|
Name |
Accession |
Description |
Interval |
E-value |
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
3-442 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 691.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 3 RIESDTIGSLPIYEGAYYGIHSYRAKENFAFTDQKV--DLTMIKQVARIKAAAALANQQSGTLSKEKAQIIVTAAEEIIM 80
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPIsdHPELIRALAMVKKAAALANRELGLLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 81 GKWDEEFIVDTFQGGAGTSTNMNVNEVIANRGLELMGHKKGEYQYLHPLDDVNQSQSTNDVYPSAGKLALLVYIEQLDEA 160
Cdd:COG1027 81 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLALLLLLRELLEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 161 LVQLIDRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAELLTLNMGGTAIGTGLNASYRYQ 240
Cdd:COG1027 161 LERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGYI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 241 EYLYQELNRRFPRPLRPANDLIDSTQHTDSFASISGGLKTIAITLNKSANDLRLLASGPRTGFHELNLPARQAGSSIMPG 320
Cdd:COG1027 241 ELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 321 KVNPVIPEVISQIAFQVIGNDGAITFAAASGELELNAFEPVMFHNLFESCQLLTKACQIFADKCVAGITVNETACLKAVN 400
Cdd:COG1027 321 KVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYVE 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1173256776 401 NSTGTITALSPQIGYEKATAFVKEALEKNCSIEELLKQEEFL 442
Cdd:COG1027 401 NSIGLVTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGLL 442
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
1-442 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 674.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 1 MMRIESDTIGSLPIYEGAYYGIHSYRAKENFAFTDQKVDL--TMIKQVARIKAAAALANQQSGTLSKEKAQIIVTAAEEI 78
Cdd:PRK12273 4 NTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKISDypELIRALAMVKKAAALANKELGLLDEEKADAIVAACDEI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 79 IMGKWDEEFIVDTFQGGAGTSTNMNVNEVIANRGLELMGHKKGEYQYLHPLDDVNQSQSTNDVYPSAGKLALLVYIEQLD 158
Cdd:PRK12273 84 LAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIALLLSLRKLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 159 EALVQLIDRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAELLTLNMGGTAIGTGLNASYR 238
Cdd:PRK12273 164 DALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLNAPPG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 239 YQEYLYQELNRRFPRPLRPANDLIDSTQHTDSFASISGGLKTIAITLNKSANDLRLLASGPRTGFHELNLPARQAGSSIM 318
Cdd:PRK12273 244 YIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAGSSIM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 319 PGKVNPVIPEVISQIAFQVIGNDGAITFAAASGELELNAFEPVMFHNLFESCQLLTKACQIFADKCVAGITVNETACLKA 398
Cdd:PRK12273 324 PGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEERCREY 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1173256776 399 VNNSTGTITALSPQIGYEKATAFVKEALEKNCSIEELLKQEEFL 442
Cdd:PRK12273 404 VENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLL 447
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
3-439 |
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: 670.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 3 RIESDTIGSLPIYEGAYYGIHSYRAKENFAFTDQKVDLTMIKQVARIKAAAALANQQSGTLSKEKAQIIVTAAEEIIMGK 82
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISGLKIHPELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 83 WDEEFIVDTFQGGAGTSTNMNVNEVIANRGLELMGHKKGEYQYLHPLDDVNQSQSTNDVYPSAGKLALLVYIEQLDEALV 162
Cdd:cd01357 81 LHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLALILLLRKLLDALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 163 QLIDRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAELLTLNMGGTAIGTGLNASYRYQEY 242
Cdd:cd01357 161 ALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGYIEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 243 LYQELNRRFPRPLRPANDLIDSTQHTDSFASISGGLKTIAITLNKSANDLRLLASGPRTGFHELNLPARQAGSSIMPGKV 322
Cdd:cd01357 241 VVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMPGKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 323 NPVIPEVISQIAFQVIGNDGAITFAAASGELELNAFEPVMFHNLFESCQLLTKACQIFADKCVAGITVNETACLKAVNNS 402
Cdd:cd01357 321 NPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYVENS 400
|
410 420 430
....*....|....*....|....*....|....*..
