|
Name |
Accession |
Description |
Interval |
E-value |
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
11-483 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 944.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 11 ANQATRIEEDLLGQRHVPADAYYGIHTLRAIENFNISSTTISDVPEFVRGMVMTKKAAALANKELGAIPKDVANYILEAC 90
Cdd:PRK12273 1 MMMNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKISDYPELIRALAMVKKAAALANKELGLLDEEKADAIVAAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 91 DLILEtGKCMDQFPSDVFQGGAGTSVNMNTNEVIANVALELMGKEKGQYEFINPNDHVNKSQSTNCAYPTGFRIAVYNSV 170
Cdd:PRK12273 81 DEILA-GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIALLLSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 171 HQLMEAIEYLKGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEEIRALDYTSKLLLEINLGATAIGTGLN 250
Cdd:PRK12273 160 RKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 251 APTGYQALAVKHLAEVTGVEVVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRAGLNELNLPEMQAG 330
Cdd:PRK12273 240 APPGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 331 SSIMPAKVNPVIPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSVFESISLLHNACVNLRDKCIDGITVNKEV 410
Cdd:PRK12273 320 SSIMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEER 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491571196 411 CENYVYNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLTAEELDDILSVENFMHPTYKAKRYE 483
Cdd:PRK12273 400 CREYVENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTHPGYKGKRYT 472
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
16-475 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 888.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 16 RIEEDLLGQRHVPADAYYGIHTLRAIENFNISSTTISDVPEFVRGMVMTKKAAALANKELGAIPKDVANYILEACDLILE 95
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPISDHPELIRALAMVKKAAALANRELGLLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 96 tGKCMDQFPSDVFQGGAGTSVNMNTNEVIANVALELMGKEKGQYEFINPNDHVNKSQSTNCAYPTGFRIAVYNSVHQLME 175
Cdd:COG1027 81 -GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLALLLLLRELLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 176 AIEYLKGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEEIRALDYTSKLLLEINLGATAIGTGLNAPTGY 255
Cdd:COG1027 160 ALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 256 QALAVKHLAEVTGVEVVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRAGLNELNLPEMQAGSSIMP 335
Cdd:COG1027 240 IELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 336 AKVNPVIPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSVFESISLLHNACVNLRDKCIDGITVNKEVCENYV 415
Cdd:COG1027 320 GKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYV 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 416 YNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLTAEELDDILSVENFMHP 475
Cdd:COG1027 400 ENSIGLVTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGLLTEEELDEILDPENMTGP 459
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
16-468 |
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: 806.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 16 RIEEDLLGQRHVPADAYYGIHTLRAIENFNISSTTISdvPEFVRGMVMTKKAAALANKELGAIPKDVANYILEACDLILE 95
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISGLKIH--PELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 96 tGKCMDQFPSDVFQGGAGTSVNMNTNEVIANVALELMGKEKGQYEFINPNDHVNKSQSTNCAYPTGFRIAVYNSVHQLME 175
Cdd:cd01357 79 -GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLALILLLRKLLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 176 AIEYLKGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEEIRALDYTSKLLLEINLGATAIGTGLNAPTGY 255
Cdd:cd01357 158 ALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 256 QALAVKHLAEVTGVEVVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRAGLNELNLPEMQAGSSIMP 335
Cdd:cd01357 238 IELVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 336 AKVNPVIPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSVFESISLLHNACVNLRDKCIDGITVNKEVCENYV 415
Cdd:cd01357 318 GKVNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 491571196 416 YNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLTAEELDDILS 468
Cdd:cd01357 398 ENSIGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELDEILS 450
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
16-482 |
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: 800.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 16 RIEEDLLGQRHVPADAYYGIHTLRAIENFNISSTTISDVPEFVRGMVMTKKAAALANKELGAIPKDVANYILEACDLILE 95
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKISDIPEFVRGMVMVKKAAALANKELGTIPESIANAIVAACDEILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 96 TGKCMDQFPSDVFQGGAGTSVNMNTNEVIANVALELMGKEKGQYEFINPNDHVNKSQSTNCAYPTGFRIAVYNSVHQLME 175
Cdd:TIGR00839 81 NGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIAVYSSLIKLVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 176 AIEYLKGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEEIRALDYTSKLLLEINLGATAIGTGLNAPTGY 255
Cdd:TIGR00839 161 AINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 256 QALAVKHLAEVTGVEVVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRAGLNELNLPEMQAGSSIMP 335
Cdd:TIGR00839 241 SPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 336 AKVNPVIPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSVFESISLLHNACVNLRDKCIDGITVNKEVCENYV 415
Cdd:TIGR00839 321 AKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGYV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 491571196 416 YNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLTAEELDDILSVENFMHPTYKAKRY 482
Cdd:TIGR00839 401 FNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLMHPAYKAKRY 467
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
16-468 |
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: 750.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 16 RIEEDLLGQRHVPADAYYGIHTLRAIENFNISSTTISdvPEFVRGMVMTKKAAALANKELGAIPKDVANYILEACDLILE 95
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISGERMP--PELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 96 tGKCMDQFPSDVFQGGAGTSVNMNTNEVIANVALELMGKEKGQYEFINPNDHVNKSQSTNCAYPTGFRIAVYNSVHQLME 175
Cdd:cd01596 79 -GKLDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKGKYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 176 AIEYLKGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEEIRALDYTSKLLLEINLGATAIGTGLNAPTGY 255
Cdd:cd01596 158 ALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 256 QALAVKHLAEVTGVEVVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRAGLNELNLPEMQAGSSIMP 335
Cdd:cd01596 238 AEKVAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 336 AKVNPVIPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSVFESISLLHNACVNLRDKCIDGITVNKEVCENYV 415
Cdd:cd01596 318 GKVNPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 491571196 416 YNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLTAEELDDILS 468
Cdd:cd01596 398 ENSLMLVTALNPHIGYEKAAEIAKEALKEGRTLREAALELGLLTEEELDEILD 450
