|
Name |
Accession |
Description |
Interval |
E-value |
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
49-508 |
0e+00 |
|
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439884 [Multi-domain] Cd Length: 461 Bit Score: 929.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 49 SFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEV 127
Cdd:COG0114 3 ETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGG--ERMPREFIRALALIKKAAARANAELGlLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 128 AEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVL 207
Cdd:COG0114 81 IAGKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 208 LPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRI 287
Cdd:COG0114 161 LPALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 288 GFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSI 367
Cdd:COG0114 241 GFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 368 MPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINK 447
Cdd:COG0114 321 MPGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19743875 448 LMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLG 508
Cdd:COG0114 401 LLERSLMLVTALNPHIGYDKAAKIAKKAHKEGRTLREAALELGLLSEEEFDRLVDPEKMTG 461
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
49-510 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 928.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 49 SFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEV 127
Cdd:PRK00485 3 ETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGG--ERMPRELIRALALLKKAAARVNAELGlLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 128 AEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVL 207
Cdd:PRK00485 81 IAGKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 208 LPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRI 287
Cdd:PRK00485 161 LPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 288 GFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSI 367
Cdd:PRK00485 241 GFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 368 MPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINK 447
Cdd:PRK00485 321 MPGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19743875 448 LMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 510
Cdd:PRK00485 401 LLERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPG 463
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
51-506 |
0e+00 |
|
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial fumarase, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.
Pssm-ID: 176465 [Multi-domain] Cd Length: 455 Bit Score: 914.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 51 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAE 129
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGG--ERMPRELIRALGLLKKAAAQANAELGlLDEEKADAIVQAADEVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 130 GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLP 209
Cdd:cd01362 79 GKLDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQERLLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 210 GLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGF 289
Cdd:cd01362 159 ALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 290 AEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMP 369
Cdd:cd01362 239 AEKVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMP 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 370 GKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLM 449
Cdd:cd01362 319 GKVNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 19743875 450 NESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDM 506
Cdd:cd01362 399 ERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRLVDPEKM 455
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
57-509 |
0e+00 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 852.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 57 FGELKVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDH 135
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGGERERMPEPIVRAFGIVKKAAAKVNMEYGlLDPDIGKAIMQAADEVAEGKLDDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 136 FPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLH 215
Cdd:PLN00134 81 FPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATEIHSRLIPALKELH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 216 DALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAA 295
Cdd:PLN00134 161 ESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 296 KVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPT 375
Cdd:PLN00134 241 AVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 376 QCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLML 455
Cdd:PLN00134 321 QCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLML 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 19743875 456 VTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGP 509
Cdd:PLN00134 401 VTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTGP 454
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
51-502 |
0e+00 |
|
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains aspartase (L-aspartate ammonia-lyase), fumarase class II enzymes, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.
Pssm-ID: 176468 [Multi-domain] Cd Length: 450 Bit Score: 836.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 51 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAE 129
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISG--ERMPPELIRALALVKKAAALANAELGlLDEEKADAIVQACDEVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 130 GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGsKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLP 209
Cdd:cd01596 79 GKLDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKG-KYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 210 GLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGF 289
Cdd:cd01596 158 ALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 290 AEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMP 369
Cdd:cd01596 238 AEKVAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 370 GKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLM 449
Cdd:cd01596 318 GKVNPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 19743875 450 NESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVK 502
Cdd:cd01596 398 ENSLMLVTALNPHIGYEKAAEIAKEALKEGRTLREAALELGLLTEEELDEILD 450
|
|
| fumC_II |
TIGR00979 |
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ... |
50-508 |
0e+00 |
|
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium tuberculosis, Streptomyces coelicolor, Pseudomonas aeruginosa) branch deeply, although within the same branch of a phylogenetic tree rooted by aspartate ammonia-lyase sequences, and score between the trusted and noise cutoffs. [Energy metabolism, TCA cycle]
Pssm-ID: 130052 [Multi-domain] Cd Length: 458 Bit Score: 824.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 50 FRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGgvTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVA 128
Cdd:TIGR00979 1 FRIEKDSMGEIQVPADKYWGAQTQRSLENFKIG--TEKMPLELIHAFAILKKAAAIVNEDLGkLDAKKADAIVQAADEIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 129 EGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLL 208
Cdd:TIGR00979 79 AGKLDDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKNQLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 209 PGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIG 288
Cdd:TIGR00979 159 PALENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 289 FAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIM 368
Cdd:TIGR00979 239 FDEKVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 369 PGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKL 448
Cdd:TIGR00979 319 PGKVNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQL 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 449 MNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLG 508
Cdd:TIGR00979 399 LNNSLMLVTALNPHIGYDNAAKIAKKAHKEGITLKEAALELGLLSEEEFDEWVVPEQMVG 458
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
51-509 |
0e+00 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 616.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 51 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAE 129
Cdd:PRK12425 3 RTETDSLGPIEVPEDAYWGAQTQRSLINFAIGK--ERMPLAVLHALALIKKAAARVNDRNGdLPADIARLIEQAADEVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 130 GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLP 209
Cdd:PRK12425 81 GQHDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVHEQLLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 210 GLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGF 289
