|
Name |
Accession |
Description |
Interval |
E-value |
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
1-473 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 926.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 1 MLNNIRIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISDIPEFVRGMVMVKKAAAMANKELQTIPKSVANAIIAAC 80
Cdd:PRK12273 1 MMMNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKISDYPELIRALAMVKKAAALANKELGLLDEEKADAIVAAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 81 DEVLNnGKCMDQFPVDVYQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASI 160
Cdd:PRK12273 81 DEILA-GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIALLLSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 161 IKLIDALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEEVKNISRTAELLLEVNLGATAIGTGLN 240
Cdd:PRK12273 160 RKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 241 TPKEYSPLAVQKLAEVTGFACVPAEDLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAG 320
Cdd:PRK12273 240 APPGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 321 SSIMPAKVNPVVPEVVNQVCFKVIGNDITVTMASEAGQLQLNVMEPVIGQAMFESIHILSNACYNLLEKCVSGITANKEV 400
Cdd:PRK12273 320 SSIMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEER 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507080634 401 CEAFVFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLERGLLTESELDDIFSAQNLMHPAYKAKRYT 473
Cdd:PRK12273 400 CREYVENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTHPGYKGKRYT 472
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
6-465 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 861.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 6 RIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISDIPEFVRGMVMVKKAAAMANKELQTIPKSVANAIIAACDEVLN 85
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPISDHPELIRALAMVKKAAALANRELGLLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 86 nGKCMDQFPVDVYQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASIIKLID 165
Cdd:COG1027 81 -GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLALLLLLRELLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 166 ALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEEVKNISRTAELLLEVNLGATAIGTGLNTPKEY 245
Cdd:COG1027 160 ALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 246 SPLAVQKLAEVTGFACVPAEDLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMP 325
Cdd:COG1027 240 IELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 326 AKVNPVVPEVVNQVCFKVIGNDITVTMASEAGQLQLNVMEPVIGQAMFESIHILSNACYNLLEKCVSGITANKEVCEAFV 405
Cdd:COG1027 320 GKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYV 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 406 FNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLERGLLTESELDDIFSAQNLMHP 465
Cdd:COG1027 400 ENSIGLVTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGLLTEEELDEILDPENMTGP 459
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
6-473 |
0e+00 |
|
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: 851.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 6 RIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISDIPEFVRGMVMVKKAAAMANKELQTIPKSVANAIIAACDEVLN 85
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKISDIPEFVRGMVMVKKAAALANKELGTIPESIANAIVAACDEILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 86 NGKCMDQFPVDVYQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASIIKLID 165
Cdd:TIGR00839 81 NGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIAVYSSLIKLVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 166 ALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEEVKNISRTAELLLEVNLGATAIGTGLNTPKEY 245
Cdd:TIGR00839 161 AINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 246 SPLAVQKLAEVTGFACVPAEDLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMP 325
Cdd:TIGR00839 241 SPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 326 AKVNPVVPEVVNQVCFKVIGNDITVTMASEAGQLQLNVMEPVIGQAMFESIHILSNACYNLLEKCVSGITANKEVCEAFV 405
Cdd:TIGR00839 321 AKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGYV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 507080634 406 FNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLERGLLTESELDDIFSAQNLMHPAYKAKRYT 473
Cdd:TIGR00839 401 FNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLMHPAYKAKRYK 468
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
6-458 |
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: 798.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 6 RIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISdiPEFVRGMVMVKKAAAMANKELQTIPKSVANAIIAACDEVLN 85
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISGLKIH--PELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 86 nGKCMDQFPVDVYQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASIIKLID 165
Cdd:cd01357 79 -GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLALILLLRKLLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 166 ALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEEVKNISRTAELLLEVNLGATAIGTGLNTPKEY 245
Cdd:cd01357 158 ALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 246 SPLAVQKLAEVTGFACVPAEDLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMP 325
Cdd:cd01357 238 IELVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 326 AKVNPVVPEVVNQVCFKVIGNDITVTMASEAGQLQLNVMEPVIGQAMFESIHILSNACYNLLEKCVSGITANKEVCEAFV 405
Cdd:cd01357 318 GKVNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 507080634 406 FNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLERGLLTESELDDIFS 458
Cdd:cd01357 398 ENSIGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELDEILS 450
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