gi 1173256776 403 TGTITALSPQIGYEKATAFVKEALEKNCSIEELLKQE 439
Cdd:cd01357 401 IGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEE 437
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
3-447 |
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: 633.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 3 RIESDTIGSLPIYEGAYYGIHSYRAKENFAFTDQKVDLTMIKQVARIKAAAALANQQSGTLSKEKAQIIVTAAEEIIMGK 82
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISGERMPPELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 83 WDEEFIVDTFQGGAGTSTNMNVNEVIANRGLELMGHKKGEYQYLHPLDDVNQSQSTNDVYPSAGKLALLVYIEQLDEALV 162
Cdd:cd01596 81 LDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKGKYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLPALE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 163 QLIDRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAELLTLNMGGTAIGTGLNASYRYQEY 242
Cdd:cd01596 161 QLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGYAEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 243 LYQELNRRFPRPLRPANDLIDSTQHTDSFASISGGLKTIAITLNKSANDLRLLASGPRTGFHELNLPARQAGSSIMPGKV 322
Cdd:cd01596 241 VAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMPGKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 323 NPVIPEVISQIAFQVIGNDGAITFAAASGELELNAFEPVMFHNLFESCQLLTKACQIFADKCVAGITVNETACLKAVNNS 402
Cdd:cd01596 321 NPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYVENS 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1173256776 403 TGTITALSPQIGYEKATAFVKEALEKNCSIEELLKQEEFLRTETY 447
Cdd:cd01596 401 LMLVTALNPHIGYEKAAEIAKEALKEGRTLREAALELGLLTEEEL 445
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
1-442 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 616.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 1 MMRIESDTIGSLPIYEGAYYGIHSYRAKENFAFTDQKVDLTMIKQVARIKAAAALANQQSGTLSKEKAQIIVTAAEEIIM 80
Cdd:PRK13353 4 NMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYKIHPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQACDEILA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 81 GKWDEEFIVDTFQGGAGTSTNMNVNEVIANRGLELMGHKKGEYQYLHPLDDVNQSQSTNDVYPSAGKLALLVYIEQLDEA 160
Cdd:PRK13353 84 GKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLLEGLLAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 161 LVQLIDRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAELLTLNMGGTAIGTGLNASYRYQ 240
Cdd:PRK13353 164 MGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADPEYI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 241 EYLYQELNRRFPRPLRPANDLIDSTQHTDSFASISGGLKTIAITLNKSANDLRLLASGPRTGFHELNLPARQAGSSIMPG 320
Cdd:PRK13353 244 ERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSIMPG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 321 KVNPVIPEVISQIAFQVIGNDGAITFAAASGELELNAFEPVMFHNLFESCQLLTKACQIFADKCVAGITVNETACLKAVN 400
Cdd:PRK13353 324 KVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKEYVE 403
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1173256776 401 NSTGTITALSPQIGYEKATAFVKEALEKNCSIEELLKQEEFL 442
Cdd:PRK13353 404 KSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLL 445
|
|
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
1-441 |
1.48e-179 |
|
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: 509.57 E-value: 1.48e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 1 MMRIESDTIGSLPIYEGAYYGIHSYRAKENFAFTDQKVDLTMIKQVARIKAAAALANQQSGTLSKEKAQIIVTAAEEIIM 80
Cdd:COG0114 3 ETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGERMPREFIRALALIKKAAARANAELGLLDAEKADAIVAAADEVIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 81 GKWDEEFIVDTFQGGAGTSTNMNVNEVIANRGLELMGHKKGEYQYLHPLDDVNQSQSTNDVYPSAGKLALLVYIE-QLDE 159
Cdd:COG0114 83 GKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEeRLLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 160 ALVQLIDRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAELLTLNMGGTAIGTGLNASYRY 239
Cdd:COG0114 163 ALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHPGF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 240 QEYLYQELNRRFPRPLRPANDLIDSTQHTDSFASISGGLKTIAITLNKSANDLRLLASGPRTGFHELNLPARQAGSSIMP 319
Cdd:COG0114 243 AERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSIMP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 320 GKVNPVIPEVISQIAFQVIGNDGAITFAAASGELELNAFEPVMFHNLFESCQLLTKACQIFADKCVAGITVNETACLKAV 399
Cdd:COG0114 323 GKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEELL 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1173256776 400 NNSTGTITALSPQIGYEKATAFVKEALEKNCSIEE------LLKQEEF 441
Cdd:COG0114 403 ERSLMLVTALNPHIGYDKAAKIAKKAHKEGRTLREaalelgLLSEEEF 450
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
3-445 |
7.68e-174 |
|
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: 495.51 E-value: 7.68e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 3 RIESDTIGSLPIYEGAYYGIHSYRAKENFAFTDQKVDLT--MIKQVARIKAAAALANQQSGTLSKEKAQIIVTAAEEII- 79
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKISDIpeFVRGMVMVKKAAALANKELGTIPESIANAIVAACDEILn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 80 MGKWDEEFIVDTFQGGAGTSTNMNVNEVIANRGLELMGHKKGEYQYLHPLDDVNQSQSTNDVYPSAGKLALLVYIEQLDE 159