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
11-482 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 742.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 11 ANQATRIEEDLLGQRHVPADAYYGIHTLRAIENFNISSTTIsdVPEFVRGMVMTKKAAALANKELGAIPKDVANYILEAC 90
Cdd:PRK13353 1 TNKNMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYKI--HPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQAC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 91 DLILEtGKCMDQFPSDVFQGGAGTSVNMNTNEVIANVALELMGKEKGQYEFINPNDHVNKSQSTNCAYPTGFRIAVYNSV 170
Cdd:PRK13353 79 DEILA-GKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 171 HQLMEAIEYLKGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEEIRALDYTSKLLLEINLGATAIGTGLN 250
Cdd:PRK13353 158 EGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 251 APTGYQALAVKHLAEVTGVEVVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRAGLNELNLPEMQAG 330
Cdd:PRK13353 238 ADPEYIERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 331 SSIMPAKVNPVIPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSVFESISLLHNACVNLRDKCIDGITVNKEV 410
Cdd:PRK13353 318 SSIMPGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEER 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491571196 411 CENYVYNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLTAEELDDILSVENFMHPTYKAKRY 482
Cdd:PRK13353 398 CKEYVEKSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMTHPGIAGATL 469
|
|
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
13-471 |
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: 596.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 13 QATRIEEDLLGQRHVPADAYYGIHTLRAIENFNISSTTISdvPEFVRGMVMTKKAAALANKELGAIPKDVANYILEACDL 92
Cdd:COG0114 2 METRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGERMP--REFIRALALIKKAAARANAELGLLDAEKADAIVAAADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 93 ILEtGKCMDQFPSDVFQGGAGTSVNMNTNEVIANVALELMGKEKGQYEFINPNDHVNKSQSTNCAYPTGFRIAVYNSVH- 171
Cdd:COG0114 80 VIA-GKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEe 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 172 QLMEAIEYLKGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEEIRALDYTSKLLLEINLGATAIGTGLNA 251
Cdd:COG0114 159 RLLPALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 252 PTGYQALAVKHLAEVTGVEVVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRAGLNELNLPEMQAGS 331
Cdd:COG0114 239 HPGFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 332 SIMPAKVNPVIPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSVFESISLLHNACVNLRDKCIDGITVNKEVC 411
Cdd:COG0114 319 SIMPGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERI 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 412 ENYVYNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLTAEELDDILSVEN 471
Cdd:COG0114 399 EELLERSLMLVTALNPHIGYDKAAKIAKKAHKEGRTLREAALELGLLSEEEFDRLVDPEK 458
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
13-475 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 588.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 13 QATRIEEDLLGQRHVPADAYYGIHTLRAIENFNISSTTISdvPEFVRGMVMTKKAAALANKELGAIPKDVANYILEACDL 92
Cdd:PRK00485 2 METRIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMP--RELIRALALLKKAAARVNAELGLLDAEKADAIVAAADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 93 ILEtGKCMDQFPSDVFQGGAGTSVNMNTNEVIANVALELMGKEKGQYEFINPNDHVNKSQSTNCAYPTGFRIAVYNSV-H 171
Cdd:PRK00485 80 VIA-GKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIvE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 172 QLMEAIEYLKGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEEIRALDYTSKLLLEINLGATAIGTGLNA 251
Cdd:PRK00485 159 RLLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 252 PTGYQALAVKHLAEVTGVEVVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRAGLNELNLPEMQAGS 331
Cdd:PRK00485 239 HPGFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 332 SIMPAKVNPVIPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSVFESISLLHNACVNLRDKCIDGITVNKEVC 411
Cdd:PRK00485 319 SIMPGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERI 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491571196 412 ENYVYNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLTAEELDDILSVENFMHP 475
Cdd:PRK00485 399 KELLERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGP 462
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
16-467 |
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: 555.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 16 RIEEDLLGQRHVPADAYYGIHTLRAIENFNISSTTISdvPEFVRGMVMTKKAAALANKELGAIPKDVANYILEACDLILE 95
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMP--RELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 96 tGKCMDQFPSDVFQGGAGTSVNMNTNEVIANVALELMGKEKGQYEFINPNDHVNKSQSTNCAYPTGFRIAVYNSVH-QLM 174
Cdd:cd01362 79 -GKLDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQeRLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 175 EAIEYLKGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEEIRALDYTSKLLLEINLGATAIGTGLNAPTG 254
Cdd:cd01362 158 PALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 255 YQALAVKHLAEVTGVEVVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRAGLNELNLPEMQAGSSIM 334
Cdd:cd01362 238 FAEKVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 335 PAKVNPVIPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSVFESISLLHNACVNLRDKCIDGITVNKEVCENY 414
Cdd:cd01362 318 PGKVNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAEL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 491571196 415 VYNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLTAEELDDIL 467
Cdd:cd01362 398 LERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRLV 450
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
22-478 |
0e+00 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 521.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 22 LGQRHVPADAYYGIHTLRAIENFNISSTTISDVPEFVRGMVMTKKAAALANKELGAIPKDVANYILEACDLILEtGKCMD 101
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGGERERMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAE-GKLDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 102 QFPSDVFQGGAGTSVNMNTNEVIANVALELMGKEKGQYEFINPNDHVNKSQSTNCAYPTGFRIAVYNSVHQ-LMEAIEYL 180
Cdd:PLN00134 80 HFPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATEIHSrLIPALKEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 181 KGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEEIRALDYTSKLLLEINLGATAIGTGLNAPTGYQALAV 260
Cdd:PLN00134 160 HESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 261 KHLAEVTGVEVVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRAGLNELNLPEMQAGSSIMPAKVNP 340
Cdd:PLN00134 240 AAVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 341 VIPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSVFESISLLHNACVNLRDKCIDGITVNKEVCENYVYNSIG 420
Cdd:PLN00134 320 TQCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLM 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 491571196 421 IVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLTAEELDDILSVENFMHPTYK 478
