|
Name |
Accession |
Description |
Interval |
E-value |
| HOT |
cd08190 |
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This ... |
3-416 |
0e+00 |
|
Hydroxyacid-oxoacid transhydrogenase (HOT) involved in gamma-hydroxybutyrate metabolism; This family contains hydroxyacid-oxoacid transhydrogenase (HOT), also known as D-2-hydroxyglutarate transhydrogenase. It catalyzes the conversion of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA), coupled to the stoichiometric conversion of alpha-ketoglutarate to D-2-hydroxyglutarate in gamma-Hydroxybutyrate catabolism. Unlike many other alcohols, which are oxidized by NAD-linked dehydrogenases, gamma-hydroxybutyrate is metabolized to succinate semialdehyde by hydroxyacid-oxoacid transhydrogenase which does not require free NAD or NADP; instead, it uses alpha-ketoglutarate as an acceptor, converting it to d-2-hydroxyglutarate. Alpha-ketoglutarate serves as an intermediate acceptor to regenerate NAD(P) required for the oxidation of GHB. HOT also catalyzes the reversible oxidation of a hydroxyacid obligatorily coupled to the reduction of an oxoacid, and requires no cofactor. In mammals, the HOT enzyme is located in mitochondria, and is expressed with an N-terminal mitochondrial targeting sequence. HOT enzyme is member of the metal-containing alcohol dehydrogenase family. It typically contains an iron although other metal ions may be used.
Pssm-ID: 341469 [Multi-domain] Cd Length: 412 Bit Score: 731.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 3 VSNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGA 82
Cdd:cd08190 1 ASNIRFGPGATRELGMDLKRLGAKKVLVVTDPGLAKLGLVERVLESLEKAGIEVVVYDGVRVEPTDESFEEAIEFAKEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 83 FDAYVAVGGGSTMDTCKAANLYASSPhSDFLDYVNAPIGKGKPVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTG 162
Cdd:cd08190 81 FDAFVAVGGGSVIDTAKAANLYATHP-GDFLDYVNAPIGKGKPVPGPLKPLIAIPTTAGTGSETTGVAIFDLEELKVKTG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 163 IASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTALPYHMRsPCPSNPITRPAYQGSNPISDIWAIHALRIV 242
Cdd:cd08190 160 ISSRYLRPTLAIVDPLLTLTLPPRVTASSGFDVLCHALESYTARPYNAR-PRPANPDERPAYQGSNPISDVWAEKAIELI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 243 AKYLKRAVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKTYKAKDYNVDHPLVPHGLSVVLTSPAVFS 322
Cdd:cd08190 239 GKYLRRAVNDGDDLEARSNMLLASTLAGIGFGNAGVHLPHAMAYPIAGLVKDYRPPGYPVDHPHVPHGLSVALTAPAVFR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 323 FTAQMSPERHLETAEILGADTHTARIPDAGPILADTLRKFLFDLDVDDGLASIGYSKADIPALVKGTLPQERVTKLAPRP 402
Cdd:cd08190 319 FTAPACPERHLEAAELLGADTSGASDRDAGEVLADALIKLMRDIGIPNGLSALGYSEDDIPALVEGTLPQQRLLKLNPRP 398
|
410
....*....|....
gi 1333704659 403 QSEEDLSALFEASM 416
Cdd:cd08190 399 VTEEDLEEIFEDAL 412
|
|
| EutG |
COG1454 |
Alcohol dehydrogenase, class IV [Energy production and conversion]; |
6-416 |
2.40e-110 |
|
Alcohol dehydrogenase, class IV [Energy production and conversion];
Pssm-ID: 441063 [Multi-domain] Cd Length: 381 Bit Score: 329.39 E-value: 2.40e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 6 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAFDA 85
Cdd:COG1454 11 IVFGAGALAELGEELKRLGAKRALIVTDPGLAKLGLLDRVLDALEAAGIEVVVFDDVEPNPTVETVEAGAAAAREFGADV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 86 YVAVGGGSTMDTCKAANLYASSPHsDFLDYVNApigkgKPVSVPLKPLIAVP----------TtsgtgsettgVAIFDYE 155
Cdd:COG1454 91 VIALGGGSAIDAAKAIALLATNPG-DLEDYLGI-----KKVPGPPLPLIAIPttagtgsevtP----------FAVITDP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 156 HLKVKTGIASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTALpyhmrspcpsnpitrpayqGSNPISDIWA 235
Cdd:COG1454 155 ETGVKKGIADPELLPDVAILDPELTLTLPPSLTAATGMDALTHAIEAYVSK-------------------GANPLTDALA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 236 IHALRIVAKYLKRAVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakdYNvdhplVPHGLSVVL 315
Cdd:COG1454 216 LEAIRLIARNLPRAVADGDDLEAREKMALASLLAGMAFANAGLGAVHALAHPLGGL--------FH-----VPHGLANAI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 316 TSPAVFSFTAQMSPERHLETAEILGADTHTARiPDAGPILADTLRKFLFDLDVDDGLASIGYSKADIPALVKGTLpQERV 395
Cdd:COG1454 283 LLPHVLRFNAPAAPERYAEIARALGLDVGLSD-EEAAEALIEAIRELLRDLGIPTRLSELGVTEEDLPELAELAL-ADRC 360
|
410 420
....*....|....*....|.
gi 1333704659 396 TKLAPRPQSEEDLSALFEASM 416
Cdd:COG1454 361 LANNPRPLTEEDIEAILRAAY 381
|
|
| Fe-ADH |
cd08551 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large ... |
4-412 |
1.91e-105 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. They contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases, insect-type, or short-chain alcohol dehydrogenases, iron-containing alcohol dehydrogenases, among others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341481 [Multi-domain] Cd Length: 372 Bit Score: 316.31 E-value: 1.91e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 4 SNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAF 83
Cdd:cd08551 2 TRIVFGAGALARLGEELKALGGKKVLLVTDPGLVKAGLLDKVLESLKAAGIEVEVFDDVEPNPTVETVEAAAELAREEGA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 84 DAYVAVGGGSTMDTCKAANLYASSPHSDfLDYVNapigkGKPVSVPLKPLIAVPttsgtgsettGVAIFDYEHLKVKTGI 163
Cdd:cd08551 82 DLVIAVGGGSVLDTAKAIAVLATNGGSI-RDYEG-----IGKVPKPGLPLIAIPttagtgsevtPNAVITDPETGRKMGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 164 ASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTALPyhmrspcpsnpitrpayqgSNPISDIWAIHALRIVA 243
Cdd:cd08551 156 VSPYLLPDVAILDPELTLSLPPSVTAATGMDALTHAIEAYTSKK-------------------ANPISDALALEAIRLIG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 244 KYLKRAVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakdYNvdhplVPHGLSVVLTSPAVFSF 323
Cdd:cd08551 217 KNLRRAVADGSDLEAREAMLLASLLAGIAFGNAGLGAVHALAYPLGGR--------YH-----IPHGVANAILLPYVMEF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 324 TAQMSPERHLETAEILGADTHTARIPDAGPILADTLRKFLFDLDVDDGLASIGYSKADIPALVKGTLPQERVTKLAPRPQ 403
Cdd:cd08551 284 NLPACPEKYAEIAEALGEDVEGLSDEEAAEAAVEAVRELLRDLGIPTSLSELGVTEEDIPELAEDAMKSGRLLSNNPRPL 363
|
....*....
gi 1333704659 404 SEEDLSALF 412
Cdd:cd08551 364 TEEDIREIY 372
|
|
| Fe-ADH |
pfam00465 |
Iron-containing alcohol dehydrogenase; |
4-408 |
1.70e-95 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 425696 [Multi-domain] Cd Length: 362 Bit Score: 290.66 E-value: 1.70e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 4 SNIRYGAGVTKEVGMDLQNMGAKnVCLMTDKNLSQLPPVQVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAF 83
Cdd:pfam00465 2 TRIVFGAGALAELGEELKRLGAR-ALIVTDPGSLKSGLLDKVLASLEEAGIEVVVFDGVEPEPTLEEVDEAAALAREAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 84 DAYVAVGGGSTMDTCKAANLYASSPHSDFLDYvnapigKGKPVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 163
Cdd:pfam00465 81 DVIIAVGGGSVIDTAKAIALLLTNPGDVWDYL------GGKPLTKPALPLIAIPTTAGTGSEVTPLAVITDTETGEKLGI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 164 ASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTAlpyhmrspcpsnpitrpayQGSNPISDIWAIHALRIVA 243
Cdd:pfam00465 155 FSPKLLPDLAILDPELTLTLPPRLTAATGMDALAHAVEAYVS-------------------KGANPLTDALALEAIRLIA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 244 KYLKRAVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakdynvdhplVPHGLSVVLTSPAVFSF 323
Cdd:pfam00465 216 ENLPRAVADGEDLEARENMLLASTLAGLAFSNAGLGAAHALAHALGGRYG-------------IPHGLANAILLPYVLRF 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 324 TAQMSPERHLETAEILGADTHTARIPDAgpilADTLRKFLFDLDVDDGLASIGYSKADIPALVKGTLpQERVTKLAPRPQ 403
Cdd:pfam00465 283 NAPAAPEKLAQLARALGEDSDEEAAEEA----IEALRELLRELGLPTTLSELGVTEEDLDALAEAAL-RDRSLANNPRPL 357
|
....*
gi 1333704659 404 SEEDL 408
Cdd:pfam00465 358 TAEDI 362
|
|
| Fe-ADH-like |
cd14863 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-414 |
2.55e-83 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341485 [Multi-domain] Cd Length: 380 Bit Score: 260.16 E-value: 2.55e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 6 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAFDA 85
Cdd:cd14863 8 VIFGAGAVEQIGELLKELGCKKVLLVTDKGLKKAGIVDKIIDLLEEAGIEVVVFDDVEPDPPDEIVDEAAEIAREEGADG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 86 YVAVGGGSTMDTCKAANLYASSPHSDfLDYvnapIGKGKPVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIAS 165
Cdd:cd14863 88 VIGIGGGSVLDTAKAIAVLLTNPGPI-IDY----ALAGPPVPKPGIPLIAIPTTAGTGSEVTPIAVITDEENGVKKSLLG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 166 RAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTAlpyhmrspcpsnpitrpayQGSNPISDIWAIHALRIVAKY 245
Cdd:cd14863 163 PFLVPDLAILDPELTVGLPPSLTAATGMDALSHAIEAYTS-------------------KLANPMTDALALQAIRLIVKN 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 246 LKRAVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakdYNvdhplVPHGLSVVLTSPAVFSFTA 325
Cdd:cd14863 224 LPRAVKDGDNLEARENMLLASNLAGIAFNNAGTHIGHAIAHALGAL--------YH-----IPHGLACALALPVVLEFNA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 326 QMSPERHLETAEILGADTHTARIPDAGPILADTLRKFLFDLDVDDGLASIGYSKADIPALVKGTLpQERVTKLAPRPQSE 405
Cdd:cd14863 291 EAYPEKVKKIAKALGVSFPGESDEELGEAVADAIREFMKELGIPSLFEDYGIDKEDLDKIAEAVL-KDPFAMFNPRPITE 369
|
....*....
