|
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: 911.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 11 APQATRLEEDLLGQRHVPADAYYGIHTLRAVENFNISNVTISDVPEFVRGMVMTKKAAALANKELGVIPSEVAKYIIQAC 90
Cdd:PRK12273 1 MMMNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKISDYPELIRALAMVKKAAALANKELGLLDEEKADAIVAAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 91 DLILDtGKCMDQFPSDVFQGGAGTSVNMNANEVVANVALELMGKEKGQYEFINPNDHVNRSQSTNCAYPTGFRISVYNSV 170
Cdd:PRK12273 81 DEILA-GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIALLLSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 171 LKLIDAIEYLKGAFELKSQEFNTILKMGRTQLQDAVPMTVGQEFHAWAVTINEEIKNLEYTSKLLLEVNLGATAIGTGLN 250
Cdd:PRK12273 160 RKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 251 AAPGYQGLAVKHLAEVTGLECVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRTGFNELNLPELQAG 330
Cdd:PRK12273 240 APPGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 331 SSIMPAKVNPVVPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSMFESLDILTNACVNLRDKCVDGITVNKEV 410
Cdd:PRK12273 320 SSIMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEER 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1589117612 411 CESHVFNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLSEEELDDIFSVENLMHPQYKAKRYE 483
Cdd:PRK12273 400 CREYVENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTHPGYKGKRYT 472
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
16-476 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 845.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 16 RLEEDLLGQRHVPADAYYGIHTLRAVENFNISNVTISDVPEFVRGMVMTKKAAALANKELGVIPSEVAKYIIQACDLILD 95
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPISDHPELIRALAMVKKAAALANRELGLLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 96 tGKCMDQFPSDVFQGGAGTSVNMNANEVVANVALELMGKEKGQYEFINPNDHVNRSQSTNCAYPTGFRISVYNSVLKLID 175
Cdd:COG1027 81 -GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLALLLLLRELLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 176 AIEYLKGAFELKSQEFNTILKMGRTQLQDAVPMTVGQEFHAWAVTINEEIKNLEYTSKLLLEVNLGATAIGTGLNAAPGY 255
Cdd:COG1027 160 ALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 256 QGLAVKHLAEVTGLECVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRTGFNELNLPELQAGSSIMP 335
Cdd:COG1027 240 IELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 336 AKVNPVVPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSMFESLDILTNACVNLRDKCVDGITVNKEVCESHV 415
Cdd:COG1027 320 GKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYV 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1589117612 416 FNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLSEEELDDIFSVENLMHPQ 476
Cdd:COG1027 400 ENSIGLVTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGLLTEEELDEILDPENMTGPG 460
|
|
| 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: 785.56 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 16 RLEEDLLGQRHVPADAYYGIHTLRAVENFNISNVTISDVPEFVRGMVMTKKAAALANKELGVIPSEVAKYIIQACDLILD 95
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKISDIPEFVRGMVMVKKAAALANKELGTIPESIANAIVAACDEILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 96 TGKCMDQFPSDVFQGGAGTSVNMNANEVVANVALELMGKEKGQYEFINPNDHVNRSQSTNCAYPTGFRISVYNSVLKLID 175
Cdd:TIGR00839 81 NGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIAVYSSLIKLVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 176 AIEYLKGAFELKSQEFNTILKMGRTQLQDAVPMTVGQEFHAWAVTINEEIKNLEYTSKLLLEVNLGATAIGTGLNAAPGY 255
Cdd:TIGR00839 161 AINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 256 QGLAVKHLAEVTGLECVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRTGFNELNLPELQAGSSIMP 335
Cdd:TIGR00839 241 SPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 336 AKVNPVVPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSMFESLDILTNACVNLRDKCVDGITVNKEVCESHV 415
Cdd:TIGR00839 321 AKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGYV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1589117612 416 FNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLSEEELDDIFSVENLMHPQYKAKRY 482
Cdd:TIGR00839 401 FNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLMHPAYKAKRY 467
|
|
| 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: 776.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 16 RLEEDLLGQRHVPADAYYGIHTLRAVENFNISNVTISdvPEFVRGMVMTKKAAALANKELGVIPSEVAKYIIQACDLILD 95
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISGLKIH--PELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 96 tGKCMDQFPSDVFQGGAGTSVNMNANEVVANVALELMGKEKGQYEFINPNDHVNRSQSTNCAYPTGFRISVYNSVLKLID 175
Cdd:cd01357 79 -GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLALILLLRKLLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 176 AIEYLKGAFELKSQEFNTILKMGRTQLQDAVPMTVGQEFHAWAVTINEEIKNLEYTSKLLLEVNLGATAIGTGLNAAPGY 255