Cdd:PLN00134 400 LVTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTGPSDL 457
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
13-475 |
1.86e-174 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 498.76 E-value: 1.86e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 13 QATRIEEDLLGQRHVPADAYYGIHTLRAIENFNISSTTISdvPEFVRGMVMTKKAAALANKELGAIPKDVANYILEACDL 92
Cdd:PRK14515 9 NGVRIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGYKIH--EGLIKAFAIVKKAAALANTDVGRLELNKGGAIAEAAQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 93 ILEtGKCMDQFPSDVFQGGAGTSVNMNTNEVIANVALELMGKEKGQYEFINPNDHVNKSQSTNCAYPTGFRIAVYNSVHQ 172
Cdd:PRK14515 87 ILD-GKWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIATLNALEG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 173 LMEAIEYLKGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEEIRALDYTSKLLLEINLGATAIGTGLNAP 252
Cdd:PRK14515 166 LLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNAD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 253 TGYQALAVKHLAEVTGVEVVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRAGLNELNLPEMQAGSS 332
Cdd:PRK14515 246 PEYIEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 333 IMPAKVNPVIPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSVFESISLLHNACVNLRDKCIDGITVNKEVCE 412
Cdd:PRK14515 326 IMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLK 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491571196 413 NYVYNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLTAEELDDILSVENFMHP 475
Cdd:PRK14515 406 EYVEKSVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEMTHP 468
|
|
| fumC_II |
TIGR00979 |
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ... |
16-471 |
3.55e-159 |
|
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: 459.20 E-value: 3.55e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 16 RIEEDLLGQRHVPADAYYGIHTLRAIENFNISSTTISdvPEFVRGMVMTKKAAALANKELGAIPKDVANYILEACDLILE 95
Cdd:TIGR00979 2 RIEKDSMGEIQVPADKYWGAQTQRSLENFKIGTEKMP--LELIHAFAILKKAAAIVNEDLGKLDAKKADAIVQAADEILA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 96 tGKCMDQFPSDVFQGGAGTSVNMNTNEVIANVALELMGKEKGQYEFINPNDHVNKSQSTNCAYPTGFRIAVYNSV-HQLM 174
Cdd:TIGR00979 80 -GKLDDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDTFPTAMHIAAVLAIkNQLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 175 EAIEYLKGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEEIRALDYTSKLLLEINLGATAIGTGLNAPTG 254
Cdd:TIGR00979 159 PALENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 255 YQALAVKHLAEVTGVEVVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRAGLNELNLPEMQAGSSIM 334
Cdd:TIGR00979 239 FDEKVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 335 PAKVNPVIPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSVFESISLLHNACVNLRDKCIDGITVNKEVCENY 414
Cdd:TIGR00979 319 PGKVNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 491571196 415 VYNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLTAEELDDILSVEN 471
Cdd:TIGR00979 399 LNNSLMLVTALNPHIGYDNAAKIAKKAHKEGITLKEAALELGLLSEEEFDEWVVPEQ 455
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
15-475 |
3.10e-126 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 375.41 E-value: 3.10e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 15 TRIEEDLLGQRHVPADAYYGIHTLRAIENFNISSTTISdvPEFVRGMVMTKKAAALANKELGAIPKDVANYILEACDLIL 94
Cdd:PRK12425 2 SRTETDSLGPIEVPEDAYWGAQTQRSLINFAIGKERMP--LAVLHALALIKKAAARVNDRNGDLPADIARLIEQAADEVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 95 EtGKCMDQFPSDVFQGGAGTSVNMNTNEVIANVALELMGKEKGQYEFINPNDHVNKSQSTNCAYPTGFRIAVYNSVH-QL 173
Cdd:PRK12425 80 D-GQHDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVHeQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 174 MEAIEYLKGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEEIRALDYTSKLLLEINLGATAIGTGLNAPT 253
Cdd:PRK12425 159 LPAIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 254 GYQALAVKHLAEVTGVEVVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRAGLNELNLPEMQAGSSI 333
Cdd:PRK12425 239 GFAEAIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 334 MPAKVNPVIPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSVFESISLLHNACVNLRDKCIDGITVNKEVCEN 413
Cdd:PRK12425 319 MPGKVNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 491571196 414 YVYNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLTAEELDDILSVENFMHP 475
Cdd:PRK12425 399 HLERGLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEA 460
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
23-355 |
1.21e-116 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 345.12 E-value: 1.21e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 23 GQRHVPADAYYGIHTLRAIENFNISSTTIsdvpefvRGMVMTKKAAALANKelgaIPKDVANYILEACDLILETGKCMDQ 102
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDI-------KGLAALKKAAAKANV----ILKEEAAAIIKALDEVAEEGKLDDQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 103 FPSDVFQGGAGTSVNMNTNEVIAnvalELMGkekgqyEFINPNDHVNKSQSTNCAYPTGFRIAVYNSVH-QLMEAIEYLK 181
Cdd:pfam00206 70 FPLKVWQEGSGTAVNMNLNEVIG----ELLG------QLVHPNDHVHTGQSSNDQVPTALRLALKDALSeVLLPALRQLI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 182 GAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEEI-RALDYTSKLLLEINLGATAIGTGLNAPTGYQALAV 260
Cdd:pfam00206 140 DALKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDReRLQQLLPRLLVLPLGGGTAVGTGLNADPEFAELVA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 261 KHLAEVTGVEVVAAeDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPrAGLNELNLPEMQAGSSIMPAKVNP 340
Cdd:pfam00206 220 KELGFFTGLPVKAP-NSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNP 297
|
330
....*....|....*
gi 491571196 341 VIPEVVNQVCFKVLG 355
Cdd:pfam00206 298 DQLELLTGKAGRVMG 312
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
58-407 |
9.15e-115 |
|
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: 341.02 E-value: 9.15e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 58 VRGMVMTKKAAALANKELGAIPKDVANYILEACDLILEtgkcmDQFPSDVFQGGAGTSVNMNTNEVIANVALELmgkekg 137
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILE-----GIAADQVEQEGSGTHDVMAVEEVLAERAGEL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 138 qyefinPNDHVNKSQSTNCAYPTGFRIAVYNSVHQLMEAIEYLKGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHAW 217
Cdd:cd01334 70 ------NGGYVHTGRSSNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 218 AVTLNEEIRALDYTSKLLLEINLGATAIGTGLNAPTGYQALAVKHLAEVTgvevvAAEDLIEATSDCGAYVMTHGALKRL 297
Cdd:cd01334 144 AAELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAELLGFFG-----PAPNSTQAVSDRDFLVELLSALALL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 298 AVKLSKICNDLRLLSSGpraGLNELNLPEM-QAGSSIMPAKVNPVIPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEP 376
Cdd:cd01334 219 AVSLSKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSP 295
|
330 340 350
....*....|....*....|....*....|.