Cdd:PRK12425 161 AIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 290 AEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMP 369
Cdd:PRK12425 241 AEAIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 370 GKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLM 449
Cdd:PRK12425 321 GKVNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHL 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 450 NESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGP 509
Cdd:PRK12425 401 ERGLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEA 460
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
51-510 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 605.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 51 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAE 129
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPISDHPELIRALAMVKKAAALANRELGlLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 130 GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAaIEVHEVLLP 209
Cdd:COG1027 81 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLAL-LLLLRELLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 210 GLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGF 289
Cdd:COG1027 160 ALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 290 AEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMP 369
Cdd:COG1027 240 IELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 370 GKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLM 449
Cdd:COG1027 320 GKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYV 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19743875 450 NESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 510
Cdd:COG1027 400 ENSIGLVTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGLLTEEELDEILDPENMTGPG 460
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
48-510 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 582.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 48 NSFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADE 126
Cdd:PRK12273 3 MNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKISDYPELIRALAMVKKAAALANKELGlLDEEKADAIVAACDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 127 VAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAaIEVHEV 206
Cdd:PRK12273 83 ILAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIAL-LLSLRK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 207 LLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTR 286
Cdd:PRK12273 162 LLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLNAP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 287 IGFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSS 366
Cdd:PRK12273 242 PGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAGSS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 367 IMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERIN 446
Cdd:PRK12273 322 IMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEERCR 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19743875 447 KLMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 510
Cdd:PRK12273 402 EYVENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTHPG 465
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
51-499 |
0e+00 |
|
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), Bacillus aspartase and related proteins. It is a member of the Lyase class I family, which includes both aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid.
Pssm-ID: 176462 [Multi-domain] Cd Length: 450 Bit Score: 575.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 51 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAE 129
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISG--LKIHPELIRALAMVKKAAALANAELGlLDEEKAEAIVKACDEIIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 130 GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAaIEVHEVLLP 209
Cdd:cd01357 79 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLAL-ILLLRKLLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 210 GLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGF 289
Cdd:cd01357 158 ALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 290 AEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMP 369
Cdd:cd01357 238 IELVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 370 GKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLM 449
Cdd:cd01357 318 GKVNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 19743875 450 NESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDE 499
Cdd:cd01357 398 ENSIGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELDE 447
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
47-510 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 560.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 47 QNSFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVteRMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAAD 125
Cdd:PRK13353 2 NKNMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGY--KIHPELIRAFAQVKKAAALANADLGlLPRRIAEAIVQACD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 126 EVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHE 205
Cdd:PRK13353 80 EILAGKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLLEG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 206 vLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNT 285
Cdd:PRK13353 160 -LLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 286 RIGFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGS 365
Cdd:PRK13353 239 DPEYIERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 366 SIMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERI 445
Cdd:PRK13353 319 SIMPGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERC 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19743875 446 NKLMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 510
Cdd:PRK13353 399 KEYVEKSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMTHPG 463
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
51-509 |
2.12e-151 |
|
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a number of other lyases, as modeled by pfam00206. Fumarate hydratase scores as high as 570 bits against this model. [Energy metabolism, Amino acids and amines]
Pssm-ID: 213564 [Multi-domain] Cd Length: 468 Bit Score: 440.81 E-value: 2.12e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 51 RIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAE 129
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKISDIPEFVRGMVMVKKAAALANKELGtIPESIANAIVAACDEILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 130 -GKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAaIEVHEVLL 208
Cdd:TIGR00839 81 nGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIAV-YSSLIKLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 209 PGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIG 288
Cdd:TIGR00839 160 DAINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 289 FAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIM 368
Cdd:TIGR00839 240 YSPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 369 PGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKL 448
Cdd:TIGR00839 320 PAKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGY 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19743875 449 MNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGP 509
Cdd:TIGR00839 400 VFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLMHP 460
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
58-389 |
1.24e-146 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 422.55 E-value: 1.24e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 58 GELKVPNDKYYGAQTVRSTMNFKIGGVTermptpvIKAFGILKRAAAEVNQDYgldPKIANAIMKAADEVAE-GKLNDHF 136
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEED-------IKGLAALKKAAAKANVIL---KEEAAAIIKALDEVAEeGKLDDQF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 137 PLVVWQTGSGTQTNMNVNEVISnraiEMLGgelgskIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHD 216
Cdd:pfam00206 71 PLKVWQEGSGTAVNMNLNEVIG----ELLG------QLVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLID 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 217 ALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPR-IYELAAGGTAVGTGLNTRIGFAEKVAA 295
Cdd:pfam00206 141 ALKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPRlLVLPLGGGTAVGTGLNADPEFAELVAK 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 296 KVAALTGLPfVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPrSGLGELILPENEPGSSIMPGKVNPT 375
Cdd:pfam00206 221 ELGFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPD 298
|
330
....*....|....