gi 1333704659 406 EDLSALFEA 414
Cdd:cd14863 370 EEVAEILEA 378
|
|
| Fe-ADH-like |
cd08191 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
4-416 |
2.43e-77 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341470 [Multi-domain] Cd Length: 392 Bit Score: 244.83 E-value: 2.43e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 4 SNIRYGAGVTKEVGMDLQNMGAKnVCLMTDKNLSQLPPVQVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAF 83
Cdd:cd08191 5 SRLLFGPGARRALGRVAARLGSR-VLIVTDPRLASTPLVAELLAALTAAGVAVEVFDGGQPELPVSTVADAAAAARAFDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 84 DAYVAVGGGSTMDTCKAANLYASSPhSDFLDYvnapIGKGKpVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 163
Cdd:cd08191 84 DVVIGLGGGSNMDLAKVVALLLAHG-GDPRDY----YGEDR-VPGPVLPLIAVPTTAGTGSEVTPVAVLTDPARGMKVGV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 164 ASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTALPyhmRSPCPSNPiTRPAYQGSNPISDIWAIHALRIVA 243
Cdd:cd08191 158 SSPYLRPAVAIVDPELTLTCPPGVTADSGIDALTHAIESYTARD---FPPFPRLD-PDPVYVGKNPLTDLLALEAIRLIG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 244 KYLKRAVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKTykakdynvdhplvPHGLSVVLTSPAVFSF 323
Cdd:cd08191 234 RHLPRAVRDGDDLEARSGMALAALLAGLAFGTAGTAAAHALQYPIGALTHT-------------SHGVGNGLLLPYVMRF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 324 TAQMSPERHLETAEILGADT--HTARIPDAGPilaDTLRKFLFDLDVDDGLASIGYSKADIPALVKGTLPQERVTKLAPR 401
Cdd:cd08191 301 NRPARAAELAEIARALGVTTagTSEEAADRAI---ERVEELLARIGIPTTLADLGVTEADLPGLAEKALSVTRLIANNPR 377
|
410
....*....|....*
gi 1333704659 402 PQSEEDLSALFEASM 416
Cdd:cd08191 378 PPTEEDLLRILRAAF 392
|
|
| Fe-ADH-like |
cd08185 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
5-413 |
2.71e-76 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase-like (ADH) proteins. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase fold and is a member of the iron-containing alcohol dehydrogenase-like family. They are distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341464 [Multi-domain] Cd Length: 379 Bit Score: 242.02 E-value: 2.71e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 5 NIRYGAGVTKEVGmDLQNMGAKNVCLMTDKNLSQLPPV-QVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAF 83
Cdd:cd08185 6 RILFGAGKLNELG-EEALRPGKKALIVTGKGSSKKTGLlDRVKKLLEKAGVEVVVFDKVEPNPLTTTVMEGAALAKEEGC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 84 DAYVAVGGGSTMDTCKAANLYASSPHsDFLDYVNAPIGKGKPVSVPLkPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 163
Cdd:cd08185 85 DFVIGLGGGSSMDAAKAIAFMATNPG-DIWDYIFGGTGKGPPPEKAL-PIIAIPTTAGTGSEVDPWAVITNPETKEKKGI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 164 ASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTALpyhmrspcpsnpitrpayqGSNPISDIWAIHALRIVA 243
Cdd:cd08185 163 GHPALFPKVSIVDPELMLTVPPRVTAYTGFDALFHAFESYISK-------------------NANPFSDMLALEAIRLVA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 244 KYLKRAVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakdynvdHPLVPHGLSVVLTSPAVFSF 323
Cdd:cd08185 224 KYLPRAVKDGSDLEAREKMAWASTLAGIVIANSGTTLPHGLEHPLSGY------------HPNIPHGAGLAALYPAYFEF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 324 TAQMSPERhleTAEILGADTHTARIPDAGPILADTLRKFLFDLDVDDGLASIGYSKADIPALVkgtlpqERVTKLA---- 399
Cdd:cd08185 292 TIEKAPEK---FAFVARAEASGLSDAKAAEDFIEALRKLLKDIGLDDLLSDLGVTEEDIPWLA------ENAMETMgglf 362
|
410
....*....|....*..
gi 1333704659 400 ---PRPQSEEDLSALFE 413
Cdd:cd08185 363 annPVELTEEDIVEIYE 379
|
|
| Fe-ADH-like |
cd08194 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
4-414 |
4.94e-70 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341473 [Multi-domain] Cd Length: 378 Bit Score: 225.49 E-value: 4.94e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 4 SNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAF 83
Cdd:cd08194 2 RTIIIGGGALEELGEEAASLGGKRALIVTDKVMVKLGLVDKVTQLLAEAGIAYAVFDDVVSEPTDEMVEEGLALYKEGGC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 84 DAYVAVGGGSTMDTCKAANLYASSPhSDFLDYVNAPIGKGKPVsvplkPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 163
Cdd:cd08194 82 DFIVALGGGSPIDTAKAIAVLATNG-GPIRDYMGPRKVDKPGL-----PLIAIPTTAGTGSEVTRFTVITDTETDVKMLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 164 ASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYtalpyhmrspcpsnpITRPAyqgsNPISDIWAIHALRIVA 243
Cdd:cd08194 156 KGPALLPAVAIVDPELTLSMPPRVTAATGIDALTHAIEAY---------------VSRKA----QPLTDTLALSAIKLIG 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 244 KYLKRAVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLVktykakdynvdHplVPHGLSVVLTSPAVFSF 323
Cdd:cd08194 217 RNLRRAYADGDDLEAREAMMLAALEAGIAFSNSSVALVHGMSRPIGALF-----------H--VPHGLSNAMLLPAVTEF 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 324 TAQMSPERHLETAEILGADTHTARIPDAGPILADTLRKFLFDLDVdDGLASIGYSKAD----IPALVKGTL----PQerv 395
Cdd:cd08194 284 SLPGAPERYAEIARAMGIATEGDSDEEAAEKLVEALERLCADLEI-PTLREYGIDEEEfeaaLDKMAEDALasgsPA--- 359
|
410
....*....|....*....
gi 1333704659 396 tkLAPRPQSEEDLSALFEA 414
Cdd:cd08194 360 --NNPRVPTKEEIIELYRE 376
|
|
| Fe-ADH-like |
cd17814 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
8-412 |
6.94e-70 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341489 [Multi-domain] Cd Length: 374 Bit Score: 225.11 E-value: 6.94e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 8 YGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIE-FAKKGAfDAY 86
Cdd:cd17814 9 FGVGARKLAGRYAKNLGARKVLVVTDPGVIKAGWVDEVLDSLEAEGLEYVVFSDVTPNPRDFEVMEGAElYREEGC-DGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 87 VAVGGGSTMDTCKAANLYASSpHSDFLDYvnapIGKGKpVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASR 166
Cdd:cd17814 88 VAVGGGSPIDCAKGIGIVVSN-GGHILDY----EGVDK-VRRPLPPLICIPTTAGSSADVSQFAIITDTERRVKMAIISK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 167 AIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTalpyhmrspcpSNpitrpayqGSNPISDIWAIHALRIVAKYL 246
Cdd:cd17814 162 TLVPDVSLIDPETLTTMDPELTACTGMDALTHAIEAYV-----------SN--------ASSPLTDLHALEAIRLISENL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 247 KRAVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLVktykakDynvdhplVPHGLSVVLTSPAVFSFTAQ 326
Cdd:cd17814 223 PKAVADPDDLEAREKMMLASLQAGLAFSNASLGAVHAMAHSLGGLL------D-------LPHGECNALLLPHVIRFNFP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 327 MSPERHLETAEILGADTHTARIPDAGPILADTLRKFLFDLDVDDGLASIGYSKADIPALVKGTLpqeR----VTKlaPRP 402
Cdd:cd17814 290 AAPERYRKIAEAMGLDVDGLDDEEVAERLIEAIRDLREDLGIPETLSELGVDEEDIPELAKRAM---KdpclVTN--PRR 364
|
410
....*....|
gi 1333704659 403 QSEEDLSALF 412
Cdd:cd17814 365 PTREDIEEIY 374
|
|
| Fe-ADH-like |
cd08196 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
5-412 |
3.73e-69 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341475 [Multi-domain] Cd Length: 367 Bit Score: 222.84 E-value: 3.73e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 5 NIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQVVMDSLvkNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAFD 84
Cdd:cd08196 8 KIIFGEGILKELPDIIKELGGKRGLLVTDPSFIKSGLAKRIVESL--KGRIVAVFSDVEPNPTVENVDKCARLARENGAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 85 AYVAVGGGSTMDTCKAANLYASSPHSdFLDYvnapIGKGKPVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIA 164
Cdd:cd08196 86 FVIAIGGGSVLDTAKAAACLAKTDGS-IEDY----LEGKKKIPKKGLPLIAIPTTAGTGSEVTPVAVLTDKEKGKKAPLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 165 SRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTALpyhmrspcpsnpitrpayqGSNPISDIWAIHALRIVAK 244
Cdd:cd08196 161 SPGFYPDIAIVDPELTYSMPPKVTASTGIDALCHAIEAYWSI-------------------NHQPISDALALEAAKLVLE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 245 YLKRAVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakdYNvdhplVPHGLSVVLTSPAVFSFT 324
Cdd:cd08196 222 NLEKAYNNPNDKEAREKMALASLLAGLAFSQTRTTASHACSYPLTSH--------FG-----IPHGEACALTLPSFIRLN 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 325 AQMSPERHLETAEILGADTHTAripdagpiLADTLRKFLFDLDVDDGLASIGYSKADIPALVKGTLPQERVtKLAPRPQS 404
Cdd:cd08196 289 AEALPGRLDELAKQLGFKDAEE--------LADKIEELKKRIGLRTRLSELGITEEDLEEIVEESFHPNRA-NNNPVEVT 359
|
....*...
gi 1333704659 405 EEDLSALF 412
Cdd:cd08196 360 KEDLEKLL 367
|
|
| LPO |
cd08176 |
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between ... |
8-413 |
1.71e-66 |
|
Lactadehyde:propanediol oxidoreductase (LPO) catalyzes the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria; Lactadehyde:propanediol oxidoreductase (LPO) is a member of the group III iron-activated dehydrogenases which catalyze the interconversion between L-lactaldehyde and L-1,2-propanediol in Escherichia coli and other enterobacteria. L-fucose and L-rhamnose are used by Escherichia coli through an inducible pathway mediated by the fucose regulon comprising four linked operons fucO, fucA, fucPIK, and fucR. The fucA-encoded aldolase catalyzes the formation of dihydroxyacetone phosphate and L-lactaldehyde. Under anaerobic conditions, with NADH as a cofactor, lactaldehyde is converted by a fucO-encoded lactadehyde:propanediol oxidoreductase (LPO) to L-1,2-propanediol, which is excreted as a fermentation product. In mutant strains, E. coli adapted to grow on L-1,2-propanediol, FucO catalyzes the oxidation of the polyol to L-lactaldehyde. FucO is induced regardless of the respiratory conditions of the culture, remains fully active in the absence of oxygen. In the presence of oxygen, this enzyme becomes oxidatively inactivated by a metal-catalyzed oxidation mechanism. FucO is an iron-dependent metalloenzyme that is inactivated by other metals, such as zinc, copper, or cadmium. This enzyme can also reduce glycol aldehyde with similar efficiency. Beside L-1,2-propanediol, the enzyme is also able to oxidize methanol as an alternative substrate.
Pssm-ID: 341455 [Multi-domain] Cd Length: 378 Bit Score: 216.26 E-value: 1.71e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 8 YGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAFDAYV 87
Cdd:cd08176 11 FGWGAIEEIGEEAKKRGFKKALIVTDKGLVKFGIVDKVTDVLKEAGIAYTVFDEVKPNPTIENVMAGVAAYKESGADGII 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 88 AVGGGSTMDTCKAANLYASSPHSDfldyVNAPIGKgKPVSVPLKPLIAVPTTSGTGSETTGVA-IFDYEHlKVKTGIASR 166
Cdd:cd08176 91 AVGGGSSIDTAKAIGIIVANPGAD----VRSLEGV-APTKNPAVPIIAVPTTAGTGSEVTINYvITDTEK-KRKFVCVDP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 167 AIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTALpyhmrspcpsnpitrpayqGSNPISDIWAIHALRIVAKYL 246
Cdd:cd08176 165 HDIPTVAIVDPDLMSSMPKGLTAATGMDALTHAIEGYITK-------------------GAWELSDMLALKAIELIAKNL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 247 KRAVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakdYNvdhplVPHGLSVVLTSPAVFSFTAQ 326
Cdd:cd08176 226 RKAVANPNNVEARENMALAQYIAGMAFSNVGLGIVHSMAHPLSAF--------YD-----TPHGVANAILLPYVMEFNAP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 327 MSPERHLETAEILGADTHTARIPDAGPILADTLRKFLFDLDVDDGLASIGYSKADIPALVKGTLpQERVTKLAPRPQSEE 406
Cdd:cd08176 293 ATGEKYRDIARAMGVDTTGMSDEEAAEAAVDAVKKLSKDVGIPQKLSELGVKEEDIEALAEDAL-NDVCTPGNPREATKE 371
|
....*..