gi 491571196 377 VIAQSVFESISLLHNACVNLRDKCiDGITVN 407
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 ... |
118-397 |
2.82e-55 |
|
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: 184.35 E-value: 2.82e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 118 MNTNEVIANVALELMGKEKGQYefinpndHVNKSQSTNCAYPTGFRIAVYNSVHQLMEAIEYLKGAFELKAQEFKDVLKM 197
Cdd:cd01594 14 ALVEEVLAGRAGELAGGLHGSA-------LVHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 198 GRTQLQDAVPMTVGQEFHAWAVTLNEEIRALDYTskllleinlgataigtglnaptgyqalavkhlaevtgvevvaaedl 277
Cdd:cd01594 87 GRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEA---------------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 278 ieatsdcgAYVMTHGALKRLAVKLSKICNDLRLLSSGPRAGLNELNLPeMQAGSSIMPAKVNPVIPEVVNQVCFKVLGND 357
Cdd:cd01594 121 --------AVAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGNL 191
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 491571196 358 NTVSFAAEGGQLQLNVMEPVIAQSVFESISLLHNACVNLR 397
Cdd:cd01594 192 VAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
421-471 |
4.24e-18 |
|
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: 77.75 E-value: 4.24e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 491571196 421 IVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLTAEELDDILSVEN 471
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPEN 51
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
66-470 |
4.95e-18 |
|
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: 86.25 E-value: 4.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 66 KAAALANKELGAIPKDVANYILEACDLILETGKCMDQFPSDVFQggagtSVNMNT-NEVIANVALELMGKEkgqyefinp 144
Cdd:TIGR00838 36 IAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPFILDPDDE-----DIHMAIeRELIDRVGEDLGGKL--------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 145 ndHVNKSQSTNCAypTGFRIAVYNSVHQLMEAIEYLKGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEE 224
Cdd:TIGR00838 102 --HTGRSRNDQVA--TDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLRD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 225 IRALDYTSKLLLEINLGATAIgtglnAPTGYqALAVKHLAEVTG--------VEVVAAEDLI-EATSDCgAYVMTHgalk 295
Cdd:TIGR00838 178 YERLQDALKRVNVSPLGSGAL-----AGTGF-PIDREYLAELLGfdavtensLDAVSDRDFIlELLFVA-ALIMVH---- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 296 rlavkLSKICNDLRLLSSGpRAGLNELNlPEMQAGSSIMPAKVNPVIPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVME 375
Cdd:TIGR00838 247 -----LSRFAEDLILWSTG-EFGFVELP-DEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 376 PVIAQSVFESISLLHNaCVNLRDKCIDGITVNKEVCENYVYNSIGIVTYLNPYI---------GHHegdIVGKI---CAE 443
Cdd:TIGR00838 320 QEDKEPLFDALKTVEL-SLEMATGMLDTITVNKERMEEAASAGFSNATELADYLvrkgvpfreAHH---IVGELvatAIE 395
|
410 420 430
....*....|....*....|....*....|.