Cdd:cd01357 158 ALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 256 QGLAVKHLAEVTGLECVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRTGFNELNLPELQAGSSIMP 335
Cdd:cd01357 238 IELVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 336 AKVNPVVPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSMFESLDILTNACVNLRDKCVDGITVNKEVCESHV 415
Cdd:cd01357 318 GKVNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1589117612 416 FNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLSEEELDDIFS 468
Cdd:cd01357 398 ENSIGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELDEILS 450
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
14-482 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 724.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 14 ATRLEEDLLGQRHVPADAYYGIHTLRAVENFNISNVTIsdVPEFVRGMVMTKKAAALANKELGVIPSEVAKYIIQACDLI 93
Cdd:PRK13353 4 NMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYKI--HPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQACDEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 94 LDtGKCMDQFPSDVFQGGAGTSVNMNANEVVANVALELMGKEKGQYEFINPNDHVNRSQSTNCAYPTGFRISVYNSVLKL 173
Cdd:PRK13353 82 LA-GKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLLEGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 174 IDAIEYLKGAFELKSQEFNTILKMGRTQLQDAVPMTVGQEFHAWAVTINEEIKNLEYTSKLLLEVNLGATAIGTGLNAAP 253
Cdd:PRK13353 161 LAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 254 GYQGLAVKHLAEVTGLECVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRTGFNELNLPELQAGSSI 333
Cdd:PRK13353 241 EYIERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 334 MPAKVNPVVPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSMFESLDILTNACVNLRDKCVDGITVNKEVCES 413
Cdd:PRK13353 321 MPGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1589117612 414 HVFNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLSEEELDDIFSVENLMHPQYKAKRY 482
Cdd:PRK13353 401 YVEKSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMTHPGIAGATL 469
|
|
| 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: 716.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 16 RLEEDLLGQRHVPADAYYGIHTLRAVENFNISNVTISdvPEFVRGMVMTKKAAALANKELGVIPSEVAKYIIQACDLILD 95
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISGERMP--PELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 96 tGKCMDQFPSDVFQGGAGTSVNMNANEVVANVALELMGKEKGQYEFINPNDHVNRSQSTNCAYPTGFRISVYNSVLKLID 175
Cdd:cd01596 79 -GKLDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKGKYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 176 AIEYLKGAFELKSQEFNTILKMGRTQLQDAVPMTVGQEFHAWAVTINEEIKNLEYTSKLLLEVNLGATAIGTGLNAAPGY 255
Cdd:cd01596 158 ALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 256 QGLAVKHLAEVTGLECVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRTGFNELNLPELQAGSSIMP 335
Cdd:cd01596 238 AEKVAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 336 AKVNPVVPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSMFESLDILTNACVNLRDKCVDGITVNKEVCESHV 415
Cdd:cd01596 318 GKVNPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1589117612 416 FNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLSEEELDDIFS 468
Cdd:cd01596 398 ENSLMLVTALNPHIGYEKAAEIAKEALKEGRTLREAALELGLLTEEELDEILD 450
|
|
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
13-474 |
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: 558.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 13 QATRLEEDLLGQRHVPADAYYGIHTLRAVENFNISNVTISdvPEFVRGMVMTKKAAALANKELGVIPSEVAKYIIQACDL 92
Cdd:COG0114 2 METRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGERMP--REFIRALALIKKAAARANAELGLLDAEKADAIVAAADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 93 ILDtGKCMDQFPSDVFQGGAGTSVNMNANEVVANVALELMGKEKGQYEFINPNDHVNRSQSTNCAYPTGFRISVYNSVLK 172
Cdd:COG0114 80 VIA-GKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 173 -LIDAIEYLKGAFELKSQEFNTILKMGRTQLQDAVPMTVGQEFHAWAVTINEEIKNLEYTSKLLLEVNLGATAIGTGLNA 251
Cdd:COG0114 159 rLLPALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 252 APGYQGLAVKHLAEVTGLECVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRTGFNELNLPELQAGS 331
Cdd:COG0114 239 HPGFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 332 SIMPAKVNPVVPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSMFESLDILTNACVNLRDKCVDGITVNKEVC 411
Cdd:COG0114 319 SIMPGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERI 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1589117612 412 ESHVFNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLSEEELDDIFSVENLMH 474
Cdd:COG0114 399 EELLERSLMLVTALNPHIGYDKAAKIAKKAHKEGRTLREAALELGLLSEEEFDRLVDPEKMTG 461