gi 19743875 376 QCEAMTMVAAQVMG 389
Cdd:pfam00206 299 QLELLTGKAGRVMG 312
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
47-509 |
1.54e-145 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 426.34 E-value: 1.54e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 47 QNSFRIEYDTFGELKVPNDKYYGAQTVRSTMNFKIGGVteRMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAAD 125
Cdd:PRK14515 8 KNGVRIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGY--KIHEGLIKAFAIVKKAAALANTDVGrLELNKGGAIAEAAQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 126 EVAEGKLNDHFPLVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAaIEVHE 205
Cdd:PRK14515 86 EILDGKWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIAT-LNALE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 206 VLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNT 285
Cdd:PRK14515 165 GLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 286 RIGFAEKVAAKVAALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGS 365
Cdd:PRK14515 245 DPEYIEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 366 SIMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERI 445
Cdd:PRK14515 325 SIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRL 404
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19743875 446 NKLMNESLMLVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGP 509
Cdd:PRK14515 405 KEYVEKSVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEMTHP 468
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
93-441 |
8.82e-123 |
|
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; The Lyase class I family contains class II fumarase, aspartase, adenylosuccinate lyase (ASL), argininosuccinate lyase (ASAL), prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. It belongs to the Lyase_I superfamily. Proteins of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits.
Pssm-ID: 176461 [Multi-domain] Cd Length: 325 Bit Score: 362.21 E-value: 8.82e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 93 IKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFplvvWQTGSGTQTNMNVNEVISNRAIEMlggelgs 171
Cdd:cd01334 1 IRADLQVEKAHAKALAELGlLPKEAAEAILAALDEILEGIAADQV----EQEGSGTHDVMAVEEVLAERAGEL------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 172 kipvhpNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGY 251
Cdd:cd01334 70 ------NGGYVHTGRSSNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 252 VQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAkvaaLTGLpFVTAPNKFEALAAHDALVELSGAMNTT 331
Cdd:cd01334 144 AAELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAE----LLGF-FGPAPNSTQAVSDRDFLVELLSALALL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 332 ACSLMKIANDIRFLGSGprsGLGELILPEN-EPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKP 410
Cdd:cd01334 219 AVSLSKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSP 295
|
330 340 350
....*....|....*....|....*....|.
gi 19743875 411 MMIKNVLHSARLLGDASVSFTENCvVGIQAN 441
Cdd:cd01334 296 VEREALPDSFDLLDAALRLLTGVL-EGLEVN 325
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
151-431 |
2.79e-64 |
|
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase, which catalyze similar beta-elimination reactions; Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively.
Pssm-ID: 176466 [Multi-domain] Cd Length: 231 Bit Score: 208.62 E-value: 2.79e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 151 MNVNEVISNRAIEMLGGELGSKipvhpndHVNKSQSSNDtFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIK 230
Cdd:cd01594 14 ALVEEVLAGRAGELAGGLHGSA-------LVHKGRSSND-IGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 231 IGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAmpriyelaaggtavgtglntrigfaekvaakvaaltglpfvtapn 310
Cdd:cd01594 86 PGRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEA--------------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 311 kfealaahdALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPeNEPGSSIMPGKVNPTQCEAMTMVAAQVMGN 390
Cdd:cd01594 121 ---------AVAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGN 190
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 19743875 391 HVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFT 431
Cdd:cd01594 191 LVAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
455-506 |
6.81e-28 |
|
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to L-malate as part of the Kreb's cycle. The full-length protein forms a tetramer with visible globular shape. FumaraseC_C is the C-terminal 65 residues referred to as domain 3. The core of the molecule consists of a bundle of 20 alpha-helices from the five-helix bundle of domain 2. The projections from the core of the tetramer are generated from domains 1 and 3 of each subunit. FumaraseC_C does not appear to be part of either the active site or the activation site but is helical in structure forming a little bundle.
