSTDN-----KVVKDVLER 380
Cdd:cd07129 353 GPASLVVRYDDAAELLAVAEALEGQLTATIHGEEDdlalaRELLPVLER 401
|
|
| ALDH-like |
cd07077 |
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde ... |
13-430 |
3.46e-04 |
|
NAD(P)+-dependent aldehyde dehydrogenase-like (ALDH-like) family; The aldehyde dehydrogenase-like (ALDH-like) group of the ALDH superfamily of NAD(P)+-dependent enzymes which, in general, oxidize a wide range of endogenous and exogenous aliphatic and aromatic aldehydes to their corresponding carboxylic acids and play an important role in detoxification. This group includes families ALDH18, ALDH19, and ALDH20 and represents such proteins as gamma-glutamyl phosphate reductase, LuxC-like acyl-CoA reductase, and coenzyme A acylating aldehyde dehydrogenase. All of these proteins have a conserved cysteine that aligns with the catalytic cysteine of the ALDH group.
Pssm-ID: 143396 [Multi-domain] Cd Length: 397 Bit Score: 42.98 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 13 EAFNSGK----TRTAEFRLKQLKAMLNLMKENEGALLEALKKDLRKPNFESI--------ISEVLFTKNEIvcainnlTE 80
Cdd:cd07077 1 ESAKNAQrtlaVNHDEQRDLIINAIANALYDTRQRLASEAVSERGAYIRSLIanwiammgCSESKLYKNID-------TE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 81 WMKPEYVEKTL-VTKLDT--CFIKKEPFGVALIIGPWNYPIqLVLTPFIGAVAAGNCAILKPSEVSPNSSQLLSELLPKy 157
Cdd:cd07077 74 RGITASVGHIQdVLLPDNgeTYVRAFPIGVTMHILPSTNPL-SGITSALRGIATRNQCIFRPHPSAPFTNRALALLFQA- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 158 ldkdcfAVVCGGVKE--------TTELLEE-----KFDYIFFTGGTHVGKiimtAAAKH--LTPVSLELGGKNPCYVDKS 222
Cdd:cd07077 152 ------ADAAHGPKIlvlyvphpSDELAEEllshpKIDLIVATGGRDAVD----AAVKHspHIPVIGFGAGNSPVVVDET 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 223 CDINNTAHRIAWARFLNmGQTCIAPDYVLCTKAVREELVPALINCLEEFYGKNPQESedlgriinekhfnrlkallssgK 302
Cdd:cd07077 222 ADEERASGSVHDSKFFD-QNACASEQNLYVVDDVLDPLYEEFKLKLVVEGLKVPQET----------------------K 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119029253 303 VAVGGQTDEKDKYIaptvlvdvketdpvmqEEIFGPILPIVDVENIDEA--IAFMNRHEKPLALY--VYSTDNKVVKDVL 378
Cdd:cd07077 279 PLSKETTPSFDDEA----------------LESMTPLECQFRVLDVISAveNAWMIIESGGGPHTrcVYTHKINKVDDFV 342
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2119029253 379 ERTSSGGFCSND-CIMQMTLFslpFGGVGDSGM--GMYHGR---FSFDTFSHKRACML 430
Cdd:cd07077 343 QYIDTASFYPNEsSKKGRGAF---AGKGVERIVtsGMNNIFgagVGHDALRPLKRLVR 397
|
|
| |