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
13-476 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 552.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 13 QATRLEEDLLGQRHVPADAYYGIHTLRAVENFNISNVTISdvPEFVRGMVMTKKAAALANKELGVIPSEVAKYIIQACDL 92
Cdd:PRK00485 2 METRIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMP--RELIRALALLKKAAARVNAELGLLDAEKADAIVAAADE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 93 ILDtGKCMDQFPSDVFQGGAGTSVNMNANEVVANVALELMGKEKGQYEFINPNDHVNRSQSTNCAYPTGFRISVYNSVL- 171
Cdd:PRK00485 80 VIA-GKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVe 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 172 KLIDAIEYLKGAFELKSQEFNTILKMGRTQLQDAVPMTVGQEFHAWAVTINEEIKNLEYTSKLLLEVNLGATAIGTGLNA 251
Cdd:PRK00485 159 RLLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 252 APGYQGLAVKHLAEVTGLECVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRTGFNELNLPELQAGS 331
Cdd:PRK00485 239 HPGFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGS 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 332 SIMPAKVNPVVPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSMFESLDILTNACVNLRDKCVDGITVNKEVC 411
Cdd:PRK00485 319 SIMPGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERI 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1589117612 412 ESHVFNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLSEEELDDIFSVENLMHPQ 476
Cdd:PRK00485 399 KELLERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPG 463
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
16-466 |
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: 524.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 16 RLEEDLLGQRHVPADAYYGIHTLRAVENFNISNVTISdvPEFVRGMVMTKKAAALANKELGVIPSEVAKYIIQACDLILD 95
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMP--RELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 96 tGKCMDQFPSDVFQGGAGTSVNMNANEVVANVALELMGKEKGQYEFINPNDHVNRSQSTNCAYPTGFRISVYNSVLK-LI 174
Cdd:cd01362 79 -GKLDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQErLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 175 DAIEYLKGAFELKSQEFNTILKMGRTQLQDAVPMTVGQEFHAWAVTINEEIKNLEYTSKLLLEVNLGATAIGTGLNAAPG 254
Cdd:cd01362 158 PALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 255 YQGLAVKHLAEVTGLECVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRTGFNELNLPELQAGSSIM 334
Cdd:cd01362 238 FAEKVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 335 PAKVNPVVPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSMFESLDILTNACVNLRDKCVDGITVNKEVCESH 414
Cdd:cd01362 318 PGKVNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAEL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1589117612 415 VFNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLSEEELDDI 466
Cdd:cd01362 398 LERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRL 449
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
22-478 |
5.90e-173 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 494.21 E-value: 5.90e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 22 LGQRHVPADAYYGIHTLRAVENFNISNVTISDVPEFVRGMVMTKKAAALANKELGVIPSEVAKYIIQACDLILDtGKCMD 101
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGGERERMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAE-GKLDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 102 QFPSDVFQGGAGTSVNMNANEVVANVALELMGKEKGQYEFINPNDHVNRSQSTNCAYPTGFRISVYNSVL-KLIDAIEYL 180
Cdd:PLN00134 80 HFPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATEIHsRLIPALKEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 181 KGAFELKSQEFNTILKMGRTQLQDAVPMTVGQEFHAWAVTINEEIKNLEYTSKLLLEVNLGATAIGTGLNAAPGYQGLAV 260
Cdd:PLN00134 160 HESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 261 KHLAEVTGLECVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRTGFNELNLPELQAGSSIMPAKVNP 340
Cdd:PLN00134 240 AAVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 341 VVPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSMFESLDILTNACVNLRDKCVDGITVNKEVCESHVFNSIG 420
Cdd:PLN00134 320 TQCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLM 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1589117612 421 IVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLSEEELDDIFSVENLMHPQYK 478
Cdd:PLN00134 400 LVTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTGPSDL 457
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
13-475 |
6.69e-163 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 469.48 E-value: 6.69e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 13 QATRLEEDLLGQRHVPADAYYGIHTLRAVENFNISNVTISdvPEFVRGMVMTKKAAALANKELGVIPSEVAKYIIQACDL 92