Cdd:TIGR00839 81 NGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIAVYSSLIKLVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 160 ALVQLIDRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAELLTLNMGGTAIGTGLNASYRY 239
Cdd:TIGR00839 161 AINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 240 QEYLYQELNRRFPRPLRPANDLIDSTQHTDSFASISGGLKTIAITLNKSANDLRLLASGPRTGFHELNLPARQAGSSIMP 319
Cdd:TIGR00839 241 SPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 320 GKVNPVIPEVISQIAFQVIGNDGAITFAAASGELELNAFEPVMFHNLFESCQLLTKACQIFADKCVAGITVNETACLKAV 399
Cdd:TIGR00839 321 AKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGYV 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1173256776 400 NNSTGTITALSPQIGYEKATAFVKEALEKNCSIEELLKQEEFLRTE 445
Cdd:TIGR00839 401 FNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEE 446
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
1-447 |
9.43e-174 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 495.00 E-value: 9.43e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 1 MMRIESDTIGSLPIYEGAYYGIHSYRAKENFAFTDQKVDLTMIKQVARIKAAAALANQQSGTLSKEKAQIIVTAAEEIIM 80
Cdd:PRK00485 3 ETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALALLKKAAARVNAELGLLDAEKADAIVAAADEVIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 81 GKWDEEFIVDTFQGGAGTSTNMNVNEVIANRGLELMGHKKGEYQYLHPLDDVNQSQSTNDVYPSAGKLALLVYI-EQLDE 159
Cdd:PRK00485 83 GKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIvERLLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 160 ALVQLIDRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAELLTLNMGGTAIGTGLNASYRY 239
Cdd:PRK00485 163 ALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHPGF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 240 QEYLYQELNRRFPRPLRPANDLIDSTQHTDSFASISGGLKTIAITLNKSANDLRLLASGPRTGFHELNLPARQAGSSIMP 319
Cdd:PRK00485 243 AERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSIMP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 320 GKVNPVIPEVISQIAFQVIGNDGAITFAAASGELELNAFEPVMFHNLFESCQLLTKACQIFADKCVAGITVNETACLKAV 399
Cdd:PRK00485 323 GKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKELL 402
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1173256776 400 NNSTGTITALSPQIGYEKATAFVKEALEKNCSIEELLKQEEFLRTETY 447
Cdd:PRK00485 403 ERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEF 450
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
3-447 |
1.32e-170 |
|
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: 486.62 E-value: 1.32e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 3 RIESDTIGSLPIYEGAYYGIHSYRAKENFAFTDQKVDLTMIKQVARIKAAAALANQQSGTLSKEKAQIIVTAAEEIIMGK 82
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 83 WDEEFIVDTFQGGAGTSTNMNVNEVIANRGLELMGHKKGEYQYLHPLDDVNQSQSTNDVYPSAGKLALLVYI-EQLDEAL 161
Cdd:cd01362 81 LDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALqERLLPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 162 VQLIDRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAELLTLNMGGTAIGTGLNASYRYQE 241
Cdd:cd01362 161 KHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGFAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 242 YLYQELNRRFPRPLRPANDLIDSTQHTDSFASISGGLKTIAITLNKSANDLRLLASGPRTGFHELNLPARQAGSSIMPGK 321
Cdd:cd01362 241 KVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMPGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 322 VNPVIPEVISQIAFQVIGNDGAITFAAASGELELNAFEPVMFHNLFESCQLLTKACQIFADKCVAGITVNETACLKAVNN 401
Cdd:cd01362 321 VNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELLER 400
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1173256776 402 STGTITALSPQIGYEKATAFVKEALEKNCSIEELLKQEEFLRTETY 447
Cdd:cd01362 401 SLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEF 446
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
9-441 |
4.97e-158 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 454.92 E-value: 4.97e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 9 IGSLPIYEGAYYGIHSYRAKENFAFTDQKVDLTM--IKQVARIKAAAALANQQSGTLSKEKAQIIVTAAEEIIMGKWDEE 86
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGGERERMPEpiVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAEGKLDDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 87 FIVDTFQGGAGTSTNMNVNEVIANRGLELMGHKKGEYQYLHPLDDVNQSQSTNDVYPSAGKLALLVYI-EQLDEALVQLI 165
Cdd:PLN00134 81 FPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATEIhSRLIPALKELH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 166 DRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAELLTLNMGGTAIGTGLNASYRYQEYLYQ 245
Cdd:PLN00134 161 ESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 246 ELNRRFPRPLRPANDLIDSTQHTDSFASISGGLKTIAITLNKSANDLRLLASGPRTGFHELNLPARQAGSSIMPGKVNPV 325
Cdd:PLN00134 241 AVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 326 IPEVISQIAFQVIGNDGAITFAAASGELELNAFEPVMFHNLFESCQLLTKACQIFADKCVAGITVNETACLKAVNNSTGT 405
Cdd:PLN00134 321 QCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLML 400
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1173256776 406 ITALSPQIGYEKATAFVKEALEKNCSIEE------LLKQEEF 441
Cdd:PLN00134 401 VTALNPKIGYDKAAAVAKKAHKEGTTLKEaalklgVLTAEEF 442
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
2-445 |
