|
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: 913.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 1 MLNNIRIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISDIPEFVRGMVMVKKAAAQANKELQTIPKSVANAIIAAC 80
Cdd:PRK12273 1 MMMNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKISDYPELIRALAMVKKAAALANKELGLLDEEKADAIVAAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 81 DEVLNnGKCMDQFPVDVFQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASI 160
Cdd:PRK12273 81 DEILA-GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIALLLSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 161 LKLIDAINQLGEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFNVLLNEETKCILRTAELLLEVNLGATAIGTRLN 240
Cdd:PRK12273 160 RKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 241 TPDGYQQLAVQKLAEVSNLPVVPAEDLIEATSDCGAYVMVHSSLKRLAVKLSKICNDLRLLSSGPRAGLNEINLPELQAG 320
Cdd:PRK12273 240 APPGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 321 SSIMPAKVNPVVPEVVNQVCFKVIGNDTTVTMASEAGQLQLNVMEPVIGQAMFESIHILTNACYNLLEKCVSGITANKAV 400
Cdd:PRK12273 320 SSIMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEER 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827578796 401 CESYVYNSIGIVTYLNPYIGHHNGDIVGKICAETGKSVRDVVLERGLLTAAELDDIFSAQNLMHPAYKAKRYT 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: 850.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 6 RIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISDIPEFVRGMVMVKKAAAQANKELQTIPKSVANAIIAACDEVLN 85
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPISDHPELIRALAMVKKAAALANRELGLLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 86 nGKCMDQFPVDVFQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASILKLID 165
Cdd:COG1027 81 -GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLALLLLLRELLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 166 AINQLGEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFNVLLNEETKCILRTAELLLEVNLGATAIGTRLNTPDGY 245
Cdd:COG1027 160 ALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 246 QQLAVQKLAEVSNLPVVPAEDLIEATSDCGAYVMVHSSLKRLAVKLSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMP 325
Cdd:COG1027 240 IELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 326 AKVNPVVPEVVNQVCFKVIGNDTTVTMASEAGQLQLNVMEPVIGQAMFESIHILTNACYNLLEKCVSGITANKAVCESYV 405
Cdd:COG1027 320 GKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYV 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 406 YNSIGIVTYLNPYIGHHNGDIVGKICAETGKSVRDVVLERGLLTAAELDDIFSAQNLMHP 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: 821.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 6 RIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISDIPEFVRGMVMVKKAAAQANKELQTIPKSVANAIIAACDEVLN 85
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKISDIPEFVRGMVMVKKAAALANKELGTIPESIANAIVAACDEILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 86 NGKCMDQFPVDVFQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASILKLID 165
Cdd:TIGR00839 81 NGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIAVYSSLIKLVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 166 AINQLGEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFNVLLNEETKCILRTAELLLEVNLGATAIGTRLNTPDGY 245
Cdd:TIGR00839 161 AINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 246 QQLAVQKLAEVSNLPVVPAEDLIEATSDCGAYVMVHSSLKRLAVKLSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMP 325
Cdd:TIGR00839 241 SPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 326 AKVNPVVPEVVNQVCFKVIGNDTTVTMASEAGQLQLNVMEPVIGQAMFESIHILTNACYNLLEKCVSGITANKAVCESYV 405
Cdd:TIGR00839 321 AKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGYV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827578796 406 YNSIGIVTYLNPYIGHHNGDIVGKICAETGKSVRDVVLERGLLTAAELDDIFSAQNLMHPAYKAKRYT 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: 786.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 6 RIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISdiPEFVRGMVMVKKAAAQANKELQTIPKSVANAIIAACDEVLN 85
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISGLKIH--PELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 86 nGKCMDQFPVDVFQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASILKLID 165
Cdd:cd01357 79 -GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLALILLLRKLLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 166 AINQLGEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFNVLLNEETKCILRTAELLLEVNLGATAIGTRLNTPDGY 245
Cdd:cd01357 158 ALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 246 QQLAVQKLAEVSNLPVVPAEDLIEATSDCGAYVMVHSSLKRLAVKLSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMP 325
Cdd:cd01357 238 IELVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 326 AKVNPVVPEVVNQVCFKVIGNDTTVTMASEAGQLQLNVMEPVIGQAMFESIHILTNACYNLLEKCVSGITANKAVCESYV 405