Cdd:PRK14515 9 NGVRIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGYKIH--EGLIKAFAIVKKAAALANTDVGRLELNKGGAIAEAAQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 93 ILDtGKCMDQFPSDVFQGGAGTSVNMNANEVVANVALELMGKEKGQYEFINPNDHVNRSQSTNCAYPTGFRISVYNSVLK 172
Cdd:PRK14515 87 ILD-GKWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIATLNALEG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 173 LIDAIEYLKGAFELKSQEFNTILKMGRTQLQDAVPMTVGQEFHAWAVTINEEIKNLEYTSKLLLEVNLGATAIGTGLNAA 252
Cdd:PRK14515 166 LLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNAD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 253 PGYQGLAVKHLAEVTGLECVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRTGFNELNLPELQAGSS 332
Cdd:PRK14515 246 PEYIEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSS 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 333 IMPAKVNPVVPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSMFESLDILTNACVNLRDKCVDGITVNKEVCE 412
Cdd:PRK14515 326 IMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLK 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1589117612 413 SHVFNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLSEEELDDIFSVENLMHP 475
Cdd:PRK14515 406 EYVEKSVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEMTHP 468
|
|
| fumC_II |
TIGR00979 |
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ... |
16-473 |
2.86e-153 |
|
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: 444.17 E-value: 2.86e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 16 RLEEDLLGQRHVPADAYYGIHTLRAVENFNISNVTISdvPEFVRGMVMTKKAAALANKELGVIPSEVAKYIIQACDLILd 95
Cdd:TIGR00979 2 RIEKDSMGEIQVPADKYWGAQTQRSLENFKIGTEKMP--LELIHAFAILKKAAAIVNEDLGKLDAKKADAIVQAADEIL- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 96 TGKCMDQFPSDVFQGGAGTSVNMNANEVVANVALELMGKEKGQYEFINPNDHVNRSQSTNCAYPTGFRISVYNSVL-KLI 174
Cdd:TIGR00979 79 AGKLDDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKnQLI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 175 DAIEYLKGAFELKSQEFNTILKMGRTQLQDAVPMTVGQEFHAWAVTINEEIKNLEYTSKLLLEVNLGATAIGTGLNAAPG 254
Cdd:TIGR00979 159 PALENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 255 YQGLAVKHLAEVTGLECVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRTGFNELNLPELQAGSSIM 334
Cdd:TIGR00979 239 FDEKVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 335 PAKVNPVVPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSMFESLDILTNACVNLRDKCVDGITVNKEVCESH 414
Cdd:TIGR00979 319 PGKVNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1589117612 415 VFNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLSEEELDDIFSVENLM 473
Cdd:TIGR00979 399 LNNSLMLVTALNPHIGYDNAAKIAKKAHKEGITLKEAALELGLLSEEEFDEWVVPEQMV 457
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
15-475 |
9.98e-118 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 353.46 E-value: 9.98e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 15 TRLEEDLLGQRHVPADAYYGIHTLRAVENFNISNvtiSDVP-EFVRGMVMTKKAAALANKELGVIPSEVAKYIIQACDLI 93
Cdd:PRK12425 2 SRTETDSLGPIEVPEDAYWGAQTQRSLINFAIGK---ERMPlAVLHALALIKKAAARVNDRNGDLPADIARLIEQAADEV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 94 LDtGKCMDQFPSDVFQGGAGTSVNMNANEVVANVALELMGKEKGQYEFINPNDHVNRSQSTNCAYPTGFRISVYNSV-LK 172
Cdd:PRK12425 79 LD-GQHDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVhEQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 173 LIDAIEYLKGAFELKSQEFNTILKMGRTQLQDAVPMTVGQEFHAWAVTINEEIKNLEYTSKLLLEVNLGATAIGTGLNAA 252
Cdd:PRK12425 158 LLPAIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 253 PGYQGLAVKHLAEVTGLECVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPRTGFNELNLPELQAGSS 332
Cdd:PRK12425 238 HGFAEAIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 333 IMPAKVNPVVPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVIAQSMFESLDILTNACVNLRDKCVDGITVNKEVCE 412
Cdd:PRK12425 318 IMPGKVNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMA 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1589117612 413 SHVFNSIGIVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLSEEELDDIFSVENLMHP 475
Cdd:PRK12425 398 AHLERGLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEA 460
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
23-355 |
4.26e-110 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 328.56 E-value: 4.26e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 23 GQRHVPADAYYGIHTLRAVENFNISNVTIsdvpefvRGMVMTKKAAALANkelgVIPSEVAKYIIQACDLILDTGKCMDQ 102
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDI-------KGLAALKKAAAKAN----VILKEEAAAIIKALDEVAEEGKLDDQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 103 FPSDVFQGGAGTSVNMNANEVVAnvalELMGkekgqyEFINPNDHVNRSQSTNCAYPTGFRISVYNSVL-KLIDAIEYLK 181