1.65e-157 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 454.46 E-value: 1.65e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 2 MRIESDTIGSLPIYEGAYYGIHSYRAKENFAFTDQKVDLTMIKQVARIKAAAALANQQSGTLSKEKAQIIVTAAEEIIMG 81
Cdd:PRK14515 11 VRIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGYKIHEGLIKAFAIVKKAAALANTDVGRLELNKGGAIAEAAQEILDG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 82 KWDEEFIVDTFQGGAGTSTNMNVNEVIANRGLELMGHKKGEYQYLHPLDDVNQSQSTNDVYPSAGKLALLVYIEQLDEAL 161
Cdd:PRK14515 91 KWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIATLNALEGLLQTM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 162 VQLIDRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAELLTLNMGGTAIGTGLNASYRYQE 241
Cdd:PRK14515 171 GYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNADPEYIE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 242 YLYQELNRRFPRPLRPANDLIDSTQHTDSFASISGGLKTIAITLNKSANDLRLLASGPRTGFHELNLPARQAGSSIMPGK 321
Cdd:PRK14515 251 AVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSIMPGK 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 322 VNPVIPEVISQIAFQVIGNDGAITFAAASGELELNAFEPVMFHNLFESCQLLTKACQIFADKCVAGITVNETACLKAVNN 401
Cdd:PRK14515 331 VNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKEYVEK 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1173256776 402 STGTITALSPQIGYEKATAFVKEALEKNCSIEELLKQEEFLRTE 445
Cdd:PRK14515 411 SVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQE 454
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
1-447 |
6.94e-113 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 339.98 E-value: 6.94e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 1 MMRIESDTIGSLPIYEGAYYGIHSYRAKENFAFTDQKVDLTMIKQVARIKAAAALANQQSGTLSKEKAQIIVTAAEEIIM 80
Cdd:PRK12425 1 MSRTETDSLGPIEVPEDAYWGAQTQRSLINFAIGKERMPLAVLHALALIKKAAARVNDRNGDLPADIARLIEQAADEVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 81 GKWDEEFIVDTFQGGAGTSTNMNVNEVIANRGLELMGHKKGEYQYLHPLDDVNQSQSTNDVYPSAGKLA--------LLV 152
Cdd:PRK12425 81 GQHDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAaaqavheqLLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 153 YIEQLDEALVQLIDRwHMKakevqhVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAELLTLNMGGTAIGTG 232
Cdd:PRK12425 161 AIAELSGGLAEQSAR-HAK------LVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 233 LNASYRYQEYLYQELNRRFPRPLRPANDLIDSTQHTDSFASISGGLKTIAITLNKSANDLRLLASGPRTGFHELNLPARQ 312
Cdd:PRK12425 234 LNAPHGFAEAIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 313 AGSSIMPGKVNPVIPEVISQIAFQVIGNDGAITFAAASGELELNAFEPVMFHNLFESCQLLTKACQIFADKCVAGITVNE 392
Cdd:PRK12425 314 PGSSIMPGKVNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDA 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1173256776 393 TACLKAVNNSTGTITALSPQIGYEKATAFVKEALEKNCSIEELLKQEEFLRTETY 447
Cdd:PRK12425 394 EQMAAHLERGLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQF 448
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
43-391 |
1.12e-102 |
|
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: 308.66 E-value: 1.12e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 43 IKQVARIKAAAALANQQSGTLSKEKAQIIVTAAEEIIMGKWDEEFivdtFQGGAGTSTNMNVNEVIANRGLELMGHKkge 122
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQV----EQEGSGTHDVMAVEEVLAERAGELNGGY--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 123 yqylhplddVNQSQSTNDVYPSAGKLALLVYIEQLDEALVQLIDRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYA 202
Cdd:cd01334 74 ---------VHTGRSSNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 203 HSLTRCRERLHHLSAELLTLNMGGTAIGTGLNASYRYQEYLYQELNRrfprpLRPANDLIDSTQHTDSFASISGGLKTIA 282
Cdd:cd01334 145 AELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAELLGF-----FGPAPNSTQAVSDRDFLVELLSALALLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 283 ITLNKSANDLRLLASGprtGFHELNLPAR-QAGSSIMPGKVNPVIPEVISQIAFQVIGNDGAITFAAASGELELNAFEPV 361
Cdd:cd01334 220 VSLSKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPV 296
|
330 340 350
....*....|....*....|....*....|
gi 1173256776 362 MFHNLFESCQLLTKACQIFADKCvAGITVN 391
Cdd:cd01334 297 EREALPDSFDLLDAALRLLTGVL-EGLEVN 325
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
18-339 |
4.63e-85 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 263.08 E-value: 4.63e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 18 AYYGIHSYRAKENFAFTDQKVDLTMI-KQVARIKaaaalanqqsGTLSKEKAQIIVTAAEEII-MGKWDEEFIVDTFQGG 95
Cdd:pfam00206 9 ALMGIFTDRSRFNFRLGEEDIKGLAAlKKAAAKA----------NVILKEEAAAIIKALDEVAeEGKLDDQFPLKVWQEG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 96 AGTSTNMNVNEVIAnrglELMGhkkgeyQYLHPLDDVNQSQSTNDVYPSAGKLALLVYI-EQLDEALVQLIDRWHMKAKE 174
Cdd:pfam00206 79 SGTAVNMNLNEVIG----ELLG------QLVHPNDHVHTGQSSNDQVPTALRLALKDALsEVLLPALRQLIDALKEKAKE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 175 VQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAELLTL-NMGGTAIGTGLNASYRYQEYLYQELNrRFPR 253
Cdd:pfam00206 149 FADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLpLGGGTAVGTGLNADPEFAELVAKELG-FFTG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 254 PLRPANDLIDSTQHTDSFASISGGLKTIAITLNKSANDLRLLASGPrTGFHELNLPARQAGSSIMPGKVNPVIPEVISQI 333
Cdd:pfam00206 228 LPVKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPDQLELLTGK 306
|
....*.