Pssm-ID: 463083 [Multi-domain] Cd Length: 52 Bit Score: 105.48 E-value: 6.81e-28
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 19743875 455 LVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDM 506
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
202-508 |
8.42e-26 |
|
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439786 [Multi-domain] Cd Length: 436 Bit Score: 109.79 E-value: 8.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 202 EVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGtAVGT 281
Cdd:COG0015 113 EALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVGKIGG-AVGT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 282 GLNtrigfaekvaakvaaltglpFVTAPNKFEALAA----------------HDALVELSGAMNTTACSLMKIANDIRFL 345
Cdd:COG0015 192 YAA--------------------HGEAWPEVEERVAeklglkpnpvttqiepRDRHAELFSALALIAGSLEKIARDIRLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 346 GsgpRSGLGEL--ILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGN--HVAVTV------GGSNGHFELNVFkPMMIkn 415
Cdd:COG0015 252 Q---RTEVGEVeePFAKGQVGSSAMPHKRNPIDSENIEGLARLARALaaALLEALaswherDLSDSSVERNIL-PDAF-- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 416 vlhsarLLGDASVSFTENCVVGIQANTERINKLMNESLMLV------TALNPH-IG----YDKAAKIAKTAHKNGSTLKE 484
Cdd:COG0015 326 ------LLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVlseavlMALVRRgLGreeaYELVKELARGAWEEGNDLRE 399
|
330 340
....*....|....*....|....*....
gi 19743875 485 tAIE-----LGYLTAEQFDEWVKPKDMLG 508
Cdd:COG0015 400 -LLAadpeiPAELSKEELEALFDPANYLG 427
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
202-476 |
1.07e-24 |
|
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. These proteins are members of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). pCMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone, in the beta-ketoadipate pathway. ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.
Pssm-ID: 176467 [Multi-domain] Cd Length: 381 Bit Score: 105.66 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 202 EVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGtAVGT 281
Cdd:cd01595 103 DALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGGISG-AVGT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 282 GLNtrigFAEKVAAKVAALT---GLPFVTAPNKFEAlaaHDALVELSGAMNTTACSLMKIANDIRFLGsgpRSGLGELIL 358
Cdd:cd01595 182 HAS----LGPKGPEVEERVAeklGLKVPPITTQIEP---RDRIAELLSALALIAGTLEKIATDIRLLQ---RTEIGEVEE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 359 P--ENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNhvavtvggsnghfelnvFKPMMIKNVL-------HSA--RLLG--- 424
Cdd:cd01595 252 PfeKGQVGSSTMPHKRNPIDSENIEGLARLVRAL-----------------AAPALENLVQwherdlsDSSveRNILpda 314
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19743875 425 ----DASVSFTENCVVGIQANTERINKLMNESLMLV------TALNPH-IGYDKAAKIAKTAH 476
Cdd:cd01595 315 flllDAALSRLQGLLEGLVVNPERMRRNLDLTWGLIlseavmMALAKKgLGRQEAYELVKEEN 377
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
202-508 |
5.45e-22 |
|
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains pCLME and related proteins, and belongs to the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. CMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone in the beta-ketoadipate pathway. This pathway is responsible for the catabolism of a variety of aromatic compounds into intermediates of the citric cycle in prokaryotic and eukaryotic micro-organisms.
Pssm-ID: 176469 [Multi-domain] Cd Length: 437 Bit Score: 98.47 E-value: 5.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 202 EVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGtAVGT 281
Cdd:cd01597 113 DALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGG-AAGT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 282 -------GLNTRIGFaekvaakvAALTGLPFVTAPnkfeALAAHDALVELSGAMNTTACSLMKIANDIRFLGsgpRSGLG 354
Cdd:cd01597 192 laslgdqGLAVQEAL--------AAELGLGVPAIP----WHTARDRIAELASFLALLTGTLGKIARDVYLLM---QTEIG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 355 ELILP--ENEPGSSIMPGKVNPTQCEAMTMVAAQVMGnHVAVTV---------GGSNGHFELNVFKPMMIknvlhsarlL 423
Cdd:cd01597 257 EVAEPfaKGRGGSSTMPHKRNPVGCELIVALARRVPG-LAALLLdamvqeherDAGAWHAEWIALPEIFL---------L 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 424 GDASVSFTENCVVGIQANTERINK--------LMNESLMLvtALNPHIGYDKA----AKIAKTAHKNGSTLKETAIE--- 488
Cdd:cd01597 327 ASGALEQAEFLLSGLEVNEDRMRAnldltgglILSEAVMM--ALAPKLGRQEAhdlvYEACMRAVEEGRPLREVLLEdpe 404
|
330 340
....*....|....*....|.