4-475 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 748.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 4 NIRIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKIsdIPEFVRGMVMVKKAAAMANKELQTIPKSVANAIIAACDEV 83
Cdd:PRK13353 4 NMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYKI--HPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQACDEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 84 LNnGKCMDQFPVDVYQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASIIKL 163
Cdd:PRK13353 82 LA-GKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLLEGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 164 IDALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEEVKNISRTAELLLEVNLGATAIGTGLNTPK 243
Cdd:PRK13353 161 LAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 244 EYSPLAVQKLAEVTGFACVPAEDLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSI 323
Cdd:PRK13353 241 EYIERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 324 MPAKVNPVVPEVVNQVCFKVIGNDITVTMASEAGQLQLNVMEPVIGQAMFESIHILSNACYNLLEKCVSGITANKEVCEA 403
Cdd:PRK13353 321 MPGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKE 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 507080634 404 FVFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLERGLLTESELDDIFSAQNLMHPAYKAKRYTDE 475
Cdd:PRK13353 401 YVEKSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMTHPGIAGATLLKK 472
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
6-458 |
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: 724.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 6 RIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISdiPEFVRGMVMVKKAAAMANKELQTIPKSVANAIIAACDEVLN 85
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISGERMP--PELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 86 nGKCMDQFPVDVYQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASIIKLID 165
Cdd:cd01596 79 -GKLDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKGKYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 166 ALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEEVKNISRTAELLLEVNLGATAIGTGLNTPKEY 245
Cdd:cd01596 158 ALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 246 SPLAVQKLAEVTGFACVPAEDLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMP 325
Cdd:cd01596 238 AEKVAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 326 AKVNPVVPEVVNQVCFKVIGNDITVTMASEAGQLQLNVMEPVIGQAMFESIHILSNACYNLLEKCVSGITANKEVCEAFV 405
Cdd:cd01596 318 GKVNPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 507080634 406 FNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLERGLLTESELDDIFS 458
Cdd:cd01596 398 ENSLMLVTALNPHIGYEKAAEIAKEALKEGRTLREAALELGLLTEEELDEILD 450
|
|
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
4-456 |
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: 560.03 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 4 NIRIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISdiPEFVRGMVMVKKAAAMANKELQTIPKSVANAIIAACDEV 83
Cdd:COG0114 3 ETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGERMP--REFIRALALIKKAAARANAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 84 LNnGKCMDQFPVDVYQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASIIK- 162
Cdd:COG0114 81 IA-GKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEEr 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 163 LIDALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEEVKNISRTAELLLEVNLGATAIGTGLNTP 242
Cdd:COG0114 160 LLPALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 243 KEYSPLAVQKLAEVTGFACVPAEDLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSS 322
Cdd:COG0114 240 PGFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 323 IMPAKVNPVVPEVVNQVCFKVIGNDITVTMASEAGQLQLNVMEPVIGQAMFESIHILSNACYNLLEKCVSGITANKEVCE 402
Cdd:COG0114 320 IMPGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIE 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 507080634 403 AFVFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLERGLLTESELDDI 456
Cdd:COG0114 400 ELLERSLMLVTALNPHIGYDKAAKIAKKAHKEGRTLREAALELGLLSEEEFDRL 453
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
4-465 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 550.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 4 NIRIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISdiPEFVRGMVMVKKAAAMANKELQTIPKSVANAIIAACDEV 83
Cdd:PRK00485 3 ETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMP--RELIRALALLKKAAARVNAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 84 LNnGKCMDQFPVDVYQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASII-K 162
Cdd:PRK00485 81 IA-GKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVeR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 163 LIDALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEEVKNISRTAELLLEVNLGATAIGTGLNTP 242
Cdd:PRK00485 160 LLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 243 KEYSPLAVQKLAEVTGFACVPAEDLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSS 322
Cdd:PRK00485 240 PGFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 323 IMPAKVNPVVPEVVNQVCFKVIGNDITVTMASEAGQLQLNVMEPVIGQAMFESIHILSNACYNLLEKCVSGITANKEVCE 402
Cdd:PRK00485 320 IMPGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIK 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507080634 403 AFVFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLERGLLTESELDDIFSAQNLMHP 465
Cdd:PRK00485 400 ELLERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGP 462
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
6-456 |
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: 523.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 6 RIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISdiPEFVRGMVMVKKAAAMANKELQTIPKSVANAIIAACDEVLN 85