gi 491571196 444 TGKSVRDVVLERG----LLTAEELDDILSVE 470
Cdd:TIGR00838 396 RGKGLEELTLEELqkfsPEFDEDVYEALDPE 426
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
57-472 |
3.56e-16 |
|
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: 80.51 E-value: 3.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 57 FVRGMVMTKKAAALANKELGAIPKDVANYILEACDLILETgkcmdqfPSDVFQGGAGTSvnmntNEVIANV-AL-ELMGK 134
Cdd:COG0015 20 KIRAWLDVEIALAEAQAELGLIPAEAAAAIRAAADDFEID-------AERIKEIEKETR-----HDVKAFVyALkEKVGA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 135 EKGQY-------EFINpnDhvnksqstncaypTGFRIAVYNSVHQLMEAIEYLKGAFELKAQEFKDVLKMGRTQLQDAVP 207
Cdd:COG0015 88 EAGEYihfgatsQDIN--D-------------TALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 208 MTVGQEFHAWAVTLNEEIRALDYTSK--LLLEINlGATaiGTgLNApTGYQALAV-KHLAEVTGVEV------VAAEDLI 278
Cdd:COG0015 153 TTFGKKLAVWAAELLRQLERLEEARErvLVGKIG-GAV--GT-YAA-HGEAWPEVeERVAEKLGLKPnpvttqIEPRDRH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 279 eatsdcgAYVMThgALKRLAVKLSKICNDLRLLSsgpRAGLNELNLP--EMQAGSSIMPAKVNPVIPEVVNQVCFKVLGN 356
Cdd:COG0015 228 -------AELFS--ALALIAGSLEKIARDIRLLQ---RTEVGEVEEPfaKGQVGSSAMPHKRNPIDSENIEGLARLARAL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 357 dntVSFAAEGGQLQL------NVMEPVIAQsvfESISLLHNACVNLRdKCIDGITVNKEVCENYVYNSIG------IVTY 424
Cdd:COG0015 296 ---AAALLEALASWHerdlsdSSVERNILP---DAFLLLDGALERLL-KLLEGLVVNPERMRANLDLTGGlvlseaVLMA 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 491571196 425 L--------NPYighhegDIVGKIC---AETGKSVRDVVLE----RGLLTAEELDDILSVENF 472
Cdd:COG0015 369 LvrrglgreEAY------ELVKELArgaWEEGNDLRELLAAdpeiPAELSKEELEALFDPANY 425
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
145-473 |
1.41e-15 |
|
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: 78.74 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 145 NDHVnksqstncayPTGFRIAVYNSVHQLMEAIEYLKGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEE 224
Cdd:cd01359 88 NDQV----------ATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERD 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 225 IRALDYTSKLLLEINLGATAI-GTGLNaptgyqaLAVKHLAEVTG--------VEVVAAED-LIEATSDCgAYVMTHgal 294
Cdd:cd01359 158 LERLADAYKRVNVSPLGAGALaGTTFP-------IDRERTAELLGfdgptensLDAVSDRDfVLEFLSAA-ALLMVH--- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 295 krlavkLSKICNDLRLLSSGPRAGLNelnLP-EMQAGSSIMPAKVNPVIPEVVNQVCFKVLGNDNTVSFAAEGGQLQLN- 372
Cdd:cd01359 227 ------LSRLAEDLILWSTQEFGFVE---LPdAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNk 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 373 ----VMEPviaqsVFESISLLHnACVNLRDKCIDGITVNKEVCENYVYNSIGIVTYLNPYI----------GHHegdIVG 438
Cdd:cd01359 298 dlqeDKEP-----LFDAVDTLI-ASLRLLTGVISTLTVNPERMREAAEAGFSTATDLADYLvrekgvpfreAHH---IVG 368
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 491571196 439 KI---CAETGKSVRDVVLER----GLLTAEELDDILSVENFM 473
Cdd:cd01359 369 RAvrlAEEKGKDLSDLTLAElqaiSPLFEEDVREALDPENSV 410
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
58-346 |
3.27e-15 |
|
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: 77.16 E-value: 3.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 58 VRGMVMTKKAAALANKELGAIPKDVANYILEACDliletgkcmdQFPSDVFQGGAGTSVNMNtnEVIANV-AL-ELMGKE 135
Cdd:cd01595 11 LRTWLDVEAALAEAQAELGLIPKEAAEEIRAAAD----------VFEIDAERIAEIEKETGH--DVIAFVyALaEKCGED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 136 KGQY-------EFINpnDhvnksqstncaypTGFRIAVYNSVHQLMEAIEYLKGAFELKAQEFKDVLKMGRTQLQDAVPM 208
Cdd:cd01595 79 AGEYvhfgatsQDIN--D-------------TALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 209 TVGQEFHAWAVTLneeIRALDYTSKLLLEINLGAT--AIGTGLNAptGYQALAV-KHLAEVTGVEV------VAAEDLIe 279
Cdd:cd01595 144 TFGKKFAVWAAEL---LRHLERLEEARERVLVGGIsgAVGTHASL--GPKGPEVeERVAEKLGLKVppittqIEPRDRI- 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 491571196 280 atsdcgAYVMThgALKRLAVKLSKICNDLRLLSsgpRAGLNELNLP--EMQAGSSIMPAKVNPVIPEVV 346
Cdd:cd01595 218 ------AELLS--ALALIAGTLEKIATDIRLLQ---RTEIGEVEEPfeKGQVGSSTMPHKRNPIDSENI 275
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
58-471 |
2.03e-13 |
|
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: 71.89 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 58 VRGMVMTKKAAALANKELGAIPKDVANYILEACDLI-LEtgkcMDQFPSDVFQGGagtsvnmntNEVIANVA--LELMGK 134
Cdd:cd01597 21 VQAMLDVEAALARAQAELGVIPKEAAAEIAAAADVErLD----LEALAEATARTG---------HPAIPLVKqlTAACGD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 135 EKGQYefinpndhVNKSQSTNCAYPTGFRIAVYNSVHQLMEAIEYLKGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEF 214
Cdd:cd01597 88 AAGEY--------VHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 215 HAWAVTLNEEIRALDYTSKLLLEINLGAtAIGTGlnAPTGYQALAV-KHLAEVTGVEV------VAAEDLIEATSdcgay 287
Cdd:cd01597 160 AVWLSELLRHRERLDELRPRVLVVQFGG-AAGTL--ASLGDQGLAVqEALAAELGLGVpaipwhTARDRIAELAS----- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 288 vmthgALKRLAVKLSKICNDLRLLSsgpRAGLNELNLPEMQA--GSSIMPAKVNPVIPEVVnQVCFKVLGNDNTVSFAAE 365
Cdd:cd01597 232 -----FLALLTGTLGKIARDVYLLM---QTEIGEVAEPFAKGrgGSSTMPHKRNPVGCELI-VALARRVPGLAALLLDAM 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 366 -------GGQLQLNVMepviaqSVFESISLLHNACVNLRDkCIDGITVNKEV------CENYVYNSIGIVTYLNPYIGHH 432
Cdd:cd01597 303 vqeherdAGAWHAEWI------ALPEIFLLASGALEQAEF-LLSGLEVNEDRmranldLTGGLILSEAVMMALAPKLGRQ 375
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 491571196 433 EG-DIVGKICAET---GKSVRDVVLE----RGLLTAEELDDILSVEN 471
Cdd:cd01597 376 EAhDLVYEACMRAveeGRPLREVLLEdpevAAYLSDEELDALLDPAN 422
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
166-347 |
3.93e-13 |
|
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: 71.22 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 166 VYNSVHQLM--EAIE-YLKGAFEL------KAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEEIRALDYTSKLLL 236
Cdd:TIGR00928 100 IVDTALALLlrDALEiILPKLKQLidrlkeLAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQLERLLQAKERIK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 237 eINLGATAIGTGLNAPTGYQALAvKHLAEVTGVEVVAAEDLIEATSDCGAYVMthgALKRLAVKLSKICNDLRLLSsgpR 316
Cdd:TIGR00928 180 -VGGISGAVGTHAAAYPLVEEVE-ERVTEFLGLKPVPISTQIEPRDRHAELLD---ALALLATTLEKFAVDIRLLQ---R 251
|
170 180 190
....*....|....*....|....*....|...