Cdd:cd01357 318 GKVNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1827578796 406 YNSIGIVTYLNPYIGHHNGDIVGKICAETGKSVRDVVLERGLLTAAELDDIFS 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: 742.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 4 NIRIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKIsdIPEFVRGMVMVKKAAAQANKELQTIPKSVANAIIAACDEV 83
Cdd:PRK13353 4 NMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYKI--HPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQACDEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 84 LNnGKCMDQFPVDVFQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASILKL 163
Cdd:PRK13353 82 LA-GKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLLEGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 164 IDAINQLGEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFNVLLNEETKCILRTAELLLEVNLGATAIGTRLNTPD 243
Cdd:PRK13353 161 LAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 244 GYQQLAVQKLAEVSNLPVVPAEDLIEATSDCGAYVMVHSSLKRLAVKLSKICNDLRLLSSGPRAGLNEINLPELQAGSSI 323
Cdd:PRK13353 241 EYIERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 324 MPAKVNPVVPEVVNQVCFKVIGNDTTVTMASEAGQLQLNVMEPVIGQAMFESIHILTNACYNLLEKCVSGITANKAVCES 403
Cdd:PRK13353 321 MPGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKE 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827578796 404 YVYNSIGIVTYLNPYIGHHNGDIVGKICAETGKSVRDVVLERGLLTAAELDDIFSAQNLMHPAYKAKRYTDE 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: 710.73 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 6 RIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISdiPEFVRGMVMVKKAAAQANKELQTIPKSVANAIIAACDEVLN 85
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISGERMP--PELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 86 nGKCMDQFPVDVFQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASILKLID 165
Cdd:cd01596 79 -GKLDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKGKYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 166 AINQLGEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFNVLLNEETKCILRTAELLLEVNLGATAIGTRLNTPDGY 245
Cdd:cd01596 158 ALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 246 QQLAVQKLAEVSNLPVVPAEDLIEATSDCGAYVMVHSSLKRLAVKLSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMP 325
Cdd:cd01596 238 AEKVAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 326 AKVNPVVPEVVNQVCFKVIGNDTTVTMASEAGQLQLNVMEPVIGQAMFESIHILTNACYNLLEKCVSGITANKAVCESYV 405
Cdd:cd01596 318 GKVNPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1827578796 406 YNSIGIVTYLNPYIGHHNGDIVGKICAETGKSVRDVVLERGLLTAAELDDIFS 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: 545.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 4 NIRIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISdiPEFVRGMVMVKKAAAQANKELQTIPKSVANAIIAACDEV 83
Cdd:COG0114 3 ETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGERMP--REFIRALALIKKAAARANAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 84 LNnGKCMDQFPVDVFQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASILK- 162
Cdd:COG0114 81 IA-GKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEEr 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 163 LIDAINQLGEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFNVLLNEETKCILRTAELLLEVNLGATAIGTRLNTP 242
Cdd:COG0114 160 LLPALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 243 DGYQQLAVQKLAEVSNLPVVPAEDLIEATSDCGAYVMVHSSLKRLAVKLSKICNDLRLLSSGPRAGLNEINLPELQAGSS 322
Cdd:COG0114 240 PGFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 323 IMPAKVNPVVPEVVNQVCFKVIGNDTTVTMASEAGQLQLNVMEPVIGQAMFESIHILTNACYNLLEKCVSGITANKAVCE 402
Cdd:COG0114 320 IMPGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIE 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1827578796 403 SYVYNSIGIVTYLNPYIGHHNGDIVGKICAETGKSVRDVVLERGLLTAAELDDI 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: 533.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 4 NIRIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISdiPEFVRGMVMVKKAAAQANKELQTIPKSVANAIIAACDEV 83
Cdd:PRK00485 3 ETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMP--RELIRALALLKKAAARVNAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 84 LNnGKCMDQFPVDVFQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASIL-K 162
Cdd:PRK00485 81 IA-GKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVeR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 163 LIDAINQLGEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFNVLLNEETKCILRTAELLLEVNLGATAIGTRLNTP 242
Cdd:PRK00485 160 LLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 243 DGYQQLAVQKLAEVSNLPVVPAEDLIEATSDCGAYVMVHSSLKRLAVKLSKICNDLRLLSSGPRAGLNEINLPELQAGSS 322
Cdd:PRK00485 240 PGFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 323 IMPAKVNPVVPEVVNQVCFKVIGNDTTVTMASEAGQLQLNVMEPVIGQAMFESIHILTNACYNLLEKCVSGITANKAVCE 402