gi 1173256776 334 AFQVIG 339
Cdd:pfam00206 307 AGRVMG 312
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
102-381 |
3.98e-54 |
|
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: 180.50 E-value: 3.98e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 102 MNVNEVIANRGLELMGHKKGEYqylhpldDVNQSQSTNDVYPSAGKLALLVYIEQLDEALVQLIDRWHMKAKEVQHVAKM 181
Cdd:cd01594 14 ALVEEVLAGRAGELAGGLHGSA-------LVHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 182 GRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSaelltlnmggtaigtglnasyryqeylyqelnrrfprplrpandl 261
Cdd:cd01594 87 GRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEAA--------------------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 262 idstqhtdsFASISGGLKTIAITLNKSANDLRLLASGPRTGFHELNLPaRQAGSSIMPGKVNPVIPEVISQIAFQVIGND 341
Cdd:cd01594 122 ---------VAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGNL 191
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1173256776 342 GAITFAAASGELELNAFEPVMFHNLFESCQLLTKACQIFA 381
Cdd:cd01594 192 VAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
157-439 |
2.96e-25 |
|
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: 107.33 E-value: 2.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 157 LDEALVQLIDRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAELLTLNMGGtAIGT----- 231
Cdd:cd01597 118 LERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGG-AAGTlaslg 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 232 --GLNAsyryQEYLYQELNrrFPRPLRPandlidstQHT--DSFASISGGLKTIAITLNKSANDLRLLAsgpRTGFHELN 307
Cdd:cd01597 197 dqGLAV----QEALAAELG--LGVPAIP--------WHTarDRIAELASFLALLTGTLGKIARDVYLLM---QTEIGEVA 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 308 LPARQA--GSSIMPGKVNPVIPEVISQIAFQVIGNDGAITFAAA--------SGELELNAFEpvmfhnlfESCQLLTKAC 377
Cdd:cd01597 260 EPFAKGrgGSSTMPHKRNPVGCELIVALARRVPGLAALLLDAMVqeherdagAWHAEWIALP--------EIFLLASGAL 331
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173256776 378 QIfADKCVAGITVNETACLKAVNNSTGTITA------LSPQIGYEKATAFVKE----ALEKNCSIEELLKQE 439
Cdd:cd01597 332 EQ-AEFLLSGLEVNEDRMRANLDLTGGLILSeavmmaLAPKLGRQEAHDLVYEacmrAVEEGRPLREVLLED 402
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
149-443 |
2.23e-22 |
|
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: 99.00 E-value: 2.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 149 ALLVYIEQLDEALVQLIDRwhmkAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAELLTLNMGGtA 228
Cdd:COG0015 114 ALELLLPDLDALIAALAEL----AEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVGKIGG-A 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 229 IGTG---LNASYRYQEYLYQELNrrfprpLRPANdliDSTQHT--DSFASISGGLKTIAITLNKSANDLRLLAsgpRTGF 303
Cdd:COG0015 189 VGTYaahGEAWPEVEERVAEKLG------LKPNP---VTTQIEprDRHAELFSALALIAGSLEKIARDIRLLQ---RTEV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 304 HELNLP--ARQAGSSIMPGKVNPVIPEVISQIAFQVIGNdgaITFAAASGELEL------NAFEPVMfhnLFESCQLLTK 375
Cdd:COG0015 257 GEVEEPfaKGQVGSSAMPHKRNPIDSENIEGLARLARAL---AAALLEALASWHerdlsdSSVERNI---LPDAFLLLDG 330
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1173256776 376 ACQIFAdKCVAGITVNETACLKAVNNSTGTI------TALSPQ-IGYEKATAFVKE----ALEKNCSIEELLKQEEFLR 443
Cdd:COG0015 331 ALERLL-KLLEGLVVNPERMRANLDLTGGLVlseavlMALVRRgLGREEAYELVKElargAWEEGNDLRELLAADPEIP 408
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
149-330 |
6.02e-21 |
|
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: 94.11 E-value: 6.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 149 ALLVYIEQLDEalvqLIDRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAELLTLNMGGtA 228
Cdd:cd01595 104 ALDIILPDLDA----LIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGGISG-A 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 229 IGTGLNASYR---YQEYLYQELNrrfprpLRPANdlIdSTQ--HTDSFASISGGLKTIAITLNKSANDLRLLAsgpRTGF 303
Cdd:cd01595 179 VGTHASLGPKgpeVEERVAEKLG------LKVPP--I-TTQiePRDRIAELLSALALIAGTLEKIATDIRLLQ---RTEI 246
|
170 180
....*....|....*....|....*....