Cdd:pfam00206 70 FPLKVWQEGSGTAVNMNLNEVIG----ELLG------QLVHPNDHVHTGQSSNDQVPTALRLALKDALSeVLLPALRQLI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 182 GAFELKSQEFNTILKMGRTQLQDAVPMTVGQEFHAWAVTINEEIKNLEY-TSKLLLEVNLGATAIGTGLNAAPGYQGLAV 260
Cdd:pfam00206 140 DALKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQlLPRLLVLPLGGGTAVGTGLNADPEFAELVA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 261 KHLAEVTGLEcVAAEDLIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPrTGFNELNLPELQAGSSIMPAKVNP 340
Cdd:pfam00206 220 KELGFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNP 297
|
330
....*....|....*
gi 1589117612 341 VVPEVVNQVCFKVLG 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 |
1.07e-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: 307.51 E-value: 1.07e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 58 VRGMVMTKKAAALANKELGVIPSEVAKYIIQACDLILDtgkcmDQFPSDVFQGGAGTSVNMNANEVVANVALELmgkekg 137
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILE-----GIAADQVEQEGSGTHDVMAVEEVLAERAGEL------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 138 qyefinPNDHVNRSQSTNCAYPTGFRISVYNSVLKLIDAIEYLKGAFELKSQEFNTILKMGRTQLQDAVPMTVGQEFHAW 217
Cdd:cd01334 70 ------NGGYVHTGRSSNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 218 AVTINEEIKNLEYTSKLLLEVNLGATAIGTGLNAAPGYQGLAVKHLAEVTglecvAAEDLIEATSDCGAYVMTHGALKRL 297
Cdd:cd01334 144 AAELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAELLGFFG-----PAPNSTQAVSDRDFLVELLSALALL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 298 AVKLSKICNDLRLLSSGprtGFNELNLPE-LQAGSSIMPAKVNPVVPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEP 376
Cdd:cd01334 219 AVSLSKIANDLRLLSSG---EFGEVELPDaKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSP 295
|
330 340 350
....*....|....*....|....*....|.
gi 1589117612 377 VIAQSMFESLDILTNACVNLRDKCvDGITVN 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 |
5.55e-41 |
|
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: 146.60 E-value: 5.55e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 118 MNANEVVANVALELMGKEKGQYefinpndHVNRSQSTNCAYPTGFRISVYNSVLKLIDAIEYLKGAFELKSQEFNTILKM 197
Cdd:cd01594 14 ALVEEVLAGRAGELAGGLHGSA-------LVHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 198 GRTQLQDAVPMTVGQEFHAWAVTINEEIKNLEYTsklllevnlgataigtglnaapgyqglavkhlaevtglecvaaedl 277
Cdd:cd01594 87 GRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEA---------------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 278 ieatsdcgAYVMTHGALKRLAVKLSKICNDLRLLSSGPRTGFNELNLPeLQAGSSIMPAKVNPVVPEVVNQVCFKVLGND 357
Cdd:cd01594 121 --------AVAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGNL 191
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1589117612 358 NTVSFAAEGGQLQLNVMEPVIAQSMFESLDILTNACVNLR 397
Cdd:cd01594 192 VAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
421-472 |
1.95e-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: 78.52 E-value: 1.95e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1589117612 421 IVTYLNPYIGHHEGDIVGKICAETGKSVRDVVLERGLLSEEELDDIFSVENL 472
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
66-470 |
1.90e-14 |
|
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include examples of avian delta crystallins, in which argininosuccinate lyase activity may or may not be present and the biological role is to provide the optically clear cellular protein of the eye lens. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 129918 [Multi-domain] Cd Length: 455 Bit Score: 75.08 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 66 KAAALANKELGVIPSEVAKYIIQACDLILDTGKCMDQFPSDVFQggagtSVNMNA-NEVVANVALELMGKEkgqyefinp 144
Cdd:TIGR00838 36 IAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPFILDPDDE-----DIHMAIeRELIDRVGEDLGGKL--------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 145 ndHVNRSQSTNCAypTGFRISVYNSVLKLIDAIEYLKGAF-ELKSQEFNTILKmGRTQLQDAVPMTVGQEFHAWAVTINE 223
Cdd:TIGR00838 102 --HTGRSRNDQVA--TDLRLYLRDHVLELAEALLDLQDALiELAEKHVETLMP-GYTHLQRAQPITLAHHLLAYAEMLLR 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 224 EIKNLEYTSKLLLEVNLGATAI-GTGLNAAPGYqglavkhLAEVTG--------LECVAAEDLI-EATSDCgAYVMTHga 293
Cdd:TIGR00838 177 DYERLQDALKRVNVSPLGSGALaGTGFPIDREY-------LAELLGfdavtensLDAVSDRDFIlELLFVA-ALIMVH-- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 294 lkrlavkLSKICNDLRLLSSGPrtgFNELNLP-ELQAGSSIMPAKVNPVVPEVVNQVCFKVLGNDNTVSFAAEGGQLQLN 372
Cdd:TIGR00838 247 -------LSRFAEDLILWSTGE---FGFVELPdEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 373 VMEPVIAQSMFESLDILTNaCVNLRDKCVDGITVNKEVCESHVFNSIGIVTYLNPYI---------GHHegdIVGKI--- 440
Cdd:TIGR00838 317 RDLQEDKEPLFDALKTVEL-SLEMATGMLDTITVNKERMEEAASAGFSNATELADYLvrkgvpfreAHH---IVGELvat 392
|
410 420 430
....*....|....*....|....*....|....