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMP--RELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 86 nGKCMDQFPVDVYQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASIIK-LI 164
Cdd:cd01362 79 -GKLDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQErLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 165 DALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEEVKNISRTAELLLEVNLGATAIGTGLNTPKE 244
Cdd:cd01362 158 PALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 245 YSPLAVQKLAEVTGFACVPAEDLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIM 324
Cdd:cd01362 238 FAEKVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 325 PAKVNPVVPEVVNQVCFKVIGNDITVTMASEAGQLQLNVMEPVIGQAMFESIHILSNACYNLLEKCVSGITANKEVCEAF 404
Cdd:cd01362 318 PGKVNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAEL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 507080634 405 VFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLERGLLTESELDDI 456
Cdd:cd01362 398 LERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRL 449
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
12-465 |
0e+00 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 518.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 12 LGTREVPADAYYGVHTLRAIENFYISNNKISDIPEFVRGMVMVKKAAAMANKELQTIPKSVANAIIAACDEVLNnGKCMD 91
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGGERERMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAE-GKLDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 92 QFPVDVYQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASI-IKLIDALNQL 170
Cdd:PLN00134 80 HFPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATEIhSRLIPALKEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 171 REGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEEVKNISRTAELLLEVNLGATAIGTGLNTPKEYSPLAV 250
Cdd:PLN00134 160 HESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 251 QKLAEVTGFACVPAEDLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMPAKVNP 330
Cdd:PLN00134 240 AAVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 331 VVPEVVNQVCFKVIGNDITVTMASEAGQLQLNVMEPVIGQAMFESIHILSNACYNLLEKCVSGITANKEVCEAFVFNSIG 410
Cdd:PLN00134 320 TQCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLM 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 507080634 411 IVTYLNPFIGHHNGDIVGKICAETGKSVREVVLERGLLTESELDDIFSAQNLMHP 465
Cdd:PLN00134 400 LVTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTGP 454
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
3-465 |
2.19e-169 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 485.66 E-value: 2.19e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 3 NNIRIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISdiPEFVRGMVMVKKAAAMANKELQTIPKSVANAIIAACDE 82
Cdd:PRK14515 9 NGVRIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGYKIH--EGLIKAFAIVKKAAALANTDVGRLELNKGGAIAEAAQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 83 VLNnGKCMDQFPVDVYQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASIIK 162
Cdd:PRK14515 87 ILD-GKWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIATLNALEG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 163 LIDALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEEVKNISRTAELLLEVNLGATAIGTGLNTP 242
Cdd:PRK14515 166 LLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNAD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 243 KEYSPLAVQKLAEVTGFACVPAEDLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSS 322
Cdd:PRK14515 246 PEYIEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 323 IMPAKVNPVVPEVVNQVCFKVIGNDITVTMASEAGQLQLNVMEPVIGQAMFESIHILSNACYNLLEKCVSGITANKEVCE 402
Cdd:PRK14515 326 IMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLK 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 507080634 403 AFVFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLERGLLTESELDDIFSAQNLMHP 465
Cdd:PRK14515 406 EYVEKSVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEMTHP 468
|
|
| fumC_II |
TIGR00979 |
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ... |
6-456 |
5.86e-155 |
|
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: 448.03 E-value: 5.86e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 6 RIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISdiPEFVRGMVMVKKAAAMANKELQTIPKSVANAIIAACDEVLN 85
Cdd:TIGR00979 2 RIEKDSMGEIQVPADKYWGAQTQRSLENFKIGTEKMP--LELIHAFAILKKAAAIVNEDLGKLDAKKADAIVQAADEILA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 86 nGKCMDQFPVDVYQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASII-KLI 164
Cdd:TIGR00979 80 -GKLDDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKnQLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 165 DALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEEVKNISRTAELLLEVNLGATAIGTGLNTPKE 244
Cdd:TIGR00979 159 PALENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 245 YSPLAVQKLAEVTGFACVPAEDLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIM 324
Cdd:TIGR00979 239 FDEKVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 325 PAKVNPVVPEVVNQVCFKVIGNDITVTMASEAGQLQLNVMEPVIGQAMFESIHILSNACYNLLEKCVSGITANKEVCEAF 404
Cdd:TIGR00979 319 PGKVNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 507080634 405 VFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLERGLLTESELDDI 456
Cdd:TIGR00979 399 LNNSLMLVTALNPHIGYDNAAKIAKKAHKEGITLKEAALELGLLSEEEFDEW 450
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
13-345 |
5.23e-126 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 369.01 E-value: 5.23e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 13 GTREVPADAYYGVHTLRAIENFYISNNKIsdipefvRGMVMVKKAAAMANKelqtIPKSVANAIIAACDEVLNNGKCMDQ 92
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDI-------KGLAALKKAAAKANV----ILKEEAAAIIKALDEVAEEGKLDDQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 93 FPVDVYQGGAGTSVNMNTNEVLAniglELMGhqkgeyQYLNPNDHVNKCQSTNDAYPTGFRIAVYASI-IKLIDALNQLR 171