gi 1173256776 304 HELNLPAR--QAGSSIMPGKVNPVIPEVI 330
Cdd:cd01595 247 GEVEEPFEkgQVGSSTMPHKRNPIDSENI 275
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
137-435 |
1.14e-18 |
|
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: 87.60 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 137 STNDVYPSAGKLALLVYIEQLDEALVQLIDRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLS 216
Cdd:cd01359 86 SRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLERLADAY 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 217 AELLTLNMGGTAI-GTGLNasyryqeylyqeLNRR-------FPRPLRPANDLIDSTQHTDSFASIsggLKTIAITLNKS 288
Cdd:cd01359 166 KRVNVSPLGAGALaGTTFP------------IDRErtaellgFDGPTENSLDAVSDRDFVLEFLSA---AALLMVHLSRL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 289 ANDLRLLASGPRtGFheLNLPARQA-GSSIMPGKVNPVIPEVISQIAFQVIGNdgAITFAAASGELELN-------AFEP 360
Cdd:cd01359 231 AEDLILWSTQEF-GF--VELPDAYStGSSIMPQKKNPDVLELIRGKAGRVIGA--LAGLLTTLKGLPLAynkdlqeDKEP 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 361 vmfhnLFESCQLLTKACQIFADkCVAGITVNETACLKAVNNSTGTITAL----------SPQIGYEKATAFVKEALEKNC 430
Cdd:cd01359 306 -----LFDAVDTLIASLRLLTG-VISTLTVNPERMREAAEAGFSTATDLadylvrekgvPFREAHHIVGRAVRLAEEKGK 379
|
....*
gi 1173256776 431 SIEEL 435
Cdd:cd01359 380 DLSDL 384
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
147-435 |
1.91e-17 |
|
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 439935 [Multi-domain] Cd Length: 462 Bit Score: 84.38 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 147 KLALLVYIEQLDEALVQLIDRWHMKAKEVQHVAkM-GRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAELLTLNMG 225
Cdd:COG0165 119 RLYLRDEILELIEALLALQEALLDLAEEHADTI-MpGYTHLQRAQPVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLG 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 226 GTAI-GTGLNASyryQEYLYQELNrrFPRPLRPAndlIDSTQHTDSFASISGGLKTIAITLNKSANDLRLLASGPRtGFh 304
Cdd:COG0165 198 AAALaGTTFPID---RERTAELLG--FDGPTENS---LDAVSDRDFALEFLSAASLIMVHLSRLAEELILWSSSEF-GF- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 305 eLNLPARQA-GSSIMPGKVNPVIPEVISQIAFQVIGNdgAITFAAasgelelnafepvMFHNL---------------FE 368
Cdd:COG0165 268 -VELPDAFStGSSIMPQKKNPDVAELIRGKTGRVIGN--LTGLLT-------------TMKGLplaynkdlqedkeplFD 331
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1173256776 369 SCQLLTKACQIFADkCVAGITVNETACLKAVNNSTGTITAL---------SPQIGYEKATAFVKEALEKNCSIEEL 435
Cdd:COG0165 332 AVDTLKLCLRLFAG-MIATLKVNRERMREAAGAGFSTATDLadylvrkgvPFREAHEIVGRLVRYAEEKGKDLEDL 406
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
135-325 |
2.70e-17 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 83.91 E-value: 2.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 135 SQstnDVYPSAGKLALLVYIEQLDEALVQLIDRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHH 214
Cdd:PRK09053 108 SQ---DIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 215 LSAELLTLNMGGTAigtGLNASYRYQ-----EYLYQELNrrFPRPLRPandlidstQHT--DSFASISGGLKTIAITLNK 287
Cdd:PRK09053 185 LRPRALVLQFGGAA---GTLASLGEQalpvaQALAAELQ--LALPALP--------WHTqrDRIAEFASALGLLAGTLGK 251
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1173256776 288 SANDLRLLAsgpRTGFHELNLPAR--QAGSSIMPGKVNPV 325
Cdd:PRK09053 252 IARDVSLLM---QTEVGEVFEPAAagKGGSSTMPHKRNPV 288
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
139-334 |
1.02e-16 |
|
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: 81.44 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 139 NDVYPSAGKLALLVYIEQLDEALVQLIDRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAE 218
Cdd:cd01360 92 SDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKEARER 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 219 LLTLNMGGtAIGTGLNASYRYQEYLYQELNrrfprpLRPANdliDSTQ--HTDSFASISGGLKTIAITLNKSANDLRLLA 296
Cdd:cd01360 172 ILVGKISG-AVGTYANLGPEVEERVAEKLG------LKPEP---ISTQviQRDRHAEYLSTLALIASTLEKIATEIRHLQ 241
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1173256776 297 sgpRTGFHELNLP--ARQAGSSIMPGKVNPVIPEVISQIA 334
Cdd:cd01360 242 ---RTEVLEVEEPfsKGQKGSSAMPHKRNPILSENICGLA 278
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
139-325 |
4.29e-14 |
|
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: 73.92 E-value: 4.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 139 NDVYPSAGKLALLVYIEQLDEALVQLIDRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSaE 218
Cdd:TIGR00928 98 NDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQLERLLQAK-E 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 219 LLTLNMGGTAIGTGLNASYryqeyLYQELNRRFPRPLRPANDLIdSTQ--HTDSFASISGGLKTIAITLNKSANDLRLLA 296
Cdd:TIGR00928 177 RIKVGGISGAVGTHAAAYP-----LVEEVEERVTEFLGLKPVPI-STQiePRDRHAELLDALALLATTLEKFAVDIRLLQ 250
|
170 180 190
....*....|....*....|....*....|.