gi 491571196 317 AGLNELNLP--EMQAGSSIMPAKVNPVIPEVVN 347
Cdd:TIGR00928 252 TEHFEVEEPfgKGQVGSSAMPHKRNPIDFENVC 284
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
145-471 |
2.46e-12 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 68.64 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 145 NDHVnksqstncAypTGFRIAVYNSVHQLMEAIEYLKGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEE 224
Cdd:PRK00855 112 NDQV--------A--TDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARD 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 225 IRALDYTSKLLLEINLGATAI-GTGLNaptgyqaLAVKHLAEVTG--------VEVVAAED-LIEATSDCgAYVMTHgal 294
Cdd:PRK00855 182 LERLRDARKRVNRSPLGSAALaGTTFP-------IDRERTAELLGfdgvtensLDAVSDRDfALEFLSAA-SLLMVH--- 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 295 krlavkLSKICNDLRLLSSgPRAGLneLNLPEMQA-GSSIMPAKVNPVIPEVVNQVCFKVLGNDNTVsfaaeggqlqLNV 373
Cdd:PRK00855 251 ------LSRLAEELILWSS-QEFGF--VELPDAFStGSSIMPQKKNPDVAELIRGKTGRVYGNLTGL----------LTV 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 374 M---------------EPviaqsVFESISLLHnACVNLRDKCIDGITVNKEVCENYVYNSIGIVTYLNPYI---G----- 430
Cdd:PRK00855 312 MkglplaynrdlqedkEP-----LFDAVDTLK-LSLEAMAGMLETLTVNKERMREAAGKGFSTATDLADYLvrkGvpfre 385
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 491571196 431 -HHegdIVGKI---CAETGKSVRDVVLER----GLLTAEELDDILSVEN 471
Cdd:PRK00855 386 aHE---IVGKAvreAEERGVDLADLSLEElqafSPLITEDVYEVLTPEG 431
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
172-344 |
7.80e-11 |
|
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: 63.73 E-value: 7.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 172 QLMEAIEYL-KGAFEL------KAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEEIRALDYTSKlllEINLGAT- 243
Cdd:cd01360 102 QLREALDIIlKDLKELlevlkkKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKEARE---RILVGKIs 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 244 -AIGTGLNAPTGYQALAVKHL---AEVTGVEVVAAEDLIEatsdcgaYVMTHgALkrLAVKLSKICNDLRLLSsgpRAGL 319
Cdd:cd01360 179 gAVGTYANLGPEVEERVAEKLglkPEPISTQVIQRDRHAE-------YLSTL-AL--IASTLEKIATEIRHLQ---RTEV 245
|
170 180
....*....|....*....|....*..
gi 491571196 320 NELNLP--EMQAGSSIMPAKVNPVIPE 344
Cdd:cd01360 246 LEVEEPfsKGQKGSSAMPHKRNPILSE 272
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
160-473 |
1.85e-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: 59.73 E-value: 1.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 160 TGFRIAVYNSVHQLMEAIEYLKGAFELKAQEFKDVLkM-GRTQLQDAVPMTVGQEFHAWAVTLNEEIRALDYTSKlllEI 238
Cdd:COG0165 116 TDFRLYLRDEILELIEALLALQEALLDLAEEHADTI-MpGYTHLQRAQPVTFGHHLLAYAEMLLRDRERLADAYK---RL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 239 N---LGATAI-GTGLnaPTGYQALAvKHL--AEVT--GVEVVAAED-LIEATSDCgAYVMTHgalkrlavkLSKICNDLR 309
Cdd:COG0165 192 NvspLGAAALaGTTF--PIDRERTA-ELLgfDGPTenSLDAVSDRDfALEFLSAA-SLIMVH---------LSRLAEELI 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 310 LLSSgPRAGLneLNLPEMQA-GSSIMPAKVNPVIPEVVNQVCFKVLGNDNTVsfaaeggqlqLNVM-------------- 374
Cdd:COG0165 259 LWSS-SEFGF--VELPDAFStGSSIMPQKKNPDVAELIRGKTGRVIGNLTGL----------LTTMkglplaynkdlqed 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 375 -EPviaqsVFESISLLHnACVNLRDKCIDGITVNKEVCENYVYNSigivtYLN-------------PY-IGHHegdIVGK 439
Cdd:COG0165 326 kEP-----LFDAVDTLK-LCLRLFAGMIATLKVNRERMREAAGAG-----FSTatdladylvrkgvPFrEAHE---IVGR 391
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 491571196 440 I---CAETGKSVRDVVLER----GLLTAEELDDILSVENFM 473
Cdd:COG0165 392 LvryAEEKGKDLEDLTLEElqafSPLIEEDVYEALDPEGSV 432
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
147-411 |
2.33e-09 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 59.80 E-value: 2.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 147 HVNKSQSTNCAypTGFRIAVYNSVHQLMEAIEYLKGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEEIR 226
Cdd:PRK12308 104 HTGRSRNDQVA--TDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYS 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 227 ALDYTSKLLLEINLGATAI-GTGLnaPTGYQALAVK---HLAEVTGVEVVAAEDLIEATSDCGAYVMTHgalkrlavkLS 302
Cdd:PRK12308 182 RLEDALTRLDTCPLGSGALaGTAY--PIDREALAHNlgfRRATRNSLDSVSDRDHVMELMSVASISMLH---------LS 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 303 KICNDLRLLSSGpRAGLNELNlPEMQAGSSIMPAKVNPVIPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSV 382
Cdd:PRK12308 251 RLAEDLIFYNSG-ESGFIELA-DTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKDMQEDKEGL 328
|
250 260
....*....|....*....|....*....