Cdd:pfam00206 70 FPLKVWQEGSGTAVNMNLNEVIG----ELLG------QLVHPNDHVHTGQSSNDQVPTALRLALKDALsEVLLPALRQLI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 172 EGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEEVKNISR-TAELLLEVNLGATAIGTGLNTPKEYSPLAV 250
Cdd:pfam00206 140 DALKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQlLPRLLVLPLGGGTAVGTGLNADPEFAELVA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 251 QKLAEVTGFAcVPAEDLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPrAGLNEINLPELQAGSSIMPAKVNP 330
Cdd:pfam00206 220 KELGFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNP 297
|
330
....*....|....*
gi 507080634 331 VVPEVVNQVCFKVIG 345
Cdd:pfam00206 298 DQLELLTGKAGRVMG 312
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
6-468 |
5.63e-115 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 346.52 E-value: 5.63e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 6 RIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKIsdiP-EFVRGMVMVKKAAAMANKELQTIPKSVANAIIAACDEVL 84
Cdd:PRK12425 3 RTETDSLGPIEVPEDAYWGAQTQRSLINFAIGKERM---PlAVLHALALIKKAAARVNDRNGDLPADIARLIEQAADEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 85 NnGKCMDQFPVDVYQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIA-VYASIIKL 163
Cdd:PRK12425 80 D-GQHDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAaAQAVHEQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 164 IDALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEEVKNISRTAELLLEVNLGATAIGTGLNTPK 243
Cdd:PRK12425 159 LPAIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 244 EYSPLAVQKLAEVTGFACVPAEDLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSI 323
Cdd:PRK12425 239 GFAEAIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 324 MPAKVNPVVPEVVNQVCFKVIGNDITVTMASEAGQLQLNVMEPVIGQAMFESIHILSNACYNLLEKCVSGITANKEVCEA 403
Cdd:PRK12425 319 MPGKVNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507080634 404 FVFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLERGLLTESELDDIFSAQNLMHPAYK 468
Cdd:PRK12425 399 HLERGLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEAGGH 463
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
48-397 |
8.38e-105 |
|
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: 315.21 E-value: 8.38e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 48 VRGMVMVKKAAAMANKELQTIPKSVANAIIAACDEVLNngkcmDQFPVDVYQGGAGTSVNMNTNEVLANIGLELmghqkg 127
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILE-----GIAADQVEQEGSGTHDVMAVEEVLAERAGEL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 128 eyqylnPNDHVNKCQSTNDAYPTGFRIAVYASIIKLIDALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAF 207
Cdd:cd01334 70 ------NGGYVHTGRSSNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 208 SVLLKEEVKNISRTAELLLEVNLGATAIGTGLNTPKEYSPLAVQKLaevtGFAcVPAEDLIEATSDCGAYVMVHGALKRL 287
Cdd:cd01334 144 AAELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAELL----GFF-GPAPNSTQAVSDRDFLVELLSALALL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 288 AVKMSKICNDLRLLSSGpraGLNEINLPE-LQAGSSIMPAKVNPVVPEVVNQVCFKVIGNDITVTMASEAGQLQLNVMEP 366
Cdd:cd01334 219 AVSLSKIANDLRLLSSG---EFGEVELPDaKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSP 295
|
330 340 350
....*....|....*....|....*....|.
gi 507080634 367 VIGQAMFESIHILSNACYNLLEKCvSGITAN 397
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 ... |
108-387 |
1.15e-47 |
|
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: 164.32 E-value: 1.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 108 MNTNEVLANIGLELMGHQKGEYqylnpndHVNKCQSTNDAYPTGFRIAVYASIIKLIDALNQLREGFEQKAVEFQDILKM 187
Cdd:cd01594 14 ALVEEVLAGRAGELAGGLHGSA-------LVHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 188 GRTQLQDAVPMTLGQEFHAFSVLLKEEVKNISRTAelllevnlgataigtglntpkeysplavqklaevtgfacvpaedl 267
Cdd:cd01594 87 GRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEAA--------------------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 268 ieatsdcgaYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPeLQAGSSIMPAKVNPVVPEVVNQVCFKVIGND 347
Cdd:cd01594 122 ---------VAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGNL 191
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 507080634 348 ITVTMASEAGQLQLNVMEPVIGQAMFESIHILSNACYNLL 387
Cdd:cd01594 192 VAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
411-462 |
3.61e-17 |
|
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: 75.05 E-value: 3.61e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 507080634 411 IVTYLNPFIGHHNGDIVGKICAETGKSVREVVLERGLLTESELDDIFSAQNL 462
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
143-459 |
1.52e-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: 75.47 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 143 STNDAYPTGFRIAVYASIIKLIDALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKeevKNISRTA 222
Cdd:TIGR00838 106 SRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLL---RDYERLQ 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 223 ELLLEVN---LGATAI-GTGLNTPKEYsplavqkLAEVTGFA--------CVPAEDLI-EATSDCgAYVMVHgalkrlav 289
Cdd:TIGR00838 183 DALKRVNvspLGSGALaGTGFPIDREY-------LAELLGFDavtensldAVSDRDFIlELLFVA-ALIMVH-------- 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 290 kMSKICNDLRLLSSGPragLNEINLP-ELQAGSSIMPAKVNPVVPEVVNQVCFKVIGNDITVTMASEAGQLQLNVMEPVI 368
Cdd:TIGR00838 247 -LSRFAEDLILWSTGE---FGFVELPdEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQED 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 369 GQAMFESIHILSNaCYNLLEKCVSGITANKEVCE----AFVFNSIGIVTYLN----PF-IGHHngdIVGKI---CAETGK 436
Cdd:TIGR00838 323 KEPLFDALKTVEL-SLEMATGMLDTITVNKERMEeaasAGFSNATELADYLVrkgvPFrEAHH---IVGELvatAIERGK 398
|
330 340
....*....|....*....|....