gi 1173256776 297 sgpRTGFHELNLPA--RQAGSSIMPGKVNPV 325
Cdd:TIGR00928 251 ---RTEHFEVEEPFgkGQVGSSAMPHKRNPI 278
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
147-435 |
1.19e-11 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 66.33 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 147 KLALLVYIEQLDEALVQLIDRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAELLTLNMGG 226
Cdd:PRK00855 120 RLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGS 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 227 TAI-GTGLNasyryqeylyqeLNRR-------FPRPLRPAndlIDSTQHTDSFASISGGLKTIAITLNKSANDLRLLASg 298
Cdd:PRK00855 200 AALaGTTFP------------IDRErtaellgFDGVTENS---LDAVSDRDFALEFLSAASLLMVHLSRLAEELILWSS- 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 299 PRTGFheLNLPARQA-GSSIMPGKVNPVIPEVISQIAFQVIGNdgaitfaaasgeleLNAFEPVM------FH------- 364
Cdd:PRK00855 264 QEFGF--VELPDAFStGSSIMPQKKNPDVAELIRGKTGRVYGN--------------LTGLLTVMkglplaYNrdlqedk 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 365 -NLFESCQLLTKACQIFADkCVAGITVNETACLKAVNN--STGTITA--LSpQIG------YEKATAFVKEALEKNCSIE 433
Cdd:PRK00855 328 ePLFDAVDTLKLSLEAMAG-MLETLTVNKERMREAAGKgfSTATDLAdyLV-RKGvpfreaHEIVGKAVREAEERGVDLA 405
|
..
gi 1173256776 434 EL 435
Cdd:PRK00855 406 DL 407
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
135-334 |
2.72e-11 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 64.69 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 135 SQstnDVYPSAGKLALLVYIEQLDEALVQLIDRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHH 214
Cdd:PRK05975 108 SQ---DVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRHRDRLEA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 215 LSAELLTLNMGGtAIGT----GLNASyRYQEYLYQELnrrfprplrpanDLIDSTQ-HT--DSFASISGGLKTIAITLNK 287
Cdd:PRK05975 185 LRADVFPLQFGG-AAGTleklGGKAA-AVRARLAKRL------------GLEDAPQwHSqrDFIADFAHLLSLVTGSLGK 250
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1173256776 288 SANDLRLLASGPRtgfhELNLpARQAGSSIMPGKVNPVIPEVISQIA 334
Cdd:PRK05975 251 FGQDIALMAQAGD----EISL-SGGGGSSAMPHKQNPVAAETLVTLA 292
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
150-435 |
9.54e-10 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 60.57 E-value: 9.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 150 LLVYIEQLDEALVQLidrwhmkAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAELLTLNMGGTAI 229
Cdd:PRK12308 128 LLLALDQLQQQMVNV-------AERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGSGAL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 230 -GTGLNASyryQEYLYQELNrrFPRPLRPANDLIDSTQHTD---SFASISgglktiAITLNKSANDLRLLASGpRTGFHE 305
Cdd:PRK12308 201 aGTAYPID---REALAHNLG--FRRATRNSLDSVSDRDHVMelmSVASIS------MLHLSRLAEDLIFYNSG-ESGFIE 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 306 LNlPARQAGSSIMPGKVNPVIPEVISQIAFQVIGNDGAITFAAASGELELNAFEPVMFHNLFEScqLLT-KACQIFADKC 384
Cdd:PRK12308 269 LA-DTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKDMQEDKEGLFDA--LDTwNDCMEMAALC 345
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 385 VAGITVNETACLKAVNNSTGTITAL-----SPQIGYEKATAFVKE----ALEKNCSIEEL 435
Cdd:PRK12308 346 FDGIKVNGERTLEAAKQGYANATELadylvAKGIPFREAHHIVGVavvgAIAKGCALEEL 405
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
150-340 |
5.02e-09 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 58.20 E-value: 5.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 150 LLVYIEQLDEALVQLidrwhmkAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAELLTLNMGGTAI 229
Cdd:PLN02646 142 IRKRIKTLQVALVEL-------AEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCAL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 230 -GTGLNASyryQEYLYQELNrrFPRPLRPAndlIDSTQHTDSFASISGGLKTIAITLNKSANDLRLLASGPrTGFHELNl 308
Cdd:PLN02646 215 aGTGLPID---RFMTAKDLG--FTAPMRNS---IDAVSDRDFVLEFLFANSITAIHLSRLGEEWVLWASEE-FGFVTPS- 284
|
170 180 190
....*....|....*....|....*....|..