gi 1333704659 407 DLSALFE 413
Cdd:cd08176 372 DIIALYK 378
|
|
| Fe-ADH-like |
cd14862 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
20-412 |
2.37e-63 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341484 [Multi-domain] Cd Length: 375 Bit Score: 208.23 E-value: 2.37e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 20 LQNMGAKNVCLMTDKNLSQLPPVQVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAFDAYVAVGGGSTMDTCK 99
Cdd:cd14862 19 LEQLSGKRALIVTDKVLVKLGLLKKVLKRLLQAGFEVEVFDEVEPEPPLETVLKGAEAMREFEPDLIIALGGGSVMDAAK 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 100 AANLYASSPHSDFLDYVNAPIGKGKPVSVplkpLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLIDPLH 179
Cdd:cd14862 99 AAWVLYERPDLDPEDISPLDLLGLRKKAK----LIAIPTTSGTGSEATWAIVLTDTEEPRKIAVANPELVPDVAILDPEF 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 180 TLHMPDRVVANSGFDVLCHALESYTAlpyhmrspcpsnpitrpayQGSNPISDIWAIHALRIVAKYLKRAVRNPDDLEAR 259
Cdd:cd14862 175 VLGMPPKLTAGTGLDALAHAVEAYLS-------------------TWSNDFSDALALKAIELIFKYLPRAYKDGDDLEAR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 260 SNMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakdynvdhplVPHGLSVVLTSPAVFSFTAQMSPERHLETAEIL 339
Cdd:cd14862 236 EKMHNAATIAGLAFGNSQAGLAHALGHSLGAVFH-------------VPHGIAVGLFLPYVIEFYAKVTDERYDLLKLLG 302
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333704659 340 GADTHTARIPDAgpiLADTLRKFLFDLDVDDGLASIGYSKAD----IPALVKGTLpQERVTKLAPRPQSEEDLSALF 412
Cdd:cd14862 303 IEARDEEEALKK---LVEAIRELYKEVGQPLSIKDLGISEEEfeekLDELVEYAM-EDSCTITSPRPPSEEDLKKLF 375
|
|
| Fe-ADH-like |
cd14865 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-416 |
1.88e-61 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341487 [Multi-domain] Cd Length: 383 Bit Score: 203.54 E-value: 1.88e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 6 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQVVMDSLVKNGINFKVYDNVrvePTDRSF---MEAIEFAKKGA 82
Cdd:cd14865 9 IVSGAGALENLPAELARLGARRPLIVTDKGLAAAGLLKKVEDALGDAIEIVGVFDDV---PPDSSVavvNEAAARAREAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 83 FDAYVAVGGGSTMDTCKAANLYASSPHSDFLDYVNAPIGKGkpvsvPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTG 162
Cdd:cd14865 86 ADGIIAVGGGSVIDTAKGVNILLSEGGDDLDDYGGANRLTR-----PLKPLIAIPTTAGTGSEVTLVAVIKDEEKKVKLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 163 IASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTALpyhmrspcpsnpitrpayqGSNPISDIWAIHALRIV 242
Cdd:cd14865 161 FVSPFLLPDVAILDPRLTLSLPPKLTAATGMDALTHAIEAYTSL-------------------QKNPISDALALQAIRLI 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 243 AKYLKRAVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakdynvdhplVPHGL--SVVLtsPAV 320
Cdd:cd14865 222 SENLPKAVKNGKDLEARLALAIAATMAGIAFSNSMVGLVHAIAHAVGAVAG-------------VPHGLanSILL--PHV 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 321 FSFTAQMSPERHLETAEIL--GADTHTARIPDAGPILADTLRKFLFDLDVDDGLASIGYSKADIPALVKGTLpQERVTKL 398
Cdd:cd14865 287 MRYNLDAAAERYAELALALayGVTPAGRRAEEAIEAAIDLVRRLHELCGLPTRLRDVGVPEEQLEAIAELAL-NDGAILF 365
|
410
....*....|....*...
gi 1333704659 399 APRPQSEEDLSALFEASM 416
Cdd:cd14865 366 NPREVDPEDILAILEAAY 383
|
|
| PDDH |
cd08188 |
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) ... |
9-413 |
8.70e-60 |
|
1,3-Propanediol (1,3-PD) dehydrogenase; This family includes 1,3-propanediol (1,3-PD) dehydrogenase, a key enzyme in the microbial production of 1,3-PD that has been previously characterized as the product of dhaT gene in Klebsiella pneumoniae. 1,3-PD dehydrogenase is a member of the family III metal-dependent polyol dehydrogenases, which are shown to require a divalent metal ion for catalysis. However, some members of this family showed a dependence on Fe(2+) or Zn(2+) for activity.
Pssm-ID: 341467 [Multi-domain] Cd Length: 377 Bit Score: 198.89 E-value: 8.70e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 9 GAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAFDAYVA 88
Cdd:cd08188 12 GPGCLKEIGDELKKLGGKKALIVTDKGLVKLGLVKKVTDVLEEAGIEYVIFDGVQPNPTVTNVNEGLELFKENGCDFIIS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 89 VGGGSTMDTCKAANLYASSPhSDFLDYVNapIGKgkpVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAI 168
Cdd:cd08188 92 VGGGSAHDCAKAIGILATNG-GEIEDYEG--VDK---SKKPGLPLIAINTTAGTASEVTRFAVITDEERHVKMVIVDWNV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 169 KPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTALpyhmrspcpsnpitrpayqGSNPISDIWAIHALRIVAKYLKR 248
Cdd:cd08188 166 TPTIAVNDPELMLGMPPSLTAATGMDALTHAIEAYVST-------------------GATPLTDALALEAIRLIAENLPK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 249 AVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakdYNvdhplVPHGL--SVVLtsPAVFSFTAQ 326
Cdd:cd08188 227 AVANGKDLEARENMAYAQFLAGMAFNNAGLGYVHAMAHQLGGF--------YN-----LPHGVcnAILL--PHVMEFNLP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 327 MSPERHLETAEILGADTHTARIPDAGPILADTLRKFLFDLDVDDGLASIGYSKADIPALVKGTLpQERVTKLAPRPQSEE 406
Cdd:cd08188 292 ACPERFADIARALGENTEGLSDEEAAEAAIEAIRKLSRRVGIPSGLKELGVKEEDFPLLAENAL-KDACGPTNPRQATKE 370
|
....*..
gi 1333704659 407 DLSALFE 413
Cdd:cd08188 371 DVIAIYR 377
|
|
| Fe-ADH-like |
cd14861 |
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to ... |
6-416 |
2.00e-57 |
|
Iron-containing alcohol dehydrogenases-like; This family contains proteins similar to iron-containing alcohol dehydrogenase (Fe-ADH), most of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions.
Pssm-ID: 341483 [Multi-domain] Cd Length: 374 Bit Score: 192.73 E-value: 2.00e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 6 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAFDA 85
Cdd:cd14861 6 IRFGAGAIAELPEELKALGIRRPLLVTDPGLAALGIVDRVLEALGAAGLSPAVFSDVPPNPTEADVEAGVAAYREGGCDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 86 YVAVGGGSTMDTCKAANLYASSPHS--DFLDYVNAPIGKGKPVSvplkPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 163
Cdd:cd14861 86 IIALGGGSAIDAAKAIALMATHPGPlwDYEDGEGGPAAITPAVP----PLIAIPTTAGTGSEVGRAAVITDDDTGRKKII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 164 ASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTALPYHmrspcpsnpitrpayqgsnPISDIWAIHALRIVA 243
Cdd:cd14861 162 FSPKLLPKVAICDPELTLGLPPRLTAATGMDALTHCIEAYLSPGFH-------------------PMADGIALEGLRLIS 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 244 KYLKRAVRNPDDLEARSNMHLASAFAGIGFGNaGVHLCHGMSYPISGLVKTykakdynvdhplvPHGLSVVLTSPAVFSF 323
Cdd:cd14861 223 EWLPRAVADGSDLEARGEMMMAALMGAVAFQK-GLGAVHALAHALGALYGL-------------HHGLLNAILLPYVLRF 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 324 TAQMSPERHLETAEILGADTHTariPDAgpiLADTLRKFLFDLDVDDGLASIGYSKADIPALVKGTLpQERVTKLAPRPQ 403
Cdd:cd14861 289 NRPAVEDKLARLARALGLGLGG---FDD---FIAWVEDLNERLGLPATLSELGVTEDDLDELAELAL-ADPCHATNPRPV 361
|
410
....*....|...
gi 1333704659 404 SEEDLSALFEASM 416
Cdd:cd14861 362 TAEDYRALLREAL 374
|
|
| HVD |
cd08193 |
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to ... |
3-414 |
7.69e-56 |
|
5-hydroxyvalerate dehydrogenase (HVD) catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor; 5-hydroxyvalerate dehydrogenase (HVD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the cyclopentanol metabolism biochemical pathway. It catalyzes the oxidation of 5-hydroxyvalerate to 5-oxovalerate with NAD+ as cofactor. This cyclopentanol (cpn) degradation pathway is present in some bacteria which can use cyclopentanol as sole carbon source. In Comamonas sp. strain NCIMB 9872, this enzyme is encoded by the CpnD gene.
Pssm-ID: 341472 [Multi-domain] Cd Length: 379 Bit Score: 188.49 E-value: 7.69e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 3 VSNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGA 82
Cdd:cd08193 4 VPRIICGAGAAARLGELLRELGARRVLLVTDPGLVKAGLADPALAALEAAGIAVTVFDDVVADPPEAVVEAAVEQAREAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 83 FDAYVAVGGGSTMDTCKAANLYASSPHSdfldyVNAPIGKGKpVSVPLKPLIAVPTTSGTGSETTGVAIF-DYEHlkVKT 161
Cdd:cd08193 84 ADGVIGFGGGSSMDVAKLVALLAGSDQP-----LDDIYGVGK-ATGPRLPLILVPTTAGTGSEVTPISIVtTGET--EKK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 162 GIASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTalpyhmrspcpsnpiTRpayQGSNPISDIWAIHALRI 241
Cdd:cd08193 156 GVVSPQLLPDVALLDAELTLGLPPHVTAATGIDAMVHAIEAYT---------------SR---HKKNPISDALAREALRL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 242 VAKYLKRAVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakdynvdhplVPHGLSVVLTSPAVF 321
Cdd:cd08193 218 LGANLRRAVEDGSDLEAREAMLLGSMLAGQAFANAPVAAVHALAYPLGGHFH-------------VPHGLSNALVLPHVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 322 SFTAQMSPERHLETAEILGADTHTARIPDAGPILADTLRKFLFDLDVDDGLASIGYSKADIPALVKGTLPQERVTKLAPR 401
Cdd:cd08193 285 RFNLPAAEALYAELARALLPGLAFGSDAAAAEAFIDALEELVEASGLPTRLRDVGVTEEDLPMLAEDAMKQTRLLVNNPR 364
|
410
....*....|...
gi 1333704659 402 PQSEEDLSALFEA 414
Cdd:cd08193 365 EVTEEDALAIYQA 377
|
|
| Fe-ADH-like |
cd08183 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
6-413 |
1.70e-54 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contain different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341462 [Multi-domain] Cd Length: 377 Bit Score: 185.01 E-value: 1.70e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 6 IRYGAGVTKEVGMDLQNMGaKNVCLMTDKNLSQLPPVQVVMDSLVKNGINFKVYDNVRvEPTDRSFMEAIEFAKKGAFDA 85
Cdd:cd08183 4 IVFGRGSLQELGELAAELG-KRALLVTGRSSLRSGRLARLLEALEAAGIEVALFSVSG-EPTVETVDAAVALAREAGCDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 86 YVAVGGGSTMDTCKAANLYASSPHS--DFLDYVnapiGKGKPVSVPLKPLIAVPTtsgtgsettgVA-----------IF 152
Cdd:cd08183 82 VIAIGGGSVIDAAKAIAALLTNEGSvlDYLEVV----GKGRPLTEPPLPFIAIPT----------TAgtgsevtknavLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 153 DYEHlKVKTGIASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTalpyhmrspcpSNpitrpayqGSNPISD 232
Cdd:cd08183 148 SPEH-GVKVSLRSPSMLPDVALVDPELTLSLPPEVTAASGLDALTQLIEPYV-----------SR--------KANPLTD 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 233 IWAIHALRIVAKYLKRAVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakdynvdhplVPHGL- 311
Cdd:cd08183 208 ALAREGLRLAARSLRRAYEDGEDLEAREDMALASLLGGLALANAGLGAVHGLAGPLGGMFG-------------APHGAi 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 312 -SVVLtsPAVFSFTAQMSPER----HLETAEILGADTHTARIPDAGPILADTLRKFLFDLDVdDGLASIGYSKADIPALV 386
Cdd:cd08183 275 cAALL--PPVLEANLRALRERepdsPALARYRELAGILTGDPDAAAEDGVEWLEELCEELGI-PRLSEYGLTEEDFPEIV 351
|
410 420
....*....|....*....|....*..
gi 1333704659 387 KGTLpQERVTKLAPRPQSEEDLSALFE 413
Cdd:cd08183 352 EKAR-GSSSMKGNPIELSDEELLEILE 377
|
|
| HEPD |
cd08182 |
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde ... |
4-413 |
1.71e-52 |
|
Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP); Hydroxyethylphosphoate dehydrogenase (HEPD) catalyzes the reduction of phosphonoacetaldehyde (PnAA) to hydroxyethylphosphoate (HEP) with either NADH or NADPH as a cofactor, although NADH is the preferred cofactor. PnAA is a biosynthetic intermediate for several phosphonates such as the antibiotic fosfomycin, phosphinothricin tripeptide (PTT), and 2-aminoethylphosphonate (AEP). This enzyme is named PhpC in PTT biosynthesis pathway in Streptomyces hygroscopicus and S. viridochromogenes.