Cdd:PRK00485 320 IMPGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIK 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827578796 403 SYVYNSIGIVTYLNPYIGHHNGDIVGKICAETGKSVRDVVLERGLLTAAELDDIFSAQNLMHP 465
Cdd:PRK00485 400 ELLERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGP 462
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
6-456 |
7.60e-179 |
|
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: 508.58 E-value: 7.60e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 6 RIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISdiPEFVRGMVMVKKAAAQANKELQTIPKSVANAIIAACDEVLN 85
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMP--RELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 86 nGKCMDQFPVDVFQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASILK-LI 164
Cdd:cd01362 79 -GKLDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQErLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 165 DAINQLGEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFNVLLNEETKCILRTAELLLEVNLGATAIGTRLNTPDG 244
Cdd:cd01362 158 PALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 245 YQQLAVQKLAEVSNLPVVPAEDLIEATSDCGAYVMVHSSLKRLAVKLSKICNDLRLLSSGPRAGLNEINLPELQAGSSIM 324
Cdd:cd01362 238 FAEKVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 325 PAKVNPVVPEVVNQVCFKVIGNDTTVTMASEAGQLQLNVMEPVIGQAMFESIHILTNACYNLLEKCVSGITANKAVCESY 404
Cdd:cd01362 318 PGKVNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAEL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1827578796 405 VYNSIGIVTYLNPYIGHHNGDIVGKICAETGKSVRDVVLERGLLTAAELDDI 456
Cdd:cd01362 398 LERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRL 449
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
12-465 |
3.02e-178 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 507.31 E-value: 3.02e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 12 LGTREVPADAYYGVHTLRAIENFYISNNKISDIPEFVRGMVMVKKAAAQANKELQTIPKSVANAIIAACDEVLNnGKCMD 91
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGGERERMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAE-GKLDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 92 QFPVDVFQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASIL-KLIDAINQL 170
Cdd:PLN00134 80 HFPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATEIHsRLIPALKEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 171 GEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFNVLLNEETKCILRTAELLLEVNLGATAIGTRLNTPDGYQQLAV 250
Cdd:PLN00134 160 HESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 251 QKLAEVSNLPVVPAEDLIEATSDCGAYVMVHSSLKRLAVKLSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMPAKVNP 330
Cdd:PLN00134 240 AAVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 331 VVPEVVNQVCFKVIGNDTTVTMASEAGQLQLNVMEPVIGQAMFESIHILTNACYNLLEKCVSGITANKAVCESYVYNSIG 410
Cdd:PLN00134 320 TQCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLM 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1827578796 411 IVTYLNPYIGHHNGDIVGKICAETGKSVRDVVLERGLLTAAELDDIFSAQNLMHP 465
Cdd:PLN00134 400 LVTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTGP 454
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
3-465 |
5.34e-165 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 474.49 E-value: 5.34e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 3 NNIRIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISdiPEFVRGMVMVKKAAAQANKELQTIPKSVANAIIAACDE 82
Cdd:PRK14515 9 NGVRIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGYKIH--EGLIKAFAIVKKAAALANTDVGRLELNKGGAIAEAAQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 83 VLNnGKCMDQFPVDVFQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASILK 162
Cdd:PRK14515 87 ILD-GKWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIATLNALEG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 163 LIDAINQLGEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFNVLLNEETKCILRTAELLLEVNLGATAIGTRLNTP 242
Cdd:PRK14515 166 LLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNAD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 243 DGYQQLAVQKLAEVSNLPVVPAEDLIEATSDCGAYVMVHSSLKRLAVKLSKICNDLRLLSSGPRAGLNEINLPELQAGSS 322
Cdd:PRK14515 246 PEYIEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 323 IMPAKVNPVVPEVVNQVCFKVIGNDTTVTMASEAGQLQLNVMEPVIGQAMFESIHILTNACYNLLEKCVSGITANKAVCE 402
Cdd:PRK14515 326 IMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLK 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827578796 403 SYVYNSIGIVTYLNPYIGHHNGDIVGKICAETGKSVRDVVLERGLLTAAELDDIFSAQNLMHP 465
Cdd:PRK14515 406 EYVEKSVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEMTHP 468
|
|
| fumC_II |
TIGR00979 |
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ... |
6-456 |
1.21e-150 |
|
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: 437.24 E-value: 1.21e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 6 RIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISdiPEFVRGMVMVKKAAAQANKELQTIPKSVANAIIAACDEVLN 85