gi 19743875 489 -LGYLTAEQFDEWVKPKDMLG 508
Cdd:cd01597 405 vAAYLSDEELDALLDPANYLG 425
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
180-508 |
9.71e-22 |
|
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that catalyzes step 8 in the purine biosynthesis pathway for de novo synthesis of IMP and also the final reaction in the two-step sequence from IMP to AMP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273345 [Multi-domain] Cd Length: 435 Bit Score: 97.42 E-value: 9.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 180 HVNKSQSSNDTFPTAMHIAAAiEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAM 259
Cdd:TIGR00928 90 FIHFGATSNDIVDTALALLLR-DALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 260 TRIKAAMPRIYELAAGGtAVGTGLNTRIGFAEKVAAKVAALtGLPFVTAPNKFEAlaaHDALVELSGAMNTTACSLMKIA 339
Cdd:TIGR00928 169 ERLLQAKERIKVGGISG-AVGTHAAAYPLVEEVEERVTEFL-GLKPVPISTQIEP---RDRHAELLDALALLATTLEKFA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 340 NDIRFLgsgPRSGLGEL--ILPENEPGSSIMPGKVNPTQCEAMTMVAaqVMGNHVAVTVGGSNGH-FELNVFKPMMIKNV 416
Cdd:TIGR00928 244 VDIRLL---QRTEHFEVeePFGKGQVGSSAMPHKRNPIDFENVCGLA--RVIRGYASPALENAPLwHERDLTDSSVERVI 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 417 LHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHI-------GYDKAAKIAK-----TAHKNGSTLKE 484
Cdd:TIGR00928 319 LPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIalvergmGREEAYEIVRelamgAAEVDEPDLLE 398
|
330 340
....*....|....*....|....*...
gi 19743875 485 TAIELG----YLTAEQFDEWVKPKDMLG 508
Cdd:TIGR00928 399 FLLEDEritkYLKEEELAELLDPETYIG 426
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
187-384 |
4.64e-15 |
|
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP).
Pssm-ID: 176464 [Multi-domain] Cd Length: 387 Bit Score: 76.82 E-value: 4.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 187 SNDTFPTA--MHIAAAIEVhevLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKA 264
Cdd:cd01360 91 SSDVVDTAlaLQLREALDI---ILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 265 AMPRIYELAAGGtAVGTGLNtrIGFAEKVAAKVAAltGLPFVTAPNKfeaLAAHDALVELSGAMNTTACSLMKIANDIRF 344
Cdd:cd01360 168 ARERILVGKISG-AVGTYAN--LGPEVEERVAEKL--GLKPEPISTQ---VIQRDRHAEYLSTLALIASTLEKIATEIRH 239
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 19743875 345 LgsgPRSGLGELILP--ENEPGSSIMPGKVNPTQCEAMTMVA 384
Cdd:cd01360 240 L---QRTEVLEVEEPfsKGQKGSSAMPHKRNPILSENICGLA 278
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
115-503 |
2.88e-14 |
|
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include examples of avian delta crystallins, in which argininosuccinate lyase activity may or may not be present and the biological role is to provide the optically clear cellular protein of the eye lens. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 129918 [Multi-domain] Cd Length: 455 Bit Score: 74.70 E-value: 2.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 115 KIANAIMKAADEVAEGKLNDHFPLvvwqtgsgtqtnMNVNEVISNRAIEMLGGELGSKIpvhpndHVNKSQssNDTFPTA 194
Cdd:TIGR00838 55 KIIEGLNELKEEGREGPFILDPDD------------EDIHMAIERELIDRVGEDLGGKL------HTGRSR--NDQVATD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 195 MHIAAAIEVHEvLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAA 274
Cdd:TIGR00838 115 LRLYLRDHVLE-LAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLRDYERLQDALKRVNVSPL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 275 GGTAV-GTGLntrigfaEKVAAKVAALTGLPFVTApNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPrsgL 353
Cdd:TIGR00838 194 GSGALaGTGF-------PIDREYLAELLGFDAVTE-NSLDAVSDRDFILELLFVAALIMVHLSRFAEDLILWSTGE---F 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 354 GELILP-ENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVtvggsnghfelnvfkpMMIKNVLHSA---------RLL 423
Cdd:TIGR00838 263 GFVELPdEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGM----------------LMTLKALPLAynrdlqedkEPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 424 GDaSVSFTENCV-------VGIQANTERINKLMNESLMLVTALNPHI---------GYDKAAKIAKTAHKNGSTLKETAI 487
Cdd:TIGR00838 327 FD-ALKTVELSLematgmlDTITVNKERMEEAASAGFSNATELADYLvrkgvpfreAHHIVGELVATAIERGKGLEELTL 405
|
410
....*....|....*.
gi 19743875 488 ELGYLTAEQFDEWVKP 503
Cdd:TIGR00838 406 EELQKFSPEFDEDVYE 421
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
205-389 |
1.32e-10 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 63.50 E-value: 1.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 205 EVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGtAVGTGLN 284
Cdd:PRK09053 125 DLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGG-AAGTLAS 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 285 TRIGFAEKVAAKVAALtGLPFVTAPNKfealAAHDALVELSGAMNTTACSLMKIANDIRFLgsgPRSGLGELILP--ENE 362
Cdd:PRK09053 204 LGEQALPVAQALAAEL-QLALPALPWH----TQRDRIAEFASALGLLAGTLGKIARDVSLL---MQTEVGEVFEPaaAGK 275
|
170 180
....*....|....*....|....*..