Pssm-ID: 341461 [Multi-domain] Cd Length: 370 Bit Score: 179.73 E-value: 1.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 4 SNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQVVMDSLvKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAF 83
Cdd:cd08182 2 VKIIFGPGALAELKDLLGGLGARRVLLVTGPSAVRESGAADILDAL-GGRIPVVVFSDFSPNPDLEDLERGIELFRESGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 84 DAYVAVGGGSTMDTCKAANLYASSPHSDFLdyvnAPIGKGKPVSVPLKPLIAVPTtsgtgsettgVA-----------IF 152
Cdd:cd08182 81 DVIIAVGGGSVIDTAKAIAALLGSPGENLL----LLRTGEKAPEENALPLIAIPT----------TAgtgsevtpfatIW 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 153 DyEHLKVKTGIASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTALpyhmrspcpsnpitrpayqGSNPISD 232
Cdd:cd08182 147 D-EAEGKKYSLAHPSLYPDAAILDPELTLSLPLYLTASTGLDALSHAIESIWSV-------------------NANPESR 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 233 IWAIHALRIVAKYLKRAVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISglvktykaKDYNvdhplVPHGLS 312
Cdd:cd08182 207 AYALRAIRLILENLPLLLENLPNLEAREAMAEASLLAGLAISITKTTAAHAISYPLT--------SRYG-----VPHGHA 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 313 VVLTSPAVFSFTAQ-----MSPERHLETAEILGADThtaripdaGPILADTLRKFLFDLDVDDGLASIGYSKADIPALVK 387
Cdd:cd08182 274 CALTLPAVLRYNAGaddecDDDPRGREILLALGASD--------PAEAAERLRALLESLGLPTRLSEYGVTAEDLEALAA 345
|
410 420
....*....|....*....|....*.
gi 1333704659 388 GTLPQERVtKLAPRPQSEEDLSALFE 413
Cdd:cd08182 346 SVNTPERL-KNNPVRLSEEDLLRLLE 370
|
|
| NADPH_BDH |
cd08179 |
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in ... |
20-414 |
7.08e-49 |
|
NADPH-dependent butanol dehydrogenase involved in the butanol and ethanol formation pathway in bacteria; NADPH-dependent butanol dehydrogenase (BDH) is involved in the butanol and ethanol formation pathway of some bacteria. The fermentation process is characterized by an acid producing growth phase, followed by a solvent producing phase. The latter phase is associated with the induction of solventogenic enzymes such as butanol dehydrogenase. The activity of the enzyme requires NADPH as cofactor, as well as divalent ions zinc or iron. This family is a member of the iron-containing alcohol dehydrogenase superfamily. Protein structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341458 [Multi-domain] Cd Length: 379 Bit Score: 170.45 E-value: 7.08e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 20 LQNMGAKNVCLMTDKN-LSQLPPVQVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAFDAYVAVGGGSTMDTC 98
Cdd:cd08179 18 LKTLKGKRAFIVTGGGsMKRNGFLDKVEDYLKEAGMEVKVFEGVEPDPSVETVEKGAEAMREFEPDWIIAIGGGSVIDAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 99 KAANLYASSPHSDFLDYVnapigkgKPVSVPLKP----LIAVPTTSGTGSETTGVAIF-DYEHlKVKTGIASRAIKPTLG 173
Cdd:cd08179 98 KAMWVFYEYPELTFEDAL-------VPFPLPELRkkarFIAIPSTSGTGSEVTRASVItDTEK-GIKYPLASFEITPDVA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 174 LIDPLHTLHMPDRVVANSGFDVLCHALESYTAlpyhmrspcpsnpiTRPayqgsNPISDIWAIHALRIVAKYLKRAVRNP 253
Cdd:cd08179 170 ILDPELTMTMPPHVTANTGMDALTHAIEAYVS--------------TLA-----NDFTDALALGAILDIFENLPKSYNGG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 254 DDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakdynvdhplVPHGL--SVVLtsPAVFSFTAQMSPER 331
Cdd:cd08179 231 KDLEAREKMHNASCLAGMAFSNSGLGIVHSMAHKGGAFFG-------------IPHGLanAILL--PYVIEFNSKDPEAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 332 HLETAEILGADTHtaripDAGPILADTLRKFLFDLDVDDGLASIGYS----KADIPALVKGTLpQERVTKLAPRPQSEED 407
Cdd:cd08179 296 ARYAALLIGLTDE-----ELVEDLIEAIEELNKKLGIPLSFKEAGIDedefFAKLDEMAENAM-NDACTGTNPRKPTVEE 369
|
....*..
gi 1333704659 408 LSALFEA 414
Cdd:cd08179 370 MKELLKA 376
|
|
| Fe-ADH-like |
cd08186 |
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol ... |
8-416 |
1.92e-44 |
|
Iron-containing alcohol dehydrogenase; This family contains iron-containing alcohol dehydrogenase (ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. The ADH of hyperthermophilic archaeon Thermococcus hydrothermalis oxidizes a series of primary aliphatic and aromatic alcohols, preferentially from C2 to C8, but is also active towards methanol and glycerol, and is stereospecific for monoterpenes. It has been suggested that the type III ADHs in microorganisms are involved in acetaldehyde detoxication rather than in alcohol turnover.
Pssm-ID: 341465 [Multi-domain] Cd Length: 380 Bit Score: 158.58 E-value: 1.92e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 8 YGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPV-QVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAFDAY 86
Cdd:cd08186 6 FGVGAIAKIKDILKDLGIDKVIIVTGRSSYKKSGAwDDVEKALEENGIEYVVYDKVTPNPTVDQADEAAKLARDFGADAV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 87 VAVGGGSTMDTCKAANLYASSPHS---DFLDYVNAPIGKgkpvsvplKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGI 163
Cdd:cd08186 86 IAIGGGSPIDTAKSVAVLLAYGGKtarDLYGFRFAPERA--------LPLVAINLTHGTGSEVDRFAVATIPEKGYKPGI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 164 ASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTALpyhmrspcpsnpitrpayqGSNPISDIWAIHALRIVA 243
Cdd:cd08186 158 AYDCIYPLYAIDDPRLTLTLPKEQTLYTSIDAFNHVYEAATTK-------------------VSSPYVITLAKEAIRLIA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 244 KYLKRAVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLVktykakdynvdhPLVPHGLSVVLTSPAVFSF 323
Cdd:cd08186 219 EYLPRALANPKDLEARYWLLYASMIAGIAIDNGLLHLTHALEHPLSGLK------------PELPHGLGLALLGPAVVKY 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 324 TAQMSPErhlETAEILGA-DTHTARIPDAGPILADTLRKFLFDLDVDDGLASIGYSKADIPALVK---GTLPQERVTKLA 399
Cdd:cd08186 287 IYKAVPE---TLADILRPiVPGLKGTPDEAEKAARGVEEFLFSVGFTEKLSDYGFTEDDVDRLVElafTTPSLDLLLSLA 363
|
410
....*....|....*..
gi 1333704659 400 PRPQSEEDLSALFEASM 416
Cdd:cd08186 364 PVEVTEEVVREIYEESL 380
|
|
| PPD-like |
cd08181 |
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1, ... |
5-343 |
5.97e-44 |
|
1,3-propanediol dehydrogenase-like (PPD); This family contains proteins similar to 1,3-propanediol dehydrogenase (PPD) which is a member of the iron-containing alcohol dehydrogenase superfamily, and exhibits a dehydroquinate synthase-like fold. Protein sequence similarity search and other biochemical evidences suggest that they are close to the iron-containing 1,3-propanediol dehydrogenase (EC 1.1.1.202). 1,3-propanediol dehydrogenase catalyzes the oxidation of propane-1,3-diol to 3-hydroxypropanal with the simultaneous reduction of NADP+ to NADPH. The protein structure of Thermotoga maritima TM0920 gene contains one NADP+ and one iron ion.
Pssm-ID: 341460 [Multi-domain] Cd Length: 358 Bit Score: 156.59 E-value: 5.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 5 NIRYGAGVTKEVGMDLQNMGaKNVCLMT-----DKNLSQlppvQVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAK 79
Cdd:cd08181 6 KVYFGKNCVEKHADELAALG-KKALIVTgkhsaKKNGSL----DDVTEALEENGIEYFIFDEVEENPSIETVEKGAELAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 80 KGAFDAYVAVGGGSTMDTCKAANLYASSPHSDFLDYvnapigKGKPVSVPLkPLIAVPTTSGTGSETTGVAIFDYEHLKV 159
Cdd:cd08181 81 KEGADFVIGIGGGSPLDAAKAIALLAANKDGDEDLF------QNGKYNPPL-PIVAIPTTAGTGSEVTPYSILTDHEKGT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 160 KTGIASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTAlpyhmrspcpsnpiTRpayqgSNPISDIWAIHAL 239
Cdd:cd08181 154 KKSFGNPLIFPKLALLDPKYTLSLPEELTIDTAVDALSHAIEGYLS--------------VK-----ATPLSDALALEAL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 240 RIVAKYLKRAVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPIsglvkTYKaKDynvdhplVPHGLSVVLTSPA 319
Cdd:cd08181 215 RLIGECLPNLLGDELDEEDREKLMYASTLAGMVIAQTGTTLPHGLGYPL-----TYF-KG-------IPHGRANGILLPA 281
|
330 340
....*....|....*....|....
gi 1333704659 320 VFSFTAQMSPERHLETAEILGADT 343
Cdd:cd08181 282 YLKLCEKQEPEKVDKILKLLGFGS 305
|
|
| PDD |
cd08180 |
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) ... |
20-413 |
2.11e-43 |
|
1,3-propanediol dehydrogenase (PPD) catalyzes the reduction of 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol in glycerol metabolism; 1,3-propanediol dehydrogenase (PPD) plays a role in glycerol metabolism of some bacteria in anaerobic conditions. In this degradation pathway, glycerol is converted in a two-step process to 1,3-propanediol (1,3-PD) which is then excreted into the extracellular medium. The first reaction involves the transformation of glycerol into 3-hydroxypropionaldehyde (3-HPA) by a coenzyme B-12-dependent dehydratase. The second reaction involves the dismutation of the 3-hydroxypropionaldehyde (3-HPA) to 1,3-propanediol by the NADH-linked 1,3-propanediol dehydrogenase (PPD). The enzyme requires iron ion for its function. Because many genes in this pathway are present in the propanediol utilization (pdu) operon, they are also named pdu genes. PPD is a member of the iron-containing alcohol dehydrogenase superfamily. The PPD structure has a dehydroquinate synthase-like fold.