gi 491571196 383 FESISLLhNACVNLRDKCIDGITVNKEVC 411
Cdd:PRK12308 329 FDALDTW-NDCMEMAALCFDGIKVNGERT 356
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
188-340 |
5.35e-07 |
|
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.
Pssm-ID: 176471 [Multi-domain] Cd Length: 436 Bit Score: 51.93 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 188 AQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEEIRALDYtskllLEINLGATaigtGLNAPTGYQAlAVKHLAEVT 267
Cdd:cd03302 130 ALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLER-----LRDDLRFR----GVKGTTGTQA-SFLDLFEGD 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 268 GVEVVAAEDLIeaTSDCG---AYVMTH------------GALKRLAVKLSKICNDLRLLssgprAGLNELNLP--EMQAG 330
Cdd:cd03302 200 HDKVEALDELV--TKKAGfkkVYPVTGqtysrkvdidvlNALSSLGATAHKIATDIRLL-----ANLKEVEEPfeKGQIG 272
|
170
....*....|
gi 491571196 331 SSIMPAKVNP 340
Cdd:cd03302 273 SSAMPYKRNP 282
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
58-345 |
2.56e-06 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 49.28 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 58 VRGMVMTKKAAALANKELGAIPKDVANYILEACDliletgkcmdQFPSDVFQGGAGTSVN-MNTNEVIANVALELmGKEK 136
Cdd:PRK05975 30 IAAMLAFEAALAEAEAEHGIIPAEAAERIAAACE----------TFEPDLAALRHATARDgVVVPALVRQLRAAV-GEEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 137 GQyefinpndHVNKSQSTNCAYPTGFRIAVYNSVHQLMEAIEYLKGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHA 216
Cdd:PRK05975 99 AA--------HVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLAS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 217 WAVTLNEEIRALDYTSKLLLEINLGAtAIGTGlnAPTGYQALAVK-HLAEVTGVevvaaEDLIEATSDCGAYVMTHGALK 295
Cdd:PRK05975 171 WRAPLLRHRDRLEALRADVFPLQFGG-AAGTL--EKLGGKAAAVRaRLAKRLGL-----EDAPQWHSQRDFIADFAHLLS 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 491571196 296 RLAVKLSKICNDLRLLSsgpRAGlNELNLPEmQAGSSIMPAKVNPVIPEV 345
Cdd:PRK05975 243 LVTGSLGKFGQDIALMA---QAG-DEISLSG-GGGSSAMPHKQNPVAAET 287
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
40-471 |
7.49e-06 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 48.18 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 40 AIENFNISsttISdvpeFVRGM----VMTKKAAALANKELGAIPKDVANYILEACDLILEtgkcmdQFPSDVFQGGAG-T 114
Cdd:PLN02646 30 AVEKFNES---IS----FDKRLykedIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEK------EIEAGKFEWRPDrE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 115 SVNMNtNEVianvAL-ELMGKEKGQYefinpndHVNKSQSTNCAypTGFRIAVYNSVHQLMEAIEYLKGAFELKAQEFKD 193
Cdd:PLN02646 97 DVHMN-NEA----RLtELIGEPAKKL-------HTARSRNDQVA--TDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 194 VLKMGRTQLQDAVPMTVGQEFHAWAVTLN-EEIRALDytskLLLEIN---LGATAI-GTGLnaPTGYQALAvkhlaEVTG 268
Cdd:PLN02646 163 LVVPGYTHLQRAQPVLLSHWLLSHVEQLErDAGRLVD----CRPRVNfcpLGSCALaGTGL--PIDRFMTA-----KDLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 269 VEVVAAEDlIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRAGLNELNlpEMQAGSSIMPAKVNPVIPEVVNQ 348
Cdd:PLN02646 232 FTAPMRNS-IDAVSDRDFVLEFLFANSITAIHLSRLGEEWVLWASEEFGFVTPSD--AVSTGSSIMPQKKNPDPMELVRG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 349 VCFKVLGNDNTVSFAAEGGQLQLN-----VMEPviaqsVFESISLLHNaCVNLRDKCIDGITVNKEVCENYVYNSIGIVT 423
Cdd:PLN02646 309 KSARVIGDLVTVLALCKGLPTAYNrdlqeDKEP-----LFDSVDTVSD-MLEVATEFAQNITFNPERIKKSLPAGMLDAT 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 491571196 424 YLNPYI---------GHHegdIVG---KICAETGKSVRDVVLE--RGLLTAEELD--DILSVEN 471
Cdd:PLN02646 383 TLADYLvrkgvpfreTHH---IVGaavALAESKGCELSDLTLEdlKSINPVFEEDvyEVLGVEN 443
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
188-341 |
1.08e-05 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 47.70 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 188 AQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEEIRALDYTSKLLLEINLGATAigtGLNAPTGYQALAV-KHLAEV 266
Cdd:PRK09053 142 AARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGGAA---GTLASLGEQALPVaQALAAE 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 267 TGVEVVAA------EDLIEATSdcgayvmthgALKRLAVKLSKICNDLRLLSSGPRAGLNELNLPEmQAGSSIMPAKVNP 340
Cdd:PRK09053 219 LQLALPALpwhtqrDRIAEFAS----------ALGLLAGTLGKIARDVSLLMQTEVGEVFEPAAAG-KGGSSTMPHKRNP 287
|
.