gi 19743875 363 PGSSIMPGKVNPTQCEAMTMVAAQVMG 389
Cdd:PRK09053 276 GGSSTMPHKRNPVGCAAVLTAATRAPG 302
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
194-374 |
1.73e-10 |
|
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the product of the purB gene in Escherichia coli, and related proteins. It is a member of the Lyase class I family of the Lyase_I superfamily. Members of the Lyase class I family function as homotetramers to catalyze similar beta-elimination reactions in which a Calpha-N or Calpha-O bond is cleaved with the subsequent release of fumarate as one of the products. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two non-sequential steps in the de novo purine biosynthesis pathway: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylosuccinate (SAMP) into adenosine monophosphate (AMP).
Pssm-ID: 176470 [Multi-domain] Cd Length: 425 Bit Score: 63.02 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 194 AMHIAAAIevHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKaampRIYELA 273
Cdd:cd01598 110 ALMIKEAR--NEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLK----QIEILG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 274 AGGTAVGT------------------GLNTRIGfaekvaakvaaLTGLPFVTapnkfeALAAHDALVELSGAM---NTTa 332
Cdd:cd01598 184 KFNGAVGNfnahlvaypdvdwrkfseFFVTSLG-----------LTWNPYTT------QIEPHDYIAELFDALariNTI- 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 19743875 333 csLMKIANDI------RFLGSGPRSGlgelilpenEPGSSIMPGKVNP 374
Cdd:cd01598 246 --LIDLCRDIwgyislGYFKQKVKKG---------EVGSSTMPHKVNP 282
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
205-389 |
3.72e-09 |
|
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.
Pssm-ID: 176471 [Multi-domain] Cd Length: 436 Bit Score: 58.87 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 205 EVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTaVGTG-- 282
Cdd:cd03302 113 DLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGVKGT-TGTQas 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 283 --------------LNTRI----GFaekvaAKVAALTGLpfvTAPNKFEALAAhDALVELsGAmnttacSLMKIANDIRF 344
Cdd:cd03302 192 fldlfegdhdkveaLDELVtkkaGF-----KKVYPVTGQ---TYSRKVDIDVL-NALSSL-GA------TAHKIATDIRL 255
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 19743875 345 LgsgprSGLGELILP--ENEPGSSIMPGKVNPTQCEAMTMVAAQVMG 389
Cdd:cd03302 256 L-----ANLKEVEEPfeKGQIGSSAMPYKRNPMRSERCCSLARHLMN 297
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
194-374 |
3.80e-09 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 58.61 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 194 AMHIAAAIEvhEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAmpriyELA 273
Cdd:PRK09285 132 ALMLKEARE--EVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLEAV-----EIL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 274 A--GGtAVGTgLN-------------------TRIGfaekvaakvaaLTGLPFVTA--PnkfealaaHDALVELSGAM-- 328
Cdd:PRK09285 205 GkiNG-AVGN-YNahlaaypevdwhafsrefvESLG-----------LTWNPYTTQieP--------HDYIAELFDAVar 263
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 19743875 329 -NTtacSLMKIANDI------RFLGSGPRSGlgelilpenEPGSSIMPGKVNP 374
Cdd:PRK09285 264 fNT---ILIDLDRDVwgyislGYFKQKTKAG---------EIGSSTMPHKVNP 304
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
117-396 |
6.60e-09 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 58.20 E-value: 6.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 117 ANAIMKAADEVAEGKLNDHFplvVWQTGsgtqtNMNVNEVISNRAIEMLGgELGSKIpvhpndHVNKSQssNDTFPT--A 194
Cdd:PLN02646 70 RDSILDGLDEIEKEIEAGKF---EWRPD-----REDVHMNNEARLTELIG-EPAKKL------HTARSR--NDQVATdtR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 195 MHIAAAIEVhevLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAA 274
Cdd:PLN02646 133 LWCRDAIDV---IRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 275 GGTAV-GTGLntriGFAEKVAAKVAALTGLpfvtAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPrsgL 353
Cdd:PLN02646 210 GSCALaGTGL----PIDRFMTAKDLGFTAP----MRNSIDAVSDRDFVLEFLFANSITAIHLSRLGEEWVLWASEE---F 278
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 19743875 354 GELILPEN-EPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTV 396
Cdd:PLN02646 279 GFVTPSDAvSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLA 322
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
97-459 |
6.25e-08 |
|
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASAL is a cytosolic enzyme which catalyzes the reversible breakdown of argininosuccinate to arginine and fumarate during arginine biosynthesis. In ureotelic species ASAL also catalyzes a reaction involved in the production of urea. Included in this group are the major soluble avian eye lens proteins from duck, delta 1 and delta 2 crystallin. Of these two isoforms only delta 2 has retained ASAL activity. These crystallins may have evolved by, gene recruitment of ASAL followed by gene duplication. In humans, mutations in ASAL result in the autosomal recessive disorder argininosuccinic aciduria.