gi 507080634 437 SVREVVLERGLLTESELD-DIFSA 459
Cdd:TIGR00838 399 GLEELTLEELQKFSPEFDeDVYEA 422
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
143-455 |
3.31e-13 |
|
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: 71.42 E-value: 3.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 143 STNDAYPTGFRIAVYASIIKLIDALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKeevKNISRTA 222
Cdd:cd01359 86 SRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLE---RDLERLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 223 ELLLEVN---LGATAI-GTGLNTPKEYsplavqkLAEVTGFA--------CVPAED-LIEATSDCgAYVMVHgalkrlav 289
Cdd:cd01359 163 DAYKRVNvspLGAGALaGTTFPIDRER-------TAELLGFDgptensldAVSDRDfVLEFLSAA-ALLMVH-------- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 290 kMSKICNDLRLLSSgpraglNEINLPELQA----GSSIMPAKvnpvvpevvnqvcfK--------------VIGNDITVT 351
Cdd:cd01359 227 -LSRLAEDLILWST------QEFGFVELPDaystGSSIMPQK--------------KnpdvlelirgkagrVIGALAGLL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 352 MASEAGQLQLN-----VMEPvigqaMFESIHILSNACyNLLEKCVSGITANKEVCEAFVFNSIGIVT----YLN-----P 417
Cdd:cd01359 286 TTLKGLPLAYNkdlqeDKEP-----LFDAVDTLIASL-RLLTGVISTLTVNPERMREAAEAGFSTATdladYLVrekgvP 359
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 507080634 418 F-IGHHngdIVGKI---CAETGKSVREVVLERgLLTESELDD 455
Cdd:cd01359 360 FrEAHH---IVGRAvrlAEEKGKDLSDLTLAE-LQAISPLFE 397
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
135-327 |
5.48e-11 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 64.40 E-value: 5.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 135 NDHVnkcqstndAypTGFRIAVYASIIKLIDALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEe 214
Cdd:PRK00855 112 NDQV--------A--TDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLAR- 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 215 vkNISRTAELLLEVN---LGATAI-GTGLNTPKEYSplavqklAEVTGFACVpAEDLIEATSD---------CGAYVMVH 281
Cdd:PRK00855 181 --DLERLRDARKRVNrspLGSAALaGTTFPIDRERT-------AELLGFDGV-TENSLDAVSDrdfaleflsAASLLMVH 250
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 507080634 282 galkrlavkMSKICNDLRLLSSgPRAGLneINLP-ELQAGSSIMPAK 327
Cdd:PRK00855 251 ---------LSRLAEELILWSS-QEFGF--VELPdAFSTGSSIMPQK 285
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
163-327 |
1.82e-10 |
|
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: 62.52 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 163 LIDALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEEVKNISRTAELLLEVNLGAtAIGTGLNTP 242
Cdd:cd01595 108 ILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGGISG-AVGTHASLG 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 243 KEysPLAVQK-LAEVTGFACVPAEDLIEatsDCGAYVMVHGALKRLAVKMSKICNDLRLLSsgpRAGLNEINLP--ELQA 319
Cdd:cd01595 187 PK--GPEVEErVAEKLGLKVPPITTQIE---PRDRIAELLSALALIAGTLEKIATDIRLLQ---RTEIGEVEEPfeKGQV 258
|
....*...
gi 507080634 320 GSSIMPAK 327
Cdd:cd01595 259 GSSTMPHK 266
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
163-327 |
2.59e-10 |
|
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: 62.36 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 163 LIDALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEEVKNISRTAELLLeVNLGATAIGTGLNTP 242
Cdd:TIGR00928 116 ILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQLERLLQAKERIK-VGGISGAVGTHAAAY 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 243 KEYSPLAvQKLAEVTGFACVPAEDLIEATSDCGAYVMvhgALKRLAVKMSKICNDLRLLSsgpRAGLNEINLP--ELQAG 320
Cdd:TIGR00928 195 PLVEEVE-ERVTEFLGLKPVPISTQIEPRDRHAELLD---ALALLATTLEKFAVDIRLLQ---RTEHFEVEEPfgKGQVG 267
|
....*..