Pssm-ID: 341459 [Multi-domain] Cd Length: 333 Bit Score: 154.57 E-value: 2.11e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 20 LQNMGAKNVCLMTDKNLSQLPPVQVVMDSLvKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAFDAYVAVGGGSTMDTCK 99
Cdd:cd08180 17 LKELKGKRVFIVTDPFMVKSGMVDKVTDEL-DKSNEVEIFSDVVPDPSIEVVAKGLAKILEFKPDTIIALGGGSAIDAAK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 100 AANLYassphsdfldYVNAPIGKGKPvsvplkPLIAVPTTSGTGSETTGVA-IFDYEHlKVKTGIASRAIKPTLGLIDPL 178
Cdd:cd08180 96 AIIYF----------ALKQKGNIKKP------LFIAIPTTSGTGSEVTSFAvITDPEK-GIKYPLVDDSMLPDIAILDPE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 179 HTLHMPDRVVANSGFDVLCHALESYTALpyhmrspcpsnpitrpayqGSNPISDIWAIHALRIVAKYLKRAVRNPDDLEA 258
Cdd:cd08180 159 LVKSVPPKVTADTGMDVLTHALEAYVST-------------------NANDFTDALAEKAIKLVFENLPRAYRDGDDLEA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 259 RSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakdynvdhplVPHGLSVVLTSPAVFSFtaqmsperhletaei 338
Cdd:cd08180 220 REKMHNASCMAGIAFNNAGLGINHSLAHALGGRFH-------------IPHGRANAILLPYVIEF--------------- 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333704659 339 lgadthtaripdagpiLADTLRKFLFDLDVDDGLASIGYSKAD----IPALVKGTLpQERVTKLAPRPQSEEDLSALFE 413
Cdd:cd08180 272 ----------------LIAAIRRLNKKLGIPSTLKELGIDEEEfekaIDEMAEAAL-ADRCTATNPRKPTAEDLIELLR 333
|
|
| PRK10624 |
PRK10624 |
L-1,2-propanediol oxidoreductase; Provisional |
8-416 |
9.88e-42 |
|
L-1,2-propanediol oxidoreductase; Provisional
Pssm-ID: 182595 [Multi-domain] Cd Length: 382 Bit Score: 151.30 E-value: 9.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 8 YGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIE-FAKKGAfDAY 86
Cdd:PRK10624 13 FGRGAIGALTDEVKRRGFKKALIVTDKTLVKCGVVAKVTDVLDAAGLAYEIYDGVKPNPTIEVVKEGVEvFKASGA-DYL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 87 VAVGGGSTMDTCKAANLYASSPhsDFLDYVN----APIGKgkpvsvPLKPLIAVPTTS-GTGSETTGVAIFDYEHLKVKT 161
Cdd:PRK10624 92 IAIGGGSPQDTCKAIGIISNNP--EFADVRSlegvAPTKK------PSVPIIAIPTTAgTAAEVTINYVITDEEKRRKFV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 162 GIASRAIkPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYtalpyhmrspcpsnpITRPAYqgsnPISDIWAIHALRI 241
Cdd:PRK10624 164 CVDPHDI-PQVAFVDADMMDSMPPGLKAATGVDALTHAIEGY---------------ITRGAW----ALTDMLHLKAIEI 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 242 VAKYLKRAVRNpdDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakdYNvdhplVPHGLSVVLTSPAVF 321
Cdd:PRK10624 224 IAGALRGAVAG--DKEAGEGMALGQYIAGMGFSNVGLGLVHGMAHPLGAF--------YN-----TPHGVANAILLPHVM 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 322 SFTAQMSPERHLETAEILGADTHTARIPDAGPILADTLRKFLFDLDVDDGLASIGYSKADIPALVKGTLpQERVTKLAPR 401
Cdd:PRK10624 289 EYNADFTGEKYRDIARAMGVKVEGMSLEEARNAAVEAVKALNRDVGIPPHLRDVGVKEEDIPALAQAAF-DDVCTGGNPR 367
|
410
....*....|....*
gi 1333704659 402 PQSEEDLSALFEASM 416
Cdd:PRK10624 368 EATLEDIVELYKKAW 382
|
|
| Fe-ADH-like |
cd08189 |
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol ... |
9-387 |
5.88e-41 |
|
Iron-containing alcohol dehydrogenases-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and belongs to the alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domain. Proteins of this family have not been characterized.
Pssm-ID: 341468 [Multi-domain] Cd Length: 378 Bit Score: 149.16 E-value: 5.88e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 9 GAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAFDAYVA 88
Cdd:cd08189 11 GAGSLLQLPEALKKLGIKRVLIVTDKGLVKLGLLDPLLDALKKAGIEYVVFDGVVPDPTIDNVEEGLALYKENGCDAIIA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 89 VGGGSTMDTCKAANLYASSPHSDFLDYVnapiGKGKpVSVPLKPLIAVPTTSGTGSETTGVA-IFDYEHlKVKTGIASRA 167
Cdd:cd08189 91 IGGGSVIDCAKVIAARAANPKKSVRKLK----GLLK-VRKKLPPLIAVPTTAGTGSEATIAAvITDPET-HEKYAINDPK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 168 IKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTALPYhmrspcpsnpitrpayqgsNPISDIWAIHALRIVAKYLK 247
Cdd:cd08189 165 LIPDAAVLDPELTLGLPPAITAATGMDALTHAVEAYISRSA-------------------TKETDEYALEAVKLIFENLP 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 248 RAVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakdYNvdhplVPHGL--SVVLtsPAVFSFTA 325
Cdd:cd08189 226 KAYEDGSDLEARENMLLASYYAGLAFTRAYVGYVHAIAHQLGGL--------YG-----VPHGLanAVVL--PHVLEFYG 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333704659 326 QMSPERHLETAEILGADTHTARIPDAGPILADTLRKFLFDLDVDDGLASIgySKADIPALVK 387
Cdd:cd08189 291 PAAEKRLAELADAAGLGDSGESDSEKAEAFIAAIRELNRRMGIPTTLEEL--KEEDIPEIAK 350
|
|
| AAD_C |
cd08178 |
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol ... |
23-381 |
1.33e-40 |
|
C-terminal alcohol dehydrogenase domain of the acetaldehyde dehydrogenase-alcohol dehydrogenase bifunctional two-domain protein (AAD); This alcohol dehydrogenase domain is located on the C-terminal of a bifunctional two-domain protein. The N-terminal of the protein contains an acetaldehyde-CoA dehydrogenase domain. This protein is involved in pyruvate metabolism whereby pyruvate is converted to acetyl-CoA and formate by pyruvate formate-lysase (PFL). Under anaerobic condition, acetyl-CoA is reduced to acetaldehyde and ethanol by this two-domain protein. Acetyl-CoA is first converted into an enzyme-bound thiohemiacetal by the N-terminal acetaldehyde dehydrogenase domain. The enzyme-bound thiohemiacetal is subsequently reduced by the C-terminal NAD+-dependent alcohol dehydrogenase domain. In E. coli, this protein is called AdhE and has been shown to have pyruvate formate-lyase (PFL) deactivase activity, which leads to the inactivation of PFL, a key enzyme in anaerobic metabolism. In Escherichia coli and Entamoeba histolytica, this enzyme forms homopolymeric peptides composed of more than 20 protomers associated in a helical rod-like structure.
Pssm-ID: 341457 [Multi-domain] Cd Length: 400 Bit Score: 148.87 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 23 MGAKNVCLMTDKNLSQLPPVQVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKkgAF--DAYVAVGGGSTMDTCKA 100
Cdd:cd08178 21 PGVKRAFIVTDRVLYKLGYVDKVLDVLEARGVETEVFSDVEPDPTLSTVRKGLEAMN--AFkpDVIIALGGGSAMDAAKI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 101 ANLYASSPHSDFLD------------YVNAPIGKGKPvsvplkpLIAVPTTSGTGSETTGVA-IFDyEHLKVKTGIASRA 167
Cdd:cd08178 99 MWLFYEHPETKFEDlaqrfmdirkrvYKFPKLGKKAK-------LVAIPTTSGTGSEVTPFAvITD-DKTGKKYPLADYA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 168 IKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTalpyhmrSPCpsnpitrpayqgSNPISDIWAIHALRIVAKYLK 247
Cdd:cd08178 171 LTPDMAIVDPELVMTMPKRLTADTGIDALTHAIEAYV-------SVM------------ASDYTDGLALQAIKLIFEYLP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 248 RAVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGlvkTYKakdynvdhplVPHGLSVVLTSPAVFSFTAQM 327
Cdd:cd08178 232 RSYNNGNDIEAREKMHNAATIAGMAFANAFLGICHSLAHKLGA---AFH----------IPHGRANAILLPHVIRYNATD 298
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 328 SP---------------ERHLETAEILGADTHTariPDAG-PILADTLRKFLFDLDVDDGLASIGYSKAD 381
Cdd:cd08178 299 PPtkqaafpqykyyvakERYAEIADLLGLGGKT---PEEKvESLIKAIEDLKKDLGIPTSIREAGIDEAD 365
|
|
| Fe-ADH-like |
cd14864 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
4-414 |
4.32e-40 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341486 [Multi-domain] Cd Length: 376 Bit Score: 146.68 E-value: 4.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 4 SNIRYGAGVTKEVGMDLQNMGAKNVcLMTDKNLSQLPPVQVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAF 83
Cdd:cd14864 5 PNIVFGADSLERIGEEVKEYGSRFL-LITDPVLKESGLADKIVSSLEKAGISVIVFDEIPASATSDTIDEAAELARKAGA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 84 DAYVAVGGGSTMDTCKAANLYASSPHsDFLDYVNAPIGKGKPVsvplkPLIAVPTTSGTGSETTGVAIF-DYEHLKVKTg 162
Cdd:cd14864 84 DGIIAVGGGKVLDTAKAVAILANNDG-GAYDFLEGAKPKKKPL-----PLIAVPTTPRSGFEFSDRFPVvDSRSREVKL- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 163 IASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTAlpyhmrspcpsnpitrpayQGSNPISDIWAIHALRIV 242
Cdd:cd14864 157 LKAQPGLPKAVIVDPNLMASLTGNQTAAMALAALALAVEAYLS-------------------KKSNFFSDALALKAIELV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 243 AKYLKRAVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakdYNVDHPLVphgLSVVLtsPAVFS 322
Cdd:cd14864 218 SENLDGALADPKNTPAEELLAQAGCLAGLAASSSSPGLATALALAVNSR--------YKVSKSLV---ASILL--PHVIE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 323 FTAQMSPERHLETAEILGADTHTARIPDAGPILADTLRKFLFDLDVDDGLASIGyskadipalVKGTLPQ-------ERV 395
Cdd:cd14864 285 YAATSAPDKYAKIARALGEDVEGASPEEAAIAAVEGVRRLIAQLNLPTRLKDLD---------LASSLEQlaaiaedAPK 355
|
410
....*....|....*....
gi 1333704659 396 TKLAPRPQSEEDLSALFEA 414
Cdd:cd14864 356 LNGLPRSMSSDDIFDILKA 374
|
|
| BDH |
cd08187 |
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor ... |
6-413 |
1.54e-36 |
|
Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process; The butanol dehydrogenase (BDH) is involved in the final step of the butanol formation pathway in anaerobic micro-organism. Butanol dehydrogenase catalyzes the conversion of butyraldehyde to butanol with the cofactor NAD(P)H being oxidized in the process. Activity in the reverse direction is 50-fold lower than that in the forward direction. The NADH-BDH has higher activity with longer chained aldehydes and is inhibited by metabolites containing an adenine moiety. This protein family belongs to the so-called iron-containing alcohol dehydrogenase superfamily. Since members of this superfamily use different divalent ions, preferentially iron or zinc, it has been suggested to be renamed to family III metal-dependent polyol dehydrogenases. This family also includes E. coli YqhD enzyme, an NADP-dependent dehydrogenase whose activity measurements with several alcohols demonstrate preference for alcohols longer than C3. The active site of YqhD contains a Zn metal, and a modified NADPH cofactor bearing OH groups on the saturated C5 and C6 atoms, possibly due to oxygen stress on the enzyme, which would functionally work under anaerobic conditions.