Pssm-ID: 176463 [Multi-domain] Cd Length: 435 Bit Score: 54.86 E-value: 6.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 97 GILKRAAAEvnqdygldpKIANAIMKAADEVAEGKLndhfplvVWQTGSGtqtnmNVNEVISNRAIEMLGgELGSKIpvh 176
Cdd:cd01359 27 GILTEEEAA---------KILAGLAKIRAEIEAGAF-------ELDPEDE-----DIHMAIERRLIERIG-DVGGKL--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 177 pndHVNKSqsSNDTFPTAMHIAAAIEVhEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVK 256
Cdd:cd01359 82 ---HTGRS--RNDQVATDLRLYLRDAL-LELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 257 YAMTRIKAAMPRIYELAAGGTA-VGTGLN-------TRIGFAEKvaakvaaltglpfvtAPNKFEALAAHDALVELSGAM 328
Cdd:cd01359 156 RDLERLADAYKRVNVSPLGAGAlAGTTFPidrertaELLGFDGP---------------TENSLDAVSDRDFVLEFLSAA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 329 NTTACSLMKIANDIRFLGSGPRsGLGELilpeneP-----GSSIMPGKVNPTQCEAMTMVAAQVMGNHVAV--TVGG--S 399
Cdd:cd01359 221 ALLMVHLSRLAEDLILWSTQEF-GFVEL------PdaystGSSIMPQKKNPDVLELIRGKAGRVIGALAGLltTLKGlpL 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19743875 400 NGHFELNVFKPMM---IKNVLHSARLLGDasvsftenCVVGIQANTERINKLMNESLMLVTAL 459
Cdd:cd01359 294 AYNKDLQEDKEPLfdaVDTLIASLRLLTG--------VISTLTVNPERMREAAEAGFSTATDL 348
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
167-378 |
1.47e-06 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 50.94 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 167 GELGSKIpvhpndHVNKSQssNDTFPTAMHIAAAIEVHEVLLpGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQ 246
Cdd:PRK12308 97 GDLGKKL------HTGRSR--NDQVATDLKLWCRQQGQQLLL-ALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAH 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 247 EFSGYVQQVKYAMTRIKAAMPRIYELAAG-GTAVGTG-------LNTRIGFAEKVAakvaaltglpfvtapNKFEALAAH 318
Cdd:PRK12308 168 WCLAYVEMFERDYSRLEDALTRLDTCPLGsGALAGTAypidreaLAHNLGFRRATR---------------NSLDSVSDR 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19743875 319 DALVELSGAMNTTACSLMKIANDIRFLGSGpRSGLGEliLPEN-EPGSSIMPGKVNPTQCE 378
Cdd:PRK12308 233 DHVMELMSVASISMLHLSRLAEDLIFYNSG-ESGFIE--LADTvTSGSSLMPQKKNPDALE 290
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
334-508 |
4.04e-06 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 47.72 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 334 SLMKIANDIRFLgSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNhvAVTVGGSNGH-FELNVFKPMM 412
Cdd:PRK08937 29 SLEKFANEIRLL-QRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSY--LVTALENVPLwHERDLSHSSA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 413 IKNVLHSARLLGDASVSFTENCVVGIQANTERINK--------LMNESLMLvTALNPHIG----YDKAAKIAKTAHKNGS 480
Cdd:PRK08937 106 ERIALPDAFLALDYILNRFVNILENLVVFPENIERnldktlgfIATERVLL-ELVEKGMGreeaHELIREKAMEAWKNQK 184
|
170 180 190
....*....|....*....|....*....|..
gi 19743875 481 TLKETAIE----LGYLTAEQFDEWVKPKDMLG 508
Cdd:PRK08937 185 DLRELLEAderfTKQLTKEELDELFDPEAFVG 216
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
203-378 |
1.08e-05 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 47.81 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 203 VHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSgyvqQVKYAMTRIKAAMP--RIYELAAGGT--- 277
Cdd:PLN02848 142 VNSVVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMA----NFAYRLSRQRKQLSevKIKGKFAGAVgny 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 278 -------------AVGTGLNTRIGfaekvaakvaaLTGLPFVTapnkfeALAAHDALVELSGAMNTTACSLMKIANDIRF 344
Cdd:PLN02848 218 nahmsaypevdwpAVAEEFVTSLG-----------LTFNPYVT------QIEPHDYMAELFNAVSRFNNILIDFDRDIWS 280
|
170 180 190
....*....|....*....|....*....|....