Cdd:TIGR00979 2 RIEKDSMGEIQVPADKYWGAQTQRSLENFKIGTEKMP--LELIHAFAILKKAAAIVNEDLGKLDAKKADAIVQAADEILA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 86 nGKCMDQFPVDVFQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIAVYASIL-KLI 164
Cdd:TIGR00979 80 -GKLDDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKnQLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 165 DAINQLGEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFNVLLNEETKCILRTAELLLEVNLGATAIGTRLNTPDG 244
Cdd:TIGR00979 159 PALENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 245 YQQLAVQKLAEVSNLPVVPAEDLIEATSDCGAYVMVHSSLKRLAVKLSKICNDLRLLSSGPRAGLNEINLPELQAGSSIM 324
Cdd:TIGR00979 239 FDEKVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 325 PAKVNPVVPEVVNQVCFKVIGNDTTVTMASEAGQLQLNVMEPVIGQAMFESIHILTNACYNLLEKCVSGITANKAVCESY 404
Cdd:TIGR00979 319 PGKVNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1827578796 405 VYNSIGIVTYLNPYIGHHNGDIVGKICAETGKSVRDVVLERGLLTAAELDDI 456
Cdd:TIGR00979 399 LNNSLMLVTALNPHIGYDNAAKIAKKAHKEGITLKEAALELGLLSEEEFDEW 450
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
13-345 |
1.23e-118 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 350.13 E-value: 1.23e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 13 GTREVPADAYYGVHTLRAIENFYISNNKIsdipefvRGMVMVKKAAAQANKelqtIPKSVANAIIAACDEVLNNGKCMDQ 92
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDI-------KGLAALKKAAAKANV----ILKEEAAAIIKALDEVAEEGKLDDQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 93 FPVDVFQGGAGTSVNMNTNEVLAniglELMGhqkgeyQYLNPNDHVNKCQSTNDAYPTGFRIAVYASIL-KLIDAINQLG 171
Cdd:pfam00206 70 FPLKVWQEGSGTAVNMNLNEVIG----ELLG------QLVHPNDHVHTGQSSNDQVPTALRLALKDALSeVLLPALRQLI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 172 EGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFNVLLNEETKCILR-TAELLLEVNLGATAIGTRLNTPDGYQQLAV 250
Cdd:pfam00206 140 DALKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQlLPRLLVLPLGGGTAVGTGLNADPEFAELVA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 251 QKLAEVSNLPvVPAEDLIEATSDCGAYVMVHSSLKRLAVKLSKICNDLRLLSSGPrAGLNEINLPELQAGSSIMPAKVNP 330
Cdd:pfam00206 220 KELGFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNP 297
|
330
....*....|....*
gi 1827578796 331 VVPEVVNQVCFKVIG 345
Cdd:pfam00206 298 DQLELLTGKAGRVMG 312
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
6-468 |
9.15e-116 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 348.45 E-value: 9.15e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 6 RIEEDLLGTREVPADAYYGVHTLRAIENFYISNNKISdiPEFVRGMVMVKKAAAQANKELQTIPKSVANAIIAACDEVLN 85
Cdd:PRK12425 3 RTETDSLGPIEVPEDAYWGAQTQRSLINFAIGKERMP--LAVLHALALIKKAAARVNDRNGDLPADIARLIEQAADEVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 86 nGKCMDQFPVDVFQGGAGTSVNMNTNEVLANIGLELMGHQKGEYQYLNPNDHVNKCQSTNDAYPTGFRIA-VYASILKLI 164
Cdd:PRK12425 81 -GQHDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAaAQAVHEQLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 165 DAINQLGEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFNVLLNEETKCILRTAELLLEVNLGATAIGTRLNTPDG 244
Cdd:PRK12425 160 PAIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 245 YQQLAVQKLAEVSNLPVVPAEDLIEATSDCGAYVMVHSSLKRLAVKLSKICNDLRLLSSGPRAGLNEINLPELQAGSSIM 324
Cdd:PRK12425 240 FAEAIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 325 PAKVNPVVPEVVNQVCFKVIGNDTTVTMASEAGQLQLNVMEPVIGQAMFESIHILTNACYNLLEKCVSGITANKAVCESY 404
Cdd:PRK12425 320 PGKVNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAH 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827578796 405 VYNSIGIVTYLNPYIGHHNGDIVGKICAETGKSVRDVVLERGLLTAAELDDIFSAQNLMHPAYK 468
Cdd:PRK12425 400 LERGLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEAGGH 463
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
48-397 |
4.12e-101 |
|
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: 305.58 E-value: 4.12e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 48 VRGMVMVKKAAAQANKELQTIPKSVANAIIAACDEVLNngkcmDQFPVDVFQGGAGTSVNMNTNEVLANIGLELmghqkg 127
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILE-----GIAADQVEQEGSGTHDVMAVEEVLAERAGEL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 128 eyqylnPNDHVNKCQSTNDAYPTGFRIAVYASILKLIDAINQLGEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAF 207
Cdd:cd01334 70 ------NGGYVHTGRSSNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 208 NVLLNEETKCILRTAELLLEVNLGATAIGTRLNTPDGYQQLAVQKLAEVSnlpvvPAEDLIEATSDCGAYVMVHSSLKRL 287
Cdd:cd01334 144 AAELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAELLGFFG-----PAPNSTQAVSDRDFLVELLSALALL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 288 AVKLSKICNDLRLLSSGpraGLNEINLPE-LQAGSSIMPAKVNPVVPEVVNQVCFKVIGNDTTVTMASEAGQLQLNVMEP 366
Cdd:cd01334 219 AVSLSKIANDLRLLSSG---EFGEVELPDaKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSP 295
|
330 340 350
....*....|....*....|....*....|.