Pssm-ID: 341466 [Multi-domain] Cd Length: 382 Bit Score: 137.18 E-value: 1.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 6 IRYGAGVTKEVGMDLQNMGaKNVCLMTDKN-------LSQlppvqvVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFA 78
Cdd:cd08187 10 IIFGKGAIEELGEEIKKYG-KKVLLVYGGGsikknglYDR------VVASLKEAGIEVVEFGGVEPNPRLETVREGIELA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 79 KKGAFDAYVAVGGGSTMDTCKAANLYASSPHsDFLDYVNapigKGKPVSVPLkPLIAVPTTSGTGSETTGVAIFDYEHLK 158
Cdd:cd08187 83 REENVDFILAVGGGSVIDAAKAIAAGAKYDG-DVWDFFT----GKAPPEKAL-PVGTVLTLAATGSEMNGGAVITNEETK 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 159 VKTGIASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYtalpyhmrspcpsnpITRPayqGSNPISDIWAIHA 238
Cdd:cd08187 157 EKLGFGSPLLRPKFSILDPELTYTLPKYQTAAGIVDIFSHVLEQY---------------FTGT---EDAPLQDRLAEGL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 239 LRIVAKYLKRAVRNPDDLEARSNMHLASAFA--GI-GFGNAGVHLCHGMSYPISGLvktykakdYNVDHplvPHGLSVVL 315
Cdd:cd08187 219 LRTVIENGPKALKDPDDYEARANLMWAATLAlnGLlGAGRGGDWATHAIEHELSAL--------YDITH---GAGLAIVF 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 316 tsPAVFSFTAQMSPERHLETAE-ILGADT--HTARIPDAGpILAdtLRKFLFDLDVDDGLASIGYSKADIPALVKGTLPQ 392
Cdd:cd08187 288 --PAWMRYVLKKKPERFAQFARrVFGIDPggDDEETALEG-IEA--LEEFFKSIGLPTTLSELGIDEEDIEEMAEKAVRG 362
|
410 420
....*....|....*....|.
gi 1333704659 393 ERVTKlAPRPQSEEDLSALFE 413
Cdd:cd08187 363 GGLGG-GFKPLTREDIEEILK 382
|
|
| PRK13805 |
PRK13805 |
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional |
23-381 |
5.60e-33 |
|
bifunctional acetaldehyde-CoA/alcohol dehydrogenase; Provisional
Pssm-ID: 237515 [Multi-domain] Cd Length: 862 Bit Score: 131.46 E-value: 5.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 23 MGAKNVCLMTDKNLSQLPPVQVVMDSL--VKNGINFKVYDNVRVEPTdrsfmeaIEFAKKGA-----F--DAYVAVGGGS 93
Cdd:PRK13805 478 DGKKRAFIVTDRFMVELGYVDKVTDVLkkRENGVEYEVFSEVEPDPT-------LSTVRKGAelmrsFkpDTIIALGGGS 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 94 TMDTCKAANLYASSPHSDFLD------------YVNAPIG-KGKPVSVP--------LKPlIAVpttsgtgsettgvaIF 152
Cdd:PRK13805 551 PMDAAKIMWLFYEHPETDFEDlaqkfmdirkriYKFPKLGkKAKLVAIPttsgtgseVTP-FAV--------------IT 615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 153 DyEHLKVKTGIASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTALpyhMrspcpsnpitrpayqgSNPISD 232
Cdd:PRK13805 616 D-DKTGVKYPLADYELTPDVAIVDPNLVMTMPKSLTADTGIDALTHALEAYVSV---M----------------ASDYTD 675
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 233 IWAIHALRIVAKYLKRAVRN-PDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKtykakdynvdhplVPHGL 311
Cdd:PRK13805 676 GLALQAIKLVFEYLPRSYKNgAKDPEAREKMHNASTIAGMAFANAFLGICHSMAHKLGAEFH-------------IPHGR 742
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 312 SVVLTSPAVFSFTAQ--------------MSPERHLETAEILGADTHTariPDAG-PILADTLRKFLFDLDVDDGLASIG 376
Cdd:PRK13805 743 ANAILLPHVIRYNATdppkqaafpqyeypRADERYAEIARHLGLPGST---TEEKvESLIKAIEELKAELGIPMSIKEAG 819
|
....*
gi 1333704659 377 YSKAD 381
Cdd:PRK13805 820 VDEAD 824
|
|
| PRK15454 |
PRK15454 |
ethanolamine utilization ethanol dehydrogenase EutG; |
9-415 |
3.29e-32 |
|
ethanolamine utilization ethanol dehydrogenase EutG;
Pssm-ID: 185351 [Multi-domain] Cd Length: 395 Bit Score: 125.91 E-value: 3.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 9 GAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAFDAYVA 88
Cdd:PRK15454 33 GPGAVSSCGQQAQTRGLKHLFVMADSFLHQAGMTAGLTRSLAVKGIAMTLWPCPVGEPCITDVCAAVAQLRESGCDGVIA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 89 VGGGSTMDTCKAANLYASSPHSDFLDYVNapigkgKPVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAI 168
Cdd:PRK15454 113 FGGGSVLDAAKAVALLVTNPDSTLAEMSE------TSVLQPRLPLIAIPTTAGTGSETTNVTVIIDAVSGRKQVLAHASL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 169 KPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTALpyhmrspcpsnpitrpayqGSNPISDIWAIHALRIVAKYLKR 248
Cdd:PRK15454 187 MPDVAILDAALTEGVPSHVTAMTGIDALTHAIEAYSAL-------------------NATPFTDSLAIGAIAMIGKSLPK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 249 AVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSY-PISGLvktykakdynvdHplVPHGLSVVLTSPAVFSFTAQM 327
Cdd:PRK15454 248 AVGYGHDLAARESMLLASCMAGMAFSSAGLGLCHAMAHqPGAAL------------H--IPHGLANAMLLPTVMEFNRMV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 328 SPERHLEtaeiLGADTHTARIPDAGPILAdtLRKFLFDLDVDDGLASIGYSKADIPALVKGTLpQERVTKLAPRPQSEED 407
Cdd:PRK15454 314 CRERFSQ----IGRALRTKKSDDRDAINA--VSELIAEVGIGKRLGDVGATSAHYGAWAQAAL-EDICLRSNPRTASLEQ 386
|
....*...
gi 1333704659 408 LSALFEAS 415
Cdd:PRK15454 387 IVGLYAAA 394
|
|
| PRK09860 |
PRK09860 |
putative alcohol dehydrogenase; Provisional |
9-416 |
1.09e-30 |
|
putative alcohol dehydrogenase; Provisional
Pssm-ID: 182118 [Multi-domain] Cd Length: 383 Bit Score: 121.60 E-value: 1.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 9 GAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQVVMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAFDAYVA 88
Cdd:PRK09860 15 GADSLTDAMNMMADYGFTRTLIVTDNMLTKLGMAGDVQKALEERNIFSVIYDGTQPNPTTENVAAGLKLLKENNCDSVIS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 89 VGGGSTMDTCKAANLYASSpHSDFLDYvnapigKGKPVSV-PLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRA 167
Cdd:PRK09860 95 LGGGSPHDCAKGIALVAAN-GGDIRDY------EGVDRSAkPQLPMIAINTTAGTASEMTRFCIITDEARHIKMAIVDKH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 168 IKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTALpyhmrspcpsnpitrpayqGSNPISDIWAIHALRIVAKYLK 247
Cdd:PRK09860 168 VTPLLSVNDSSLMIGMPKSLTAATGMDALTHAIEAYVSI-------------------AATPITDACALKAVTMIAENLP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 248 RAVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGLvktykakdYNvdhplVPHGLSVVLTSPAVFSFTAQM 327
Cdd:PRK09860 229 LAVEDGSNAKAREAMAYAQFLAGMAFNNASLGYVHAMAHQLGGF--------YN-----LPHGVCNAVLLPHVQVFNSKV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 328 SPERHLETAEILGADTHTARIPDAGPILADTLRKFLFDLDVDDGLASIGYSKADIPALVKGTLpQERVTKLAPRPQSEED 407
Cdd:PRK09860 296 AAARLRDCAAAMGVNVTGKNDAEGAEACINAIRELAKKVDIPAGLRDLNVKEEDFAVLATNAL-KDACGFTNPIQATHEE 374
|
....*....
gi 1333704659 408 LSALFEASM 416
Cdd:PRK09860 375 IVAIYRAAM 383
|
|
| Fe-ADH-like |
cd14866 |
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing ... |
6-414 |
7.47e-29 |
|
iron-containing alcohol dehydrogenases (Fe-ADH)-like; This family contains iron-containing alcohol dehydrogenase (Fe-ADH) which catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron ions. The protein structure represents a dehydroquinate synthase-like fold and is a member of the iron-activated alcohol dehydrogenase-like family. It is distinct from other alcohol dehydrogenases which contains different protein domains. Proteins of this family have not been characterized.
Pssm-ID: 341488 [Multi-domain] Cd Length: 384 Bit Score: 116.18 E-value: 7.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 6 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVqvvMDsLVKNGINFK---VYDNVRVEPTDRSFMEAIEFAKKGA 82
Cdd:cd14866 8 LFSGRGALARLGRELDRLGARRALVVCGSSVGANPDL---MD-PVRAALGDRlagVFDGVRPHSPLETVEAAAEALREAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 83 FDAYVAVGGGSTMDTCKAANLYASSPhSDFLDYVNAPIGKGKPVS----VPLKPLIAVPTTSGTGSETTGVAIFDYEHLK 158
Cdd:cd14866 84 ADAVVAVGGGSAIVTARAASILLAED-RDVRELCTRRAEDGLMVSprldAPKLPIFVVPTTPTTADVKAGSAVTDPPAGQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 159 vKTGIASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALES-YTAlpyhmrspcpsnpitrpayqGSNPISDIWAIH 237
Cdd:cd14866 163 -RLALFDPKTRPAAVFYDPELLATAPASLVAGAAMNGFDMAVEGlYSR--------------------HADPLADATLMH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 238 ALRIVAKYLKRAVrNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGlvktykakDYNVDHPLVpHglSVVLts 317
Cdd:cd14866 222 ALRLLADGLPRLA-DDDDPAARADLVLAAVLAGYGTDHTGGGVIHALGHAIGA--------RYGVQNGVV-H--AILL-- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 318 PAVFSFTAQMSPERHLETAEILGADTHTAriPDAGPILADTLRKFLFDLDVDDGLASIGYSKADIPALVKGTLpQERVTK 397
Cdd:cd14866 288 PHVLRFNAPATDGRLDRLAEALGVADAGD--EASAAAVVDAVEALLDALGVPTRLRDLGVSREDLPAIAEAAM-DDWFMD 364
|
410
....*....|....*...
gi 1333704659 398 LAPRPQSE-EDLSALFEA 414
Cdd:cd14866 365 NNPRPVPTaEELEALLEA 382
|
|
| 4HBD_NAD |
cd14860 |
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes ... |
65-419 |
9.01e-28 |
|
4-hydroxybutyrate dehydrogenase, also called gamma-hydroxybutyrate dehydrogenase, catalyzes the reduction of succinic simialdehyde to 4-hydroxybutyrate in the succinic degradation pathway; 4-hydroxybutyrate dehydrogenase (4HBD) is an iron-containing (type III) NAD-dependent alcohol dehydrogenase. It plays a role in the succinate metabolism biochemical pathway. It catalyzes the reduction of succinic simialdehide to 4-hydroxybutyrate in the succinate degradation pathway This succinate degradation pathway is present in some bacteria which can use succinate as sole carbon source.