gi 507080634 321 SSIMPAK 327
Cdd:TIGR00928 268 SSAMPHK 274
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
47-461 |
6.32e-10 |
|
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: 60.87 E-value: 6.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 47 FVRGMVMVKKAAAMANKELQTIPKSVANAIIAACDEvlnngkcmdqFPVD---VYQGGAGTSvnmntNEVLA---NIGlE 120
Cdd:COG0015 20 KIRAWLDVEIALAEAQAELGLIPAEAAAAIRAAADD----------FEIDaerIKEIEKETR-----HDVKAfvyALK-E 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 121 LMGHQKGEY-------QYLNpndhvnkcqstnDaypTGFRIAVYASIIKLIDALNQLREGFEQKAVEFQDILKMGRTQLQ 193
Cdd:COG0015 84 KVGAEAGEYihfgatsQDIN------------D---TALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 194 DAVPMTLGQEfhaFSVLLKEEVKNISRTAELLLEVNLGAT--AIGTGLNTPKEysPLAVQK-LAEVTGFACVPAE----- 265
Cdd:COG0015 149 HAEPTTFGKK---LAVWAAELLRQLERLEEARERVLVGKIggAVGTYAAHGEA--WPEVEErVAEKLGLKPNPVTtqiep 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 266 -DLIeatsdcgAYVMvhGALKRLAVKMSKICNDLRLLSsgpRAGLNEINLP--ELQAGSSIMPakvnpvvpevvnqvcFK 342
Cdd:COG0015 224 rDRH-------AELF--SALALIAGSLEKIARDIRLLQ---RTEVGEVEEPfaKGQVGSSAMP---------------HK 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 343 VigNDIT--------------VTMASEAGQLQL------NVMEPVIGQAMFesihILSNACYNLLEKCVSGITANKEVCE 402
Cdd:COG0015 277 R--NPIDsenieglarlaralAAALLEALASWHerdlsdSSVERNILPDAF----LLLDGALERLLKLLEGLVVNPERMR 350
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 507080634 403 A-------FVFnSIGIVTYLNP-FIGHHNG-DIVGKIC---AETGKSVREVVLE----RGLLTESELDDIFSAQN 461
Cdd:COG0015 351 AnldltggLVL-SEAVLMALVRrGLGREEAyELVKELArgaWEEGNDLRELLAAdpeiPAELSKEELEALFDPAN 424
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
143-444 |
7.16e-09 |
|
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: 57.80 E-value: 7.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 143 STNDAYPTGFRIAVYASIIKLIDALNQLREGFEQKAVEFQDILkM-GRTQLQDAVPMTLGQEFHA-FSVLLKEevknISR 220
Cdd:COG0165 109 SRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTI-MpGYTHLQRAQPVTFGHHLLAyAEMLLRD----RER 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 221 TAELLLEVN---LGATAI-GTGLNTPKEYsplavqkLAEVTGFA--------CVPAED-LIEATSDCgAYVMVHgalkrl 287
Cdd:COG0165 184 LADAYKRLNvspLGAAALaGTTFPIDRER-------TAELLGFDgptensldAVSDRDfALEFLSAA-SLIMVH------ 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 288 avkMSKICNDLRLLSSgPRAGLneINLPELQA-GSSIMPAKvnpvvpevvnqvcfK--------------VIGNDITVtm 352
Cdd:COG0165 250 ---LSRLAEELILWSS-SEFGF--VELPDAFStGSSIMPQK--------------KnpdvaelirgktgrVIGNLTGL-- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 353 aseagqlqLNVM---------------EPVigqamFESIHILSnACYNLLEKCVSGITANKEVCEAFV----FNSIGIVT 413
Cdd:COG0165 308 --------LTTMkglplaynkdlqedkEPL-----FDAVDTLK-LCLRLFAGMIATLKVNRERMREAAgagfSTATDLAD 373
|
330 340 350
....*....|....*....|....*....|....*....
gi 507080634 414 YLN----PF-IGHHngdIVGKI---CAETGKSVREVVLE 444
Cdd:COG0165 374 YLVrkgvPFrEAHE---IVGRLvryAEEKGKDLEDLTLE 409
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
143-327 |
1.57e-07 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 53.57 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 143 STNDAYPTGFRIAVYASIIKLIDALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLkeeVKNISRTA 222
Cdd:PLN02646 122 SRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQL---ERDAGRLV 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 223 ELLLEVN---LGATAI-GTGLntpkeysPLAVQKLAEVTGFAcVPAEDLIEATSDCGAYVMVHGALKRLAVKMSKICNDL 298
Cdd:PLN02646 199 DCRPRVNfcpLGSCALaGTGL-------PIDRFMTAKDLGFT-APMRNSIDAVSDRDFVLEFLFANSITAIHLSRLGEEW 270
|
170 180
....*....|....*....|....*....