gi 1827578796 367 VIGQAMFESIHILTNACYNLLEKCvSGITAN 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 |
6.95e-48 |
|
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: 164.70 E-value: 6.95e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 108 MNTNEVLANIGLELMGHQKGEYqylnpndHVNKCQSTNDAYPTGFRIAVYASILKLIDAINQLGEGFQQKAVEFQDILKM 187
Cdd:cd01594 14 ALVEEVLAGRAGELAGGLHGSA-------LVHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 188 GRTQLQDAVPMTLGQEFHAFnvllneetkcilrtaelllevnlgataigtrlntpdgYQQLAVQklaevsnlpvvpAEDL 267
Cdd:cd01594 87 GRTHLQDAQPVTLGYELRAW-------------------------------------AQVLGRD------------LERL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 268 IEAtsdcgAYVMVHSSLKRLAVKLSKICNDLRLLSSGPRAGLNEINLPeLQAGSSIMPAKVNPVVPEVVNQVCFKVIGND 347
Cdd:cd01594 118 EEA-----AVAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGNL 191
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1827578796 348 TTVTMASEAGQLQLNVMEPVIGQAMFESIHILTNACYNLL 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 |
1.51e-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: 76.20 E-value: 1.51e-17
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1827578796 411 IVTYLNPYIGHHNGDIVGKICAETGKSVRDVVLERGLLTAAELDDIFSAQNL 462
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
48-327 |
7.06e-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: 60.60 E-value: 7.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 48 VRGMVMVKKAAAQANKELQTIPKSVANAIIAACDEvlnngkcmdqFPVDVFQGGAGTSVNMNtnEVLA---NIGlELMGH 124
Cdd:cd01595 11 LRTWLDVEAALAEAQAELGLIPKEAAEEIRAAADV----------FEIDAERIAEIEKETGH--DVIAfvyALA-EKCGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 125 QKGEYQYLNpndhvnkCQST--NDaypTGFRIAVYASILKLIDAINQLGEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQ 202
Cdd:cd01595 78 DAGEYVHFG-------ATSQdiND---TALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 203 EFHAFnvlLNEETKCILRTAELLLEVNLGAT--AIGTRLN-TPDGyqqLAVQK-LAEVSNLPVVPAEDLIEatsDCGAYV 278
Cdd:cd01595 148 KFAVW---AAELLRHLERLEEARERVLVGGIsgAVGTHASlGPKG---PEVEErVAEKLGLKVPPITTQIE---PRDRIA 218
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1827578796 279 MVHSSLKRLAVKLSKICNDLRLLSsgpRAGLNEINLP--ELQAGSSIMPAK 327
Cdd:cd01595 219 ELLSALALIAGTLEKIATDIRLLQ---RTEIGEVEEPfeKGQVGSSTMPHK 266
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
143-459 |
1.41e-09 |
|
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: 60.06 E-value: 1.41e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 143 STNDAYPTGFRIAVYASILKLIDAINQLGEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFNVLLNEEtkcILRTA 222
Cdd:TIGR00838 106 SRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLRD---YERLQ 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 223 ELLLEVN---LGATAI-GTRLNTPDGY--QQLAVQKLAEVSnLPVVPAEDLI-EATSDCgAYVMVHsslkrlavkLSKIC 295
Cdd:TIGR00838 183 DALKRVNvspLGSGALaGTGFPIDREYlaELLGFDAVTENS-LDAVSDRDFIlELLFVA-ALIMVH---------LSRFA 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 296 NDLRLLSSGPragLNEINLP-ELQAGSSIMPAKVNPVVPEVVNQVCFKVIGNDTTVTMASEAGQLQLNVMEPVIGQAMFE 374
Cdd:TIGR00838 252 EDLILWSTGE---FGFVELPdEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQEDKEPLFD 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 375 SIHILTNaCYNLLEKCVSGITANKAVCESYVYNSIGIVTYLNPYI---------GHHngdIVGKI---CAETGKSVRDVV 442
Cdd:TIGR00838 329 ALKTVEL-SLEMATGMLDTITVNKERMEEAASAGFSNATELADYLvrkgvpfreAHH---IVGELvatAIERGKGLEELT 404
|
330
....*....|....*...