Pssm-ID: 341482 Cd Length: 371 Bit Score: 113.08 E-value: 9.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 65 EPTDRSFMEAIEFAKKGAFDAYVAVGGGSTMDTCKaanLYASSPHSDFLDYV--NAPIGKGKPvsvplkpLIAVPTTSGT 142
Cdd:cd14860 61 EPSDEMVEAIYKDIKKYGYKRVIAIGGGTVIDIAK---LLALKGISPVLDLFdgKIPLIKEKE-------LIIVPTTCGT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 143 GSETTGVAIFDYEHLKVKTGIASRAIKPTLGLIDP--LHTLhmPDRVVANSGFDVLCHALESYTalpyhmrSPcpsnpit 220
Cdd:cd14860 131 GSEVTNISIVELTSLGTKKGLAVDELYADKAVLIPelLKGL--PYKVFATSSIDALIHAIESYL-------SP------- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 221 rpayqGSNPISDIWAIHALR-IVAKYLKRAVRNPDDL-EARSNMHLASAFAGIGFGNAGVHLCHGMSYPISGlvkTYKak 298
Cdd:cd14860 195 -----KATPYTEMFSYKAIEmILEGYQEIAEKGEEARfPLLGDFLIASNYAGIAFGNAGCAAVHALSYPLGG---KYH-- 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 299 dynvdhplVPHGLS--VVLTspAVFSFTAQMSPERHLET-----AEILGADTHTAripdagpilADTLRKFLFDLDVDDG 371
Cdd:cd14860 265 --------VPHGEAnyAVFT--GVLKNYQEKNPDGEIKKlneflAKILGCDEEDV---------YDELEELLNKILPKKP 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1333704659 372 LASIGYSKADIPALVKGTLP-QERVTKLAPRPQSEEDLSALFeasMKLY 419
Cdd:cd14860 326 LHEYGMKEEEIDEFADSVMEnQQRLLANNYVPLDREDVAEIY---KELY 371
|
|
| MAR-like |
cd08192 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
6-414 |
1.82e-26 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase (MAR) catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer. It is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341471 [Multi-domain] Cd Length: 380 Bit Score: 109.65 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 6 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVqvVMDslVKNGINFK---VYDNVRVEPTDRSFMEAIEFAKKGA 82
Cdd:cd08192 4 VSYGPGAVEALLHELATLGASRVFIVTSKSLATKTDV--IKR--LEEALGDRhvgVFSGVRQHTPREDVLEAARAVREAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 83 FDAYVAVGGGSTMDTCKAANLYASSPHSDFLDYVNAPIGKGKPVSV--PLKPLIAVPTTSGTGSETTGVAIFDyEHLKVK 160
Cdd:cd08192 80 ADLLVSLGGGSPIDAAKAVALALAEDVTDVDQLDALEDGKRIDPNVtgPTLPHIAIPTTLSGAEFTAGAGATD-DDTGHK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 161 TGIASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYtalpYHMRSpcpsnpitrpayqgsNPISDIWAIHALR 240
Cdd:cd08192 159 QGFAHPELGPDAVILDPELTLHTPERLWLSTGIRAVDHAVETL----CSPQA---------------TPFVDALALKALR 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 241 IVAKYLKRAVRNPDDLEARSNMHLASAFAGIGFGN-AGVHLCHGMSYPISGLvktykakdYNvdhplVPHGLSVVLTSPA 319
Cdd:cd08192 220 LLFEGLPRSKADPEDLEARLKCQLAAWLSLFGLGSgVPMGASHAIGHQLGPL--------YG-----VPHGITSCIMLPA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 320 VFSFTAQMSPERHLETAEILGADTHTARIPDAgpILADTLRKFLFDLDVDDGLASIGYSKADIPALVKGTLPQERVTKLA 399
Cdd:cd08192 287 VLRFNAPVNAERQRLIARALGLVTGGLGREAA--DAADAIDALIRELGLPRTLRDVGVGRDQLEKIAENALTDVWCRTNP 364
|
410
....*....|....*
gi 1333704659 400 PRPQSEEDLSALFEA 414
Cdd:cd08192 365 RPITDKDDVLEILES 379
|
|
| YqdH |
COG1979 |
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion]; |
45-416 |
3.49e-24 |
|
Alcohol dehydrogenase YqhD, Fe-dependent ADH family [Energy production and conversion];
Pssm-ID: 441582 [Multi-domain] Cd Length: 387 Bit Score: 103.23 E-value: 3.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 45 VMDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAFDAYVAVGGGSTMDTCK---AANLYAssphSDFLDYVNapig 121
Cdd:COG1979 51 VKAALKEAGIEVVEFGGVEPNPRLETVRKGVELCKEEGIDFILAVGGGSVIDGAKaiaAGAKYD----GDPWDILT---- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 122 KGKPVSVPLkPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALE 201
Cdd:COG1979 123 GKAPVEKAL-PLGTVLTLPATGSEMNSGSVITNEETKEKLGFGSPLVFPKFSILDPELTYTLPKRQTANGIVDIFSHVME 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 202 SYtalpyhmrspcpsnpITRPAYqgsNPISDIWAIHALRIVAKYLKRAVRNPDDLEARSNMHLASAFAGIGFGNAGVH-- 279
Cdd:COG1979 202 QY---------------FTYPVD---APLQDRFAEGLLRTLIEEGPKALKDPEDYDARANLMWAATLALNGLIGAGVPqd 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 280 -LCHGMSYPISGLvktykakdYNVDHplvPHGLSVVLtsPAVFSFTAQMSPERHLETAE-ILGADTHT--ARIpDAGpil 355
Cdd:COG1979 264 wATHMIEHELSAL--------YDIDH---GAGLAIVL--PAWMRYVLEEKPEKFAQYAErVWGITEGDdeERA-LEG--- 326
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333704659 356 ADTLRKFLFDLDVDDGLASIGYSKADIPALVKGTLPQERVTKLAPRPQSEEDLSALFEASM 416
Cdd:COG1979 327 IEATEEFFESLGLPTRLSEYGIDEEDIEEMAEKATAHGMTALGEFKDLTPEDVREILELAL 387
|
|
| MAR |
cd08177 |
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic ... |
6-414 |
7.55e-19 |
|
Maleylacetate reductase is involved in many aromatic compounds degradation pathways of aerobic microbes; Maleylacetate reductase (MAR) plays an important role in the degradation of aromatic compounds in aerobic microbes. In fungi and yeasts, the enzyme is involved in the catabolism of compounds such as phenol, tyrosine, benzoate, 4-hydroxybenzoate and resorcinol. In bacteria, the enzyme contributes to the degradation of resorcinol, 2,4-dihydroxybenzoate ([beta]-resorcylate) and 2,6-dihydroxybenzoate ([gamma]-resorcylate) via hydroxyquinol and maleylacetate. Maleylacetate reductase catalyzes NADH- or NADPH-dependent reduction, at the carbon-carbon double bond, of maleylacetate or 2-chloromaleylacetate to 3-oxoadipate. In the case of 2-chloromaleylacetate, MAR initially catalyzes the NAD(P)H-dependent dechlorination to maleylacetate, which is then reduced to 3-oxoadipate. This enzyme is a homodimer and is inhibited by thiol-blocking reagents such as p-chloromercuribenzoate and Hg++, indicating that the cysteine residue is probably necessary for the catalytic activity of maleylacetate reductase.
Pssm-ID: 341456 [Multi-domain] Cd Length: 337 Bit Score: 86.79 E-value: 7.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 6 IRYGAGVTKEVGMDLQNMGAKNVCLMTDKnlSQLPPVQVVMDSLVKNGINfkVYDNVR----VEPTDRsfmeAIEFAKKG 81
Cdd:cd08177 4 VVFGAGTLAELAEELERLGARRALVLSTP--RQRALAERVAALLGDRVAG--VFDGAVmhvpVEVAER----ALAAAREA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 82 AFDAYVAVGGGSTmdtckaanlyassphsdfldyvnapIGKGKPVSVPLK-PLIAVPTTSgtgsettgvA------IFDY 154
Cdd:cd08177 76 GADGLVAIGGGSA-------------------------IGLAKAIALRTGlPIVAVPTTY---------AgsemtpIWGE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 155 EHLKVKTGIASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESYTAlpyhmrspcpsnpitrpayQGSNPISDIW 234
Cdd:cd08177 122 TEDGVKTTGRDPRVLPRTVIYDPDLTLGLPAALSVASGLNALAHAVEALYA-------------------PDANPITSLL 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 235 AIHALRIVAKYLKRAVRNPDDLEARSNMHLASAFAGIGFGNAG--VH--LCH--GMSYpisGLvktykakdynvdhplvP 308
Cdd:cd08177 183 AEEGIRALARALPRLVADPSDLEARSDALYGAWLAGVVLGSVGmgLHhkLCHvlGGTF---DL----------------P 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 309 HGL--SVVLtsPAVFSFTAQMSPERHLETAEILGADThtaripdagpiLADTLRKFLFDLDVDDGLASIGYSKADIPALV 386
Cdd:cd08177 244 HAEthAVVL--PHVLAYNAPAAPDAMARLARALGGGD-----------AAGGLYDLARRLGAPTSLRDLGMPEDDIDRAA 310
|
410 420 430
....*....|....*....|....*....|.
gi 1333704659 387 kgtlpqERVTKLA---PRPQSEEDLSALFEA 414
Cdd:cd08177 311 ------DLALANPypnPRPVERDALRALLER 335
|
|
| PRK15138 |
PRK15138 |
alcohol dehydrogenase; |
45-398 |
5.33e-10 |
|
alcohol dehydrogenase;
Pssm-ID: 185092 [Multi-domain] Cd Length: 387 Bit Score: 60.58 E-value: 5.33e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 45 VMDSLvkNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAFDAYVAVGGGSTMDTCK----AANLYASSPHSDFLDYVNAPI 120
Cdd:PRK15138 50 VLDAL--KGMDVLEFGGIEPNPTYETLMKAVKLVREEKITFLLAVGGGSVLDGTKfiaaAANYPENIDPWHILETGGKEI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 121 GKGkpvsVPLKPLIAVPTTSGTGSETtgvAIFDYEHLKVKTGIASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHAL 200
Cdd:PRK15138 128 KSA----IPMGSVLTLPATGSESNAG---AVISRKTTGDKQAFHSPHVQPVFAVLDPVYTYTLPPRQVANGVVDAFVHTV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 201 ESYTALPYHMRspcpsnpitrpayqgsnpISDIWAIHALRIVAKYLKRAVRNPDDLEARSNMHLASAFAGIGFGNAGVH- 279
Cdd:PRK15138 201 EQYVTYPVDAK------------------IQDRFAEGILLTLIEEGPKALKEPENYDVRANVMWAATQALNGLIGAGVPq 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 280 --LCHGMSYPISGLvktykakdYNVDHplvPHGLSVVLtsPAVFSFTAQMSPERHLETAEI---LGADTHTARIPDAgpi 354
Cdd:PRK15138 263 dwATHMLGHELTAM--------HGLDH---AQTLAIVL--PALWNEKRDTKRAKLLQYAERvwnITEGSDDERIDAA--- 326
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1333704659 355 LADTlRKFLFDLDVDDGLASIGYSKADIPALVKgTLPQERVTKL 398
Cdd:PRK15138 327 IAAT-RNFFEQMGVPTRLSDYGLDGSSIPALLK-KLEEHGMTQL 368
|
|
| DHQ_Fe-ADH |
cd07766 |
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); ... |
5-201 |
9.39e-10 |
|
Dehydroquinate synthase-like (DHQ-like) and iron-containing alcohol dehydrogenases (Fe-ADH); This superfamily consists of two subgroups: the dehydroquinate synthase (DHQS)-like, and a large metal-containing alcohol dehydrogenases (ADH), known as iron-containing alcohol dehydrogenases. Dehydroquinate synthase (DHQS) catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate-7-phosphate (DAHP) to dehydroquinate (DHQ) in the second step of the shikimate pathway. This pathway involves seven sequential enzymatic steps in the conversion of erythrose 4-phosphate and phosphoenolpyruvate into chorismate for subsequent synthesis of aromatic compounds. Dehydroquinate synthase-like group includes dehydroquinate synthase, 2-deoxy-scyllo-inosose synthase, and 2-epi-5-epi-valiolone synthase. The alcohol dehydrogenases (ADHs) in this superfamily contain a dehydroquinate synthase-like protein structural fold and mostly contain iron. They are distinct from other alcohol dehydrogenases which contains different protein domains. There are several distinct families of alcohol dehydrogenases: Zinc-containing long-chain alcohol dehydrogenases; insect-type, or short-chain alcohol dehydrogenases; iron-containing alcohol dehydrogenases, and others. The iron-containing family has a Rossmann fold-like topology that resembles the fold of the zinc-dependent alcohol dehydrogenases, but lacks sequence homology, and differs in strand arrangement. ADH catalyzes the reversible oxidation of alcohol to acetaldehyde with the simultaneous reduction of NAD(P)+ to NAD(P)H.