gi 507080634 299 RLLSSGPRAGLNEINlpELQAGSSIMPAK 327
Cdd:PLN02646 271 VLWASEEFGFVTPSD--AVSTGSSIMPQK 297
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
135-327 |
2.03e-07 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 53.45 E-value: 2.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 135 NDHVNKcqSTNDAYPTGFRIAVYASIIKLIDALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEE 214
Cdd:PRK06705 109 NMHIGR--SRNDMGVTMYRMSLRRYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 215 VKNISRTAELLLEVNLGATAIGTglntpkEYSPLAVQKLAEVTGFACVpAEDLIEATSDCGAYVMVHGALKRLAVKMSKI 294
Cdd:PRK06705 187 LERMKKTYKLLNQSPMGAAALST------TSFPIKRERVADLLGFTNV-IENSYDAVAGADYLLEVSSLLMVMMTNTSRW 259
|
170 180 190
....*....|....*....|....*....|...
gi 507080634 295 CNDLRLLSSGPRAGLNEINlPELQAgSSIMPAK 327
Cdd:PRK06705 260 IHDFLLLATKEYDGITVAR-PYVQI-SSIMPQK 290
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
48-461 |
2.15e-07 |
|
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: 53.02 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 48 VRGMVMVKKAAAMANKELQTIPKSVANAIIAACD-EVLNngkcMDQFPVDVyqGGAGTSVnmntnevlanIGL-----EL 121
Cdd:cd01597 21 VQAMLDVEAALARAQAELGVIPKEAAAEIAAAADvERLD----LEALAEAT--ARTGHPA----------IPLvkqltAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 122 MGHQKGEYqylnpndhVNKCQSTNDAYPTGFRIAVYASIIKLIDALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLG 201
Cdd:cd01597 85 CGDAAGEY--------VHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 202 qefHAFSVLLKEEVKNISRTAEL---LLEVNLGAtAIGTGLNTPKEysPLAVQK-LAEVTGFAcVPA-------EDLIEA 270
Cdd:cd01597 157 ---LKVAVWLSELLRHRERLDELrprVLVVQFGG-AAGTLASLGDQ--GLAVQEaLAAELGLG-VPAipwhtarDRIAEL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 271 TSDCGayvMVHGALkrlavkmSKICNDLRLLSsgpRAGLNEINLPELQA--GSSIMPAKvNPVVPEVVNQVCFKVIGNDI 348
Cdd:cd01597 230 ASFLA---LLTGTL-------GKIARDVYLLM---QTEIGEVAEPFAKGrgGSSTMPHK-RNPVGCELIVALARRVPGLA 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 349 TVTMASE-------AGQLQLNVMepvigqAMFESIHILSNACYNLLEkCVSGITANKE-------------VCEAFVFNs 408
Cdd:cd01597 296 ALLLDAMvqeherdAGAWHAEWI------ALPEIFLLASGALEQAEF-LLSGLEVNEDrmranldltggliLSEAVMMA- 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 507080634 409 igivtyLNPFIGHHNG-DIVGKICAET---GKSVREVVLE----RGLLTESELDDIFSAQN 461
Cdd:cd01597 368 ------LAPKLGRQEAhDLVYEACMRAveeGRPLREVLLEdpevAAYLSDEELDALLDPAN 422
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
163-327 |
1.32e-06 |
|
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: 50.24 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 163 LIDALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGqefHAFSVLLKEEVKNISRTAELLLEVNLGAT--AIGTGLN 240
Cdd:cd01360 110 ILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFG---LKFALWYAEFKRHLERLKEARERILVGKIsgAVGTYAN 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 241 TPKEYSPLAVQKL---AEVTGFACVPAEDLIEatsdcgaYVMVHgALkrLAVKMSKICNDLRLLSsgpRAGLNEINLP-- 315
Cdd:cd01360 187 LGPEVEERVAEKLglkPEPISTQVIQRDRHAE-------YLSTL-AL--IASTLEKIATEIRHLQ---RTEVLEVEEPfs 253
|
170
....*....|..