gi 1827578796 443 LERGLLTAAELD-DIFSA 459
Cdd:TIGR00838 405 LEELQKFSPEFDeDVYEA 422
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
47-461 |
1.92e-08 |
|
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: 56.25 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 47 FVRGMVMVKKAAAQANKELQTIPKSVANAIIAACDEvlnngkcmdqFPVDVFQGGAGTSVnmnTN-EVLA---NIGlELM 122
Cdd:COG0015 20 KIRAWLDVEIALAEAQAELGLIPAEAAAAIRAAADD----------FEIDAERIKEIEKE---TRhDVKAfvyALK-EKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 123 GHQKGEY-------QYLNpndhvnkcqstnDaypTGFRIAVYASILKLIDAINQLGEGFQQKAVEFQDILKMGRTQLQDA 195
Cdd:COG0015 86 GAEAGEYihfgatsQDIN------------D---TALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 196 VPMTLGQEFhAfnVLLNEETKCILRTAELLLEVNLGAT--AIGTRLNTPDGYQQLAvQKLAEVSNLPVVPAE------DL 267
Cdd:COG0015 151 EPTTFGKKL-A--VWAAELLRQLERLEEARERVLVGKIggAVGTYAAHGEAWPEVE-ERVAEKLGLKPNPVTtqieprDR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 268 IeatsdcgAYVMvhSSLKRLAVKLSKICNDLRLLSSgpraglNEINlpEL-------QAGSSIMP--------------A 326
Cdd:COG0015 227 H-------AELF--SALALIAGSLEKIARDIRLLQR------TEVG--EVeepfakgQVGSSAMPhkrnpidsenieglA 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 327 KvnpvvpevvnqvcfKVIGNdttVTMASEAGQLQL------NVMEPVIGQAMFesihILTNACYNLLEKCVSGITANKAV 400
Cdd:COG0015 290 R--------------LARAL---AAALLEALASWHerdlsdSSVERNILPDAF----LLLDGALERLLKLLEGLVVNPER 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 401 CESYVYNSIG------IVTYL--------NPYighhngDIVGKIC---AETGKSVRDVVLE----RGLLTAAELDDIFSA 459
Cdd:COG0015 349 MRANLDLTGGlvlseaVLMALvrrglgreEAY------ELVKELArgaWEEGNDLRELLAAdpeiPAELSKEELEALFDP 422
|
..
gi 1827578796 460 QN 461
Cdd:COG0015 423 AN 424
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
143-327 |
3.30e-08 |
|
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASAL is a cytosolic enzyme which catalyzes the reversible breakdown of argininosuccinate to arginine and fumarate during arginine biosynthesis. In ureotelic species ASAL also catalyzes a reaction involved in the production of urea. Included in this group are the major soluble avian eye lens proteins from duck, delta 1 and delta 2 crystallin. Of these two isoforms only delta 2 has retained ASAL activity. These crystallins may have evolved by, gene recruitment of ASAL followed by gene duplication. In humans, mutations in ASAL result in the autosomal recessive disorder argininosuccinic aciduria.