gi 19743875 345 LGSgprSGLGELILPENEPGSSIMPGKVNPTQCE 378
Cdd:PLN02848 281 YIS---LGYFKQITKAGEVGSSTMPHKVNPIDFE 311
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
97-374 |
4.42e-05 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 45.91 E-value: 4.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 97 GILKRAAAEvnqdygldpKIANAIMKAADEVAEGKLndhfplvVWQTGsgtqtNMNVNEVISNRAIEMLGgELGSKIpvH 176
Cdd:PRK00855 51 GILSEEEAE---------KILAGLDEILEEIEAGKF-------EFSPE-----LEDIHMAIEARLTERIG-DVGGKL--H 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 177 P----NDHVnksqssndtfPTAMHIAAAIEVHEVLLpGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYV 252
Cdd:PRK00855 107 TgrsrNDQV----------ATDLRLYLRDEIDEIAE-LLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 253 QQVKYAMTRIKAAMPRIYELAAGGTA-VGTGLNT-------RIGFAEkvaakvaaltglpfVTApNKFEALAAHDALVEL 324
Cdd:PRK00855 176 EMLARDLERLRDARKRVNRSPLGSAAlAGTTFPIdrertaeLLGFDG--------------VTE-NSLDAVSDRDFALEF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 19743875 325 SGAMNTTACSLMKIANDIrFLGSGPRSGLGELilpeneP-----GSSIMPGKVNP 374
Cdd:PRK00855 241 LSAASLLMVHLSRLAEEL-ILWSSQEFGFVEL------PdafstGSSIMPQKKNP 288
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
167-396 |
1.87e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 43.82 E-value: 1.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 167 GELGSKIpvhpndHVNKSQssNDTFPTAMHIAAAIEVHEvLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQ 246
Cdd:PRK04833 97 GDLGKKL------HTGRSR--NDQVATDLKLWCKDQVAE-LLTALRQLQSALVETAENNQDAVMPGYTHLQRAQPVTFAH 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 247 EFSGYVQQVKYAMTRIKAAMPR--IYELAAGGTAvGTG-------LNTRIGFAEKVAakvaaltglpfvtapNKFEALAA 317
Cdd:PRK04833 168 WCLAYVEMLARDESRLQDALKRldVSPLGSGALA-GTAyeidreqLAGWLGFASATR---------------NSLDSVSD 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19743875 318 HDALVELSGAMNTTACSLMKIANDIRFLGSGpRSGLGELIlPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTV 396
Cdd:PRK04833 232 RDHVLELLSDASISMVHLSRFAEDLIFFNSG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLM 308
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
179-393 |
5.90e-04 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 41.96 E-value: 5.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 179 DHVNKSQSSNDTFPTAMHIAAaIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYA 258
Cdd:PRK05975 100 AHVHFGATSQDVIDTSLMLRL-KAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 259 MTRIKAAMPRIYELAAGGtAVGTgLNTRIGFAEKVAAKVAALTGLPfvTAPnkfEALAAHDALVELSGAMNTTACSLMKI 338
Cdd:PRK05975 179 RDRLEALRADVFPLQFGG-AAGT-LEKLGGKAAAVRARLAKRLGLE--DAP---QWHSQRDFIADFAHLLSLVTGSLGKF 251
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 19743875 339 ANDIRFLgsgprSGLGELILPENEPGSSIMPGKVNPTQCEAMTMV----AAQVMGNHVA 393
Cdd:PRK05975 252 GQDIALM-----AQAGDEISLSGGGGSSAMPHKQNPVAAETLVTLarfnATQVSGLHQA 305
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
237-389 |
9.69e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 38.67 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 237 QDAVPLTLGQefsgYVQQVKYAMTRIKAAMPRIYE------LAAGGTAvGTGLNTRIGFAEKVaakvaaltgLPFVT-AP 309
Cdd:PRK02186 565 QPALPGSLGH----YLLAVDGALARETHALFALFEhidvcpLGAGAGG-GTTFPIDPEFVARL---------LGFEQpAP 630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19743875 310 NKFEALAAHDALVELSGAMNTTACSLMKIANDIRfLGSGPRSGLgeLILPEN-EPGSSIMPGKVNPTQCEAMTMVAAQVM 388
Cdd:PRK02186 631 NSLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQ-LWTTREFAL--VSLPDAlTGGSSMLPQKKNPFLLEFVKGRAGVVA 707
|
.
gi 19743875 389 G 389
Cdd:PRK02186 708 G 708
|
|
| |