Pssm-ID: 341447 [Multi-domain] Cd Length: 271 Bit Score: 58.91 E-value: 9.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 5 NIRYGAGVTKEVGMDLQNMGAKnVCLMTDKNLSQLPPVQVvmDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAFD 84
Cdd:cd07766 3 RIVFGEGAIAKLGEIKRRGFDR-ALVVSDEGVVKGVGEKV--ADSLKKGLAVAIFDFVGENPTFEEVKNAVERARAAEAD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 85 AYVAVGGGSTMDTCKAANLyassphsdfldyvnapigkgkpVSVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIA 164
Cdd:cd07766 80 AVIAVGGGSTLDTAKAVAA----------------------LLNRGIPFIIVPTTASTDSEVSPKSVITDKGGKNKQVGP 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 1333704659 165 srAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALE 201
Cdd:cd07766 138 --HYNPDVVFVDTDITKGLPPRQVASGGVDALAHAVE 172
|
|
| Fe-ADH_2 |
pfam13685 |
Iron-containing alcohol dehydrogenase; |
7-285 |
4.96e-07 |
|
Iron-containing alcohol dehydrogenase;
Pssm-ID: 404557 [Multi-domain] Cd Length: 251 Bit Score: 50.76 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 7 RYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQVVmDSLVKNGINFKVYDNVRVEPTDRSFMEAIEFAKKGAFDAY 86
Cdd:pfam13685 1 VIGPGALGRLGEYLAELGFRRVALVADANTYAAAGRKVA-ESLKRAGIEVETRLEVAGNADMETAEKLVGALRERDADAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 87 VAVGGGSTMDTCKAA----NL-YASSP----HSDFLDYvNAPI-GKGKPVSVPLKPLIAVpttsgtgsettgvaIFDyeh 156
Cdd:pfam13685 80 VGVGGGTVIDLAKYAafklGKpFISVPtaasNDGFASP-GASLtVDGKKRSIPAAAPFGV--------------IAD--- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 157 lkvkTGIASRAikptlglidplhtlhmPDRVVAnSGF-DvlchALESYTALPYHMRSpcpsnpitrpayqGSNPISDIWA 235
Cdd:pfam13685 142 ----TDVIAAA----------------PRRLLA-SGVgD----LLAKITAVADWELA-------------HAEEVAAPLA 183
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1333704659 236 IHALRIVAKYLKRAVRNPDDLEARSNMHLASAFAGIGFGNAGVHLCHGMS 285
Cdd:pfam13685 184 LLSAAMVMNFADRPLRDPGDIEALAELLSALAMGGAGSSRPASGSEHLIS 233
|
|
| G1PDH-like |
cd08174 |
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like ... |
4-136 |
3.49e-06 |
|
Glycerol-1-phosphate dehydrogenase-like; These glycerol-1-phosphate dehydrogenase-like proteins have not been characterized. The protein sequences have high similarity with that of glycerol-1-phosphate dehydrogenase (G1PDH) which plays a role in the synthesis of phosphoglycerolipids in Gram-positive bacterial species. It catalyzes the reversibly reduction of dihydroxyacetone phosphate (DHAP) to glycerol-1-phosphate (G1P) in a NADH-dependent manner. Its activity requires Ni++ ion.
Pssm-ID: 341453 [Multi-domain] Cd Length: 332 Bit Score: 48.67 E-value: 3.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 4 SNIRYGAGVTKEVG--MDLQNMGAKNVCLMTDKNLSQLPpVQVVMDSLVKNGINFKVYDNvrvepTDRSFMEAIEFA-KK 80
Cdd:cd08174 2 LILKIEEGALEHLGkyLADRNQGFGKVAIVTGEGIDELL-GEDILESLEEAGEIVTVEEN-----TDNSAEELAEKAfSL 75
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333704659 81 GAFDAYVAVGGGSTMDTCK-AANL----YASSPHSDFLDYVNAPI----GKGKPVSVPLKPLIAV 136
Cdd:cd08174 76 PKVDAIVGIGGGKVLDVAKyAAFLsklpFISVPTSLSNDGIASPVavlkVDGKRKSLGAKMPYGV 140
|
|
| GldA |
COG0371 |
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and ... |
4-101 |
6.96e-06 |
|
Glycerol dehydrogenase or related enzyme, iron-containing ADH family [Energy production and conversion]; Glycerol dehydrogenase or related enzyme, iron-containing ADH family is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440140 [Multi-domain] Cd Length: 355 Bit Score: 47.85 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 4 SNIRYGAGVTKEVGMDLQNMGaKNVCLMTDKNLSQL--PPVQvvmDSLVKNGINFKVYdNVRVEPTDRSFMEAIEFAKKG 81
Cdd:COG0371 7 RRYVQGEGALDELGEYLADLG-KRALIITGPTALKAagDRLE---ESLEDAGIEVEVE-VFGGECSEEEIERLAEEAKEQ 81
|
90 100
....*....|....*....|
gi 1333704659 82 AFDAYVAVGGGSTMDTCKAA 101
Cdd:COG0371 82 GADVIIGVGGGKALDTAKAV 101
|
|
| Gro1PDH |
cd08173 |
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between ... |
4-136 |
1.74e-05 |
|
Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH) catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme; Sn-glycerol-1-phosphate dehydrogenase (Gro1PDH, EC 1.1.1.261) plays an important role in the formation of the enantiomeric configuration of the glycerophosphate backbone (sn-glycerol-1-phosphate) of archaeal ether lipids. It catalyzes the reversible conversion between dihydroxyacetone phosphate and glycerol-1-phosphate using either NADH or NADPH as a coenzyme. The activity is zinc-dependent. One characteristic feature of archaea is that their cellular membrane has an ether linkage between the glycerol backbone and the hydrocarbon residues. The polar lipids of the members of Archaea consist of di- and tetra-ethers of glycerol with isoprenoid alcohols bound at the sn-2 and sn-3 positions of the glycerol moiety. The archaeal polar lipids have the enantiomeric configuration of a glycerophosphate backbone [sn-glycerol-1-phosphate (G-1-P)] that is the mirror image structure of the bacterial or eukaryal counterpart [sn-glycerol- 3-phosphate (G-3-P)]. The absolute stereochemistry of the glycerol moiety in all archaeal polar lipids is opposite to that of glycerol ester lipids in bacteria and eukarya.
Pssm-ID: 341452 Cd Length: 343 Bit Score: 46.39 E-value: 1.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 4 SNIRYGAGVTKEVGMDLQNMG-AKNVCLMTDKNLSQLPpVQVVMDSLVKNGINFKVYDNVRVEpTDRSFMEAIEFAKKGA 82
Cdd:cd08173 3 RNVVVGHGAINKIGEVLKKLLlGKRALIITGPNTYKIA-GKRVEDLLESSGVEVVIVDIATIE-EAAEVEKVKKLIKESK 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333704659 83 FDAYVAVGGGSTMDTCK--AANL---YASSPHSDFLDYVNAP----IGKGKPVSVPLKPLIAV 136
Cdd:cd08173 81 ADFIIGVGGGKVIDVAKyaAYKLnlpFISIPTSASHDGIASPfasiKGGDKPYSIKAKAPIAI 143
|
|
| Fe-ADH_KdnB-like |
cd08184 |
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N ... |
3-339 |
1.45e-04 |
|
Iron-containing alcohol dehydrogenase similar to Shewanella oneidensis KdnB required for Kdo8N biosynthesis; This family contains iron-containing alcohol dehydrogenase-like proteins, many of which have not been characterized. Their specific function is unknown. The protein structure represents a dehydroquinate synthase-like fold and belongs to the iron-containing alcohol dehydrogenase-like superfamily. It is distinct from other alcohol dehydrogenases which contain different protein domains. Alcohol dehydrogenase catalyzes the reduction of acetaldehyde to alcohol with NADP as cofactor. Its activity requires iron or zinc ions. This family also includes Shewanella oneidensis KdnB which is required for biosynthesis of 8-Amino-3,8-dideoxy-D-manno-octulosonic acid (Kdo8N), a unique amino sugar that has thus far only been observed on the lipopolysaccharides of marine bacteria belonging to the genus Shewanella, and thought to be important for the integrity of the bacterial cell outer membrane. KdnB requires NAD(P) and zinc ion for activity.
Pssm-ID: 341463 [Multi-domain] Cd Length: 348 Bit Score: 43.80 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 3 VSNIRYGAGVTKEVGMDLQNMGAKN---VCLMTDKNLSQLPpvqvVMDSLVKNGINFKVYDNVRVEPT----DrSFMEAI 75
Cdd:cd08184 1 VPKYLFGRGSFDQLGELLAERRKSNndyVVFFIDDVFKGKP----LLDRLPLQNGDLLIFVDTTDEPKtdqiD-ALRAQI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 76 EFAKKGAFDAYVAVGGGSTMDTCKA-ANLYA---SSPHSDFLDYVnapigKGKPVsvplkPLIAVPTTSGTGSETTGVAI 151
Cdd:cd08184 76 RAENDKLPAAVVGIGGGSTMDIAKAvSNMLTnpgSAADYQGWDLV-----KNPGI-----YKIGVPTLSGTGAEASRTAV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 152 FDYEHLKVktGIASRAIKPTLGLIDPLHTLHMPDRVVANSGFDVLCHALESytaLPYHMRspcpsnpitrpayqgsNPIS 231
Cdd:cd08184 146 LTGPEKKL--GINSDYTVFDQVILDPELIATVPRDQYFYTGMDCYIHCVES---LNGTYR----------------NAFG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 232 DIWAIHALRIVAK-YLKRAVRNPDDLEarsNMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKTykakdynvdhplvPHG 310
Cdd:cd08184 205 DAYAEKALELCRDvFLSDDMMSPENRE---KLMVASYLGGSSIANSQVGVCHALSYGLSVVLGT-------------HHG 268
|
330 340
....*....|....*....|....*....
gi 1333704659 311 LSVVLtspaVFSFTAQMSPERHLETAEIL 339
Cdd:cd08184 269 VANCI----VFNVLEEFYPEGVKEFREML 293
|
|
| GlyDH |
cd08170 |
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in ... |
7-108 |
2.67e-04 |
|
Glycerol dehydrogenases (GlyDH) catalyzes oxidation of glycerol to dihydroxyacetone in glycerol dissmilation; Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site.
Pssm-ID: 341449 [Multi-domain] Cd Length: 351 Bit Score: 42.78 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 7 RY--GAGVTKEVGMDLQNMGaKNVCLMTDKNLsqLPPV-QVVMDSLVKNGINFkVYDNVRVEPTDRSFMEAIEFAKKGAF 83
Cdd:cd08170 3 RYvqGPGALDRLGEYLAPLG-KKALVIADPFV--LDLVgERLEESLEKAGLEV-VFEVFGGECSREEIERLAAIARANGA 78
|
90 100
....*....|....*....|....*
gi 1333704659 84 DAYVAVGGGSTMDTCKAANLYASSP 108
Cdd:cd08170 79 DVVIGIGGGKTIDTAKAVADYLGLP 103
|
|
| GlyDH-like |
cd08550 |
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. ... |
7-101 |
3.74e-03 |
|
Glycerol_dehydrogenase-like; This family contains glycerol dehydrogenase (GlyDH)-like proteins. Glycerol dehydrogenases (GlyDH) is a key enzyme in the glycerol dissimilation pathway. In anaerobic conditions, many microorganisms utilize glycerol as a source of carbon through coupled oxidative and reductive pathways. One of the pathways involves the oxidation of glycerol to dihydroxyacetone with the reduction of NAD+ to NADH catalyzed by glycerol dehydrogenases. Dihydroxyacetone is then phosphorylated by dihydroxyacetone kinase and enters the glycolytic pathway for further degradation. The activity of GlyDH is zinc-dependent; the zinc ion plays a role in stabilizing an alkoxide intermediate at the active site. Some subfamilies have yet to be characterized.
Pssm-ID: 341480 [Multi-domain] Cd Length: 347 Bit Score: 39.06 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333704659 7 RY--GAGVTKEVGMDLQNMGaKNVCLMTDKN-LSQLppVQVVMDSLVKNGINFKVYDNvRVEPTDRSFMEAIEFAKKGAF 83
Cdd:cd08550 3 RYiqEPGILAKAGEYIAPLG-KKALIIGGKTaLEAV--GEKLEKSLEEAGIDYEVEVF-GGECTEENIERLAEKAKEEGA 78
|
90
....*....|....*...
gi 1333704659 84 DAYVAVGGGSTMDTCKAA 101
Cdd:cd08550 79 DVIIGIGGGKVLDTAKAV 96
|
|
| |