Pssm-ID: 176463 [Multi-domain] Cd Length: 435 Bit Score: 55.63 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 143 STNDAYPTGFRIAVYASILKLIDAINQLGEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFNVLLNEETKcilRTA 222
Cdd:cd01359 86 SRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLE---RLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 223 ELLLEVN---LGATAIGTrlntpdgyqqlavqklaevSNLPVVP---AEDL---------IEATSD---------CGAYV 278
Cdd:cd01359 163 DAYKRVNvspLGAGALAG-------------------TTFPIDRertAELLgfdgptensLDAVSDrdfvleflsAAALL 223
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1827578796 279 MVHsslkrlavkLSKICNDLRLLSSgpraglNEINLPELQA----GSSIMPAK 327
Cdd:cd01359 224 MVH---------LSRLAEDLILWST------QEFGFVELPDaystGSSIMPQK 261
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
163-327 |
5.77e-08 |
|
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: 55.05 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 163 LIDAINQLGEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFhafnVLLNEETK---CILRTAELLLEVNLGATAIGTRL 239
Cdd:TIGR00928 116 ILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRF----ALWAEEMLrqlERLLQAKERIKVGGISGAVGTHA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 240 NTPDGYQQLAvQKLAEVSNLPVVPAEDLIEATSDCGAYVMVhssLKRLAVKLSKICNDLRLLSsgpRAGLNEINLP--EL 317
Cdd:TIGR00928 192 AAYPLVEEVE-ERVTEFLGLKPVPISTQIEPRDRHAELLDA---LALLATTLEKFAVDIRLLQ---RTEHFEVEEPfgKG 264
|
170
....*....|
gi 1827578796 318 QAGSSIMPAK 327
Cdd:TIGR00928 265 QVGSSAMPHK 274
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
163-327 |
1.12e-07 |
|
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: 53.71 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 163 LIDAINQLGEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFnvlLNEETKCILRTAELLLEVNLGAT--AIGTRLN 240
Cdd:cd01360 110 ILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALW---YAEFKRHLERLKEARERILVGKIsgAVGTYAN 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 241 TPDGYQQLAVQKL----AEVSNlPVVPAEDLIEatsdcgaYVMVhssLKRLAVKLSKICNDLRLLSsgpRAGLNEINLP- 315
Cdd:cd01360 187 LGPEVEERVAEKLglkpEPIST-QVIQRDRHAE-------YLST---LALIASTLEKIATEIRHLQ---RTEVLEVEEPf 252
|
170
....*....|...
gi 1827578796 316 -ELQAGSSIMPAK 327
Cdd:cd01360 253 sKGQKGSSAMPHK 265
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
48-327 |
6.61e-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: 51.48 E-value: 6.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 48 VRGMVMVKKAAAQANKELQTIPKSVANAIIAACD-EVLNngkcMDQFPVDVfqGGAGTSVnmntnevlanIGL-----EL 121
Cdd:cd01597 21 VQAMLDVEAALARAQAELGVIPKEAAAEIAAAADvERLD----LEALAEAT--ARTGHPA----------IPLvkqltAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 122 MGHQKGEYqylnpndhVNKCQSTNDAYPTgfriavyASILKLIDA-------INQLGEGFQQKAVEFQDILKMGRTQLQD 194
Cdd:cd01597 85 CGDAAGEY--------VHWGATTQDIIDT-------ALVLQLRDAldllerdLDALLDALARLAATHRDTPMVGRTHLQH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 195 AVPMTLGqefHAFNVLLNEETKCILRTAEL---LLEVNLGAtAIGTRLNTPDgyQQLAVQK-LAEVSNLPVVP-----AE 265
Cdd:cd01597 150 ALPITFG---LKVAVWLSELLRHRERLDELrprVLVVQFGG-AAGTLASLGD--QGLAVQEaLAAELGLGVPAipwhtAR 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827578796 266 D-LIEATSDCGAyvmvhsslkrLAVKLSKICNDLRLLSsgpRAGLNEINLPELQA--GSSIMPAK 327
Cdd:cd01597 224 DrIAELASFLAL----------LTGTLGKIARDVYLLM---QTEIGEVAEPFAKGrgGSSTMPHK 275
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
135-327 |
6.65e-07 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 51.69 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 135 NDHVnkcqstndAypTGFRIAVYASILKLIDAINQLGEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFNVLLNEE 214
Cdd:PRK00855 112 NDQV--------A--TDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARD 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 215 TKcILRTAELLLEVN-LGATAI-GTRLNTPDGY--QQLAVQKLAEVSnLPVVPAED-LIEATSDCgAYVMVHsslkrlav 289
Cdd:PRK00855 182 LE-RLRDARKRVNRSpLGSAALaGTTFPIDRERtaELLGFDGVTENS-LDAVSDRDfALEFLSAA-SLLMVH-------- 250
|
170 180 190
....*....|....*....|....*....|....*....