gi 491571196 341 V 341
Cdd:PRK09053 288 V 288
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
140-360 |
1.32e-05 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 47.67 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 140 EFINpNDHVNKSQstNCAYPTGFRIAVYNSVHQLMEAIEYLKGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAV 219
Cdd:PRK06705 105 DFVS-NMHIGRSR--NDMGVTMYRMSLRRYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYD 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 220 TLNEEIRALDYTSKLLLEINLGATAIGTgLNAPTGYQALAvkHLAEVTGV-----EVVAAEDLIEATSDCGAYVMTHgal 294
Cdd:PRK06705 182 TMQRDLERMKKTYKLLNQSPMGAAALST-TSFPIKRERVA--DLLGFTNViensyDAVAGADYLLEVSSLLMVMMTN--- 255
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 491571196 295 krlavkLSKICNDLRLLSSGPRAGLNELNlPEMQAgSSIMPAKVNPVIPEVVNQVCFKVLGNDNTV 360
Cdd:PRK06705 256 ------TSRWIHDFLLLATKEYDGITVAR-PYVQI-SSIMPQKRNPVSIEHARAITSSALGEAFTV 313
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
293-472 |
1.84e-05 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 45.79 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 293 ALKRLAVKLSKICNDLRLLSsGPRAGLNELNLPEMQAGSSIMPAKVNPVIpevvnqvCFKVLGNDNTV-SFAAEGGQLQL 371
Cdd:PRK08937 22 VLALIATSLEKFANEIRLLQ-RSEIREVEEPFAKGQKGSSAMPHKRNPIG-------SERITGLARVLrSYLVTALENVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 372 NVMEPVIAQSVFESISLLH-----NACVNLRDKCIDGITVNKEVCEN-------YVYNSIGIVTYLNPYIGHHEG-DIVG 438
Cdd:PRK08937 94 LWHERDLSHSSAERIALPDaflalDYILNRFVNILENLVVFPENIERnldktlgFIATERVLLELVEKGMGREEAhELIR 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 491571196 439 K---ICAETGKSVRDVVLE----RGLLTAEELDDILSVENF 472
Cdd:PRK08937 174 EkamEAWKNQKDLRELLEAderfTKQLTKEELDELFDPEAF 214
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
180-363 |
1.01e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 44.84 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 180 LKGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEEIRALdytSKLLLEIN---LGATAiGTGLNAPTGYQ 256
Cdd:PRK02186 542 LRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHAL---FALFEHIDvcpLGAGA-GGGTTFPIDPE 617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 257 ALAVkhlaeVTGVEVVAAEDLIEATSDCGAyvmTHG--ALKRLAVKLSKICNDLRLLSSgprAGLNELNLP-EMQAGSSI 333
Cdd:PRK02186 618 FVAR-----LLGFEQPAPNSLDAVASRDGV---LHFlsAMAAISTVLSRLAQDLQLWTT---REFALVSLPdALTGGSSM 686
|
170 180 190
....*....|....*....|....*....|
gi 491571196 334 MPAKVNPVIPEVVNQVCFKVLGNDNTVSFA 363
Cdd:PRK02186 687 LPQKKNPFLLEFVKGRAGVVAGALASASAA 716
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
155-341 |
5.20e-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: 42.22 E-value: 5.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 155 NCAYPTGFRIAVyNSVhqLMEAIEYLKGAFELKAQEFKDVLKMGRTQLQDAVPMTVGQEFHAWAVTLNEEIRALDYTsKL 234
Cdd:cd01598 106 NLAYALMIKEAR-NEV--ILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLKQI-EI 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 235 LLEINlGATaiGTgLNA-----P----TGYQALAVKHL-----AEVTGVEvvaAEDLIEATSDCgayvmthgaLKRLAVK 300
Cdd:cd01598 182 LGKFN-GAV--GN-FNAhlvayPdvdwRKFSEFFVTSLgltwnPYTTQIE---PHDYIAELFDA---------LARINTI 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 491571196 301 LSKICND------LRLLSSGPRAGlnelnlpemQAGSSIMPAKVNPV 341
Cdd:cd01598 246 LIDLCRDiwgyisLGYFKQKVKKG---------EVGSSTMPHKVNPI 283
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
173-340 |
4.22e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 39.49 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 173 LMEAIEYLKGaFELKAqefkdvLKMGRTQLQDAVPMTVGQEFHAWAVTLNEEIRALDytsKLLLEINLGATAIGTGLNAP 252
Cdd:PRK06389 129 LYEIIKVIPG-FNLKG------RLPGYTHFRQAMPMTVNTYINYIKSILYHHINNLD---SFLMDLREMPYGYGSGYGSP 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 491571196 253 TgyqALAVKHLAEVTGVEVVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSsgpRAGLNELNlPEMQAGSS 332
Cdd:PRK06389 199 S---SVKFNQMSELLGMEKNIKNPVYSSSLYIKTIENISYLISSLAVDLSRICQDIIIYY---ENGIITIP-DEFTTGSS 271
|
....*...
gi 491571196 333 IMPAKVNP 340
Cdd:PRK06389 272 LMPNKRNP 279
|
|
| |