gi 1173256776 309 PARQAGSSIMPGKVNPVIPEVISQIAFQVIGN 340
Cdd:PLN02646 285 DAVSTGSSIMPQKKNPDPMELVRGKSARVIGD 316
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
132-421 |
1.77e-08 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 56.78 E-value: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 132 VNQSQSTNDVYPSAGKLALLVYIEQLDEALVQLIDRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRER 211
Cdd:PRK02186 510 LQTARSRNDINATTTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHA 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 212 LHHLSAELLTLNMG-GTAIGTGLNASYRYQEYLYQelnrrFPRPLRPANDLIDSTQHTDSFASIsggLKTIAITLNKSAN 290
Cdd:PRK02186 590 LFALFEHIDVCPLGaGAGGGTTFPIDPEFVARLLG-----FEQPAPNSLDAVASRDGVLHFLSA---MAAISTVLSRLAQ 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 291 DLRLLASGPrtgFHELNLPARQA-GSSIMPGKVNPVIPEVISQIAFQVIGndGAITFAAASGELElnafepvmFHNLFES 369
Cdd:PRK02186 662 DLQLWTTRE---FALVSLPDALTgGSSMLPQKKNPFLLEFVKGRAGVVAG--ALASASAALGKTP--------FSNSFEA 728
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173256776 370 ----CQLLTKACQIFADKC------VAGITVNETACLKAVNNSTGTITALSPQIGYEKATAF 421
Cdd:PRK02186 729 gspmNGPIAQACAAIEDAAavlvllIDGLEADQARMRAHLEDGGVSATAVAESLVVRRSISF 790
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
406-447 |
5.96e-08 |
|
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: 48.86 E-value: 5.96e-08
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1173256776 406 ITALSPQIGYEKATAFVKEALEKNCSIEELLKQEEFLRTETY 447
Cdd:pfam10415 2 VTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEEL 43
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
150-348 |
1.14e-07 |
|
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: 53.86 E-value: 1.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 150 LLVYIEQLD---EALVQLIDRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAELLTLNMGG 226
Cdd:cd03302 105 LIQIRDALDlilPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGVKG 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 227 TaigTGLNASYRYqeyLYQ-------ELNRRFPRPLRPANDLIDSTQ-HTDSF-ASISGGLKTIAITLNKSANDLRLLAs 297
Cdd:cd03302 185 T---TGTQASFLD---LFEgdhdkveALDELVTKKAGFKKVYPVTGQtYSRKVdIDVLNALSSLGATAHKIATDIRLLA- 257
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1173256776 298 gprtGFHELNLP--ARQAGSSIMPGKVNPVIPEVISQIAFQVIG--NDGAITFAA 348
Cdd:cd03302 258 ----NLKEVEEPfeKGQIGSSAMPYKRNPMRSERCCSLARHLMNlaSNAAQTAST 308
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
152-325 |
1.26e-06 |
|
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: 50.31 E-value: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 152 VYIEQLDEalvqLIDRWHMKAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHsltRCRERLHHLSAELLTLNMGGtAIGT 231
Cdd:cd01598 120 VILPLLKE----IIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVY---RLERQYKQLKQIEILGKFNG-AVGN 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 232 gLNASY-RYQEYLYQELNRRFPRPLR-PANDLIDSTQHTDSFASISGGLK---TIAITLNK---SANDLRLLASGPRTGf 303
Cdd:cd01598 192 -FNAHLvAYPDVDWRKFSEFFVTSLGlTWNPYTTQIEPHDYIAELFDALArinTILIDLCRdiwGYISLGYFKQKVKKG- 269
|
170 180
....*....|....*....|..
gi 1173256776 304 helnlparQAGSSIMPGKVNPV 325
Cdd:cd01598 270 --------EVGSSTMPHKVNPI 283
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
149-330 |
3.75e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 49.21 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 149 ALLVYIEQLDEALVQLidrwhmkAKEVQHVAKMGRTQLQEAVPMTVGESFAAYAHSLTRCRERLHHLSAELLTLNMGGTA 228
Cdd:PRK04833 127 ELLTALRQLQSALVET-------AENNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGA 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1173256776 229 I-GTGLNASyRYQeyLYQELNrrFPRPLRpaNDLiDSTQHTD------SFASISgglktiAITLNKSANDLRLLASGpRT 301
Cdd:PRK04833 200 LaGTAYEID-REQ--LAGWLG--FASATR--NSL-DSVSDRDhvlellSDASIS------MVHLSRFAEDLIFFNSG-EA 264
|
170 180
....*....|....*....|....*....
gi 1173256776 302 GFHELNlPARQAGSSIMPGKVNPVIPEVI 330
Cdd:PRK04833 265 GFVELS-DRVTSGSSLMPQKKNPDALELI 292
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
281-340 |
6.62e-04 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 40.78 E-value: 6.62e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1173256776 281 IAITLNKSANDLRLLAsgpRTGFHELNLPAR--QAGSSIMPGKVNPVIPEVISQIAFQVIGN 340
Cdd:PRK08937 26 IATSLEKFANEIRLLQ---RSEIREVEEPFAkgQKGSSAMPHKRNPIGSERITGLARVLRSY 84
|
|
| |