gi 1827578796 290 kLSKICNDLRLLSSgPRAGLneINLP-ELQAGSSIMPAK 327
Cdd:PRK00855 251 -LSRLAEELILWSS-QEFGF--VELPdAFSTGSSIMPQK 285
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
143-327 |
2.67e-05 |
|
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: 46.63 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 143 STNDAYPTGFRIAVYASILKLIDAINQLGEGFQQKAVEFQDILkM-GRTQLQDAVPMTLGQEFHA-FNVLLneetkcilR 220
Cdd:COG0165 109 SRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTI-MpGYTHLQRAQPVTFGHHLLAyAEMLL--------R 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 221 TAELLLE----VN---LGATAIGTrlntpdgyqqlavqklaevSNLPVVP---AEDL---------IEATSDCGAYVMVH 281
Cdd:COG0165 180 DRERLADaykrLNvspLGAAALAG-------------------TTFPIDRertAELLgfdgptensLDAVSDRDFALEFL 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1827578796 282 SSLKRLAVKLSKICNDLRLLSSgPRAGLneINLPELQA-GSSIMPAK 327
Cdd:COG0165 241 SAASLIMVHLSRLAEELILWSS-SEFGF--VELPDAFStGSSIMPQK 284
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
48-327 |
2.96e-04 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 43.08 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 48 VRGMVMVKKAAAQANKELQTIPKSVANAIIAACDevlnngkcMDQFPVDVFQGGAGTSVNMNTNEVLAnIGLELMGHQKG 127
Cdd:PRK09053 27 VQRMLDFEAALARAEAACGVIPAAAVAPIEAACD--------AERLDLDALAQAAALAGNLAIPLVKQ-LTAQVAARDAE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 128 EYQYlnpndhVNKCQSTNDAYPTGFRIAVYASILKLIDAINQLGEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAF 207
Cdd:PRK09053 98 AARY------VHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGW 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 208 nvlLNEETKCILRTAEL---LLEVNLGATAiGTRLNTpdGYQQLAV-QKLAEVSNL--PVVP---AEDLIeatsdcgayV 278
Cdd:PRK09053 172 ---LDALLRHRQRLAALrprALVLQFGGAA-GTLASL--GEQALPVaQALAAELQLalPALPwhtQRDRI---------A 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1827578796 279 MVHSSLKRLAVKLSKICNDLRLLSSGPRAGLNEINLPElQAGSSIMPAK 327
Cdd:PRK09053 237 EFASALGLLAGTLGKIARDVSLLMQTEVGEVFEPAAAG-KGGSSTMPHK 284
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
135-327 |
6.22e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 42.28 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 135 NDHVNKcqSTNDAYPTGFRIAVYASILKLIDAINQLGEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFNVLLNEE 214
Cdd:PRK06705 109 NMHIGR--SRNDMGVTMYRMSLRRYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRD 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 215 TKCILRTAELLLEVNLGATAIGTR---LNTPDGYQQLAVQKLAEVSNLPVVPAEDLIEATSdcgaYVMVhsslkrLAVKL 291
Cdd:PRK06705 187 LERMKKTYKLLNQSPMGAAALSTTsfpIKRERVADLLGFTNVIENSYDAVAGADYLLEVSS----LLMV------MMTNT 256
|
170 180 190
....*....|....*....|....*....|....*.
gi 1827578796 292 SKICNDLRLLSSGPRAGLNEINlPELQAgSSIMPAK 327
Cdd:PRK06705 257 SRWIHDFLLLATKEYDGITVAR-PYVQI-SSIMPQK 290
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
162-327 |
2.46e-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: 40.38 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 162 KLIDAINQLgegfQQKAVEFQDILKMGRTQLQDAVPMTLGQEFhafnVLLNEETKCILRTAELLLEvNLGATAIGTRLNT 241
Cdd:cd03302 118 KLAAVIDRL----AEFALEYKDLPTLGFTHYQPAQLTTVGKRA----CLWIQDLLMDLRNLERLRD-DLRFRGVKGTTGT 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 242 PDGYQQLAVQKLAEVSNLPVVPAEDLIEATSDC---GAY-----VMVHSSLKRLAVKLSKICNDLRLLssgprAGLNEIN 313
Cdd:cd03302 189 QASFLDLFEGDHDKVEALDELVTKKAGFKKVYPvtgQTYsrkvdIDVLNALSSLGATAHKIATDIRLL-----ANLKEVE 263
|
170
....*....|....*.
gi 1827578796 314 LP--ELQAGSSIMPAK 327
Cdd:cd03302 264 EPfeKGQIGSSAMPYK 279
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
145-233 |
7.07e-03 |
|
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: 38.76 E-value: 7.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827578796 145 NDAYPTGFRIAVYASILKLIDAInqlGEGFQQKAVEFQDILKMGRTQLQDAVPMTLGQEFHAFNVLLNEETKcILRTAEL 224
Cdd:cd01598 106 NLAYALMIKEARNEVILPLLKEI---IDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYK-QLKQIEI 181
|
....*....
gi 1827578796 225 LLEVNlGAT 233
Cdd:cd01598 182 LGKFN-GAV 189
|
|
| |