gi 507080634 316 ELQAGSSIMPAK 327
Cdd:cd01360 254 KGQKGSSAMPHK 265
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
143-327 |
1.59e-05 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 47.29 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 143 STNDAYPTGFRIAVYASIIKLIDALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKeevKNISRTA 222
Cdd:PRK04833 108 SRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLA---RDESRLQ 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 223 ELLLEVN---LGATAI-GTGLNTPKEysplavqKLAEVTGFA--------CVPAED-LIEATSDcGAYVMVHgaLKRLAv 289
Cdd:PRK04833 185 DALKRLDvspLGSGALaGTAYEIDRE-------QLAGWLGFAsatrnsldSVSDRDhVLELLSD-ASISMVH--LSRFA- 253
|
170 180 190
....*....|....*....|....*....|....*...
gi 507080634 290 kmskicNDLRLLSSGpRAGLNEINlPELQAGSSIMPAK 327
Cdd:PRK04833 254 ------EDLIFFNSG-EAGFVELS-DRVTSGSSLMPQK 283
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
142-444 |
2.73e-05 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 46.70 E-value: 2.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 142 QSTNDAYPTGFRIAVYASIIKLIDALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEEVKNISRT 221
Cdd:PRK12308 107 RSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYSRLEDA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 222 AELLLEVNLGATAI-GTGLntpkeysPLAVQKLAEVTGFACVPAEDLiEATSD---------CGAYVMVHgalkrlavkM 291
Cdd:PRK12308 187 LTRLDTCPLGSGALaGTAY-------PIDREALAHNLGFRRATRNSL-DSVSDrdhvmelmsVASISMLH---------L 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 292 SKICNDLRLLSSGpraglnEINLPELQ----AGSSIMPAKVNPVVPEVVNQVCFKVIGNDITVTMASEAGQLQLNVMEPV 367
Cdd:PRK12308 250 SRLAEDLIFYNSG------ESGFIELAdtvtSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKDMQE 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 368 IGQAMFESIHILsNACYNLLEKCVSGITANKEVCEAFV----FNSIGIVTYLN----PFI-GHHNGDIVGKICAETGKSV 438
Cdd:PRK12308 324 DKEGLFDALDTW-NDCMEMAALCFDGIKVNGERTLEAAkqgyANATELADYLVakgiPFReAHHIVGVAVVGAIAKGCAL 402
|
....*.
gi 507080634 439 REVVLE 444
Cdd:PRK12308 403 EELSLE 408
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
145-233 |
1.83e-04 |
|
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: 43.76 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 145 NDAYPTGFRIAVYASIIKLIDalnQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEEVKNISRTaEL 224
Cdd:cd01598 106 NLAYALMIKEARNEVILPLLK---EIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLKQI-EI 181
|
....*....
gi 507080634 225 LLEVNlGAT 233
Cdd:cd01598 182 LGKFN-GAV 189
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
142-327 |
1.83e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 44.07 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 142 QSTNDAYPTGFRIAVYASIIKLIDALNQLREGFEQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEEVKNISRT 221
Cdd:PRK02186 514 RSRNDINATTTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHALFAL 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 222 AELLLEVNLGATAiGTGLNTPKEysPLavqKLAEVTGFACVPAEDLIEATSDCGAyvmVHG--ALKRLAVKMSKICNDLR 299
Cdd:PRK02186 594 FEHIDVCPLGAGA-GGGTTFPID--PE---FVARLLGFEQPAPNSLDAVASRDGV---LHFlsAMAAISTVLSRLAQDLQ 664
|
170 180
....*....|....*....|....*....
gi 507080634 300 LLSSgprAGLNEINLP-ELQAGSSIMPAK 327
Cdd:PRK02186 665 LWTT---REFALVSLPdALTGGSSMLPQK 690
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
156-221 |
9.28e-03 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 38.57 E-value: 9.28e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 507080634 156 VYASIIKLIDALNQLregfeqkAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEEVKNISRT 221
Cdd:PLN02848 146 VLPTMDEIIKAISSL-------AHEFAYVPMLSRTHGQPASPTTLGKEMANFAYRLSRQRKQLSEV 204
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
162-327 |
9.91e-03 |
|
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: 38.45 E-value: 9.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 162 KLIDALNQLREgfeqKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFSVLLKEEVKNISRT-AELLLEVNLGATAIGTGLN 240
Cdd:cd03302 118 KLAAVIDRLAE----FALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLrDDLRFRGVKGTTGTQASFL 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507080634 241 TPKEYSPLAVQKL----AEVTGFACVpaEDLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLssgprAGLNEINLP- 315
Cdd:cd03302 194 DLFEGDHDKVEALdelvTKKAGFKKV--YPVTGQTYSRKVDIDVLNALSSLGATAHKIATDIRLL-----ANLKEVEEPf 266
|
170
....*....|...
gi 507080634 316 -ELQAGSSIMPAK 327
Cdd:cd03302 267 eKGQIGSSAMPYK 279
|
|
| |