gi 1589117612 441 CAETGKSVRDVVLERG----LLSEEELDDIFSVE 470
Cdd:TIGR00838 393 AIERGKGLEELTLEELqkfsPEFDEDVYEALDPE 426
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
57-471 |
2.64e-11 |
|
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: 65.49 E-value: 2.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 57 FVRGMVMTKKAAALANKELGVIPSEVAKYIIQACDLILDTgkcmdqfPSDVFQGGAGTsvnmnANEVVANV-AL-ELMGK 134
Cdd:COG0015 20 KIRAWLDVEIALAEAQAELGLIPAEAAAAIRAAADDFEID-------AERIKEIEKET-----RHDVKAFVyALkEKVGA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 135 EKGQY-------EFINpnDhvnrsqstncaypTGFRISVYNSVLKLIDAIEYLKGAFELKSQEFNTILKMGRTQLQDAVP 207
Cdd:COG0015 88 EAGEYihfgatsQDIN--D-------------TALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 208 MTVGQEFHAWAVTINEEIKNLEYTSKLLLEVNL-GATaiGTGlnAAPGYQGLAV-KHLAEVTGLEC------VAAEDLIe 279
Cdd:COG0015 153 TTFGKKLAVWAAELLRQLERLEEARERVLVGKIgGAV--GTY--AAHGEAWPEVeERVAEKLGLKPnpvttqIEPRDRH- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 280 atsdcgAYVMThgALKRLAVKLSKICNDLRLLSsgpRTGFNELNLP--ELQAGSSIMPakvnpvvpevvnqvcFKVlgnd 357
Cdd:COG0015 228 ------AELFS--ALALIAGSLEKIARDIRLLQ---RTEVGEVEEPfaKGQVGSSAMP---------------HKR---- 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 358 NTVSF----------------AAEGGQLQL------NVMEPVIAQSMFESLDILTNACVNLrdkcVDGITVNKEVCESHV 415
Cdd:COG0015 278 NPIDSenieglarlaralaaaLLEALASWHerdlsdSSVERNILPDAFLLLDGALERLLKL----LEGLVVNPERMRANL 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1589117612 416 FNSIG------IVTYL--------NPYighhegDIVGKIC---AETGKSVRDVVLE----RGLLSEEELDDIFSVEN 471
Cdd:COG0015 354 DLTGGlvlseaVLMALvrrglgreEAY------ELVKELArgaWEEGNDLRELLAAdpeiPAELSKEELEALFDPAN 424
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
58-337 |
5.54e-11 |
|
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: 64.06 E-value: 5.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 58 VRGMVMTKKAAALANKELGVIPSEVAKYIIQACDLI-LDTGKcmdqfpsdVFQGGAGTsvnmnANEVVANV-AL-ELMGK 134
Cdd:cd01595 11 LRTWLDVEAALAEAQAELGLIPKEAAEEIRAAADVFeIDAER--------IAEIEKET-----GHDVIAFVyALaEKCGE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 135 EKGQY-------EFINpndhvnrsqstNCAYptgfrisvynsVLKLIDAIEYLKGAFE-----LKSQ--EFNTILKMGRT 200
Cdd:cd01595 78 DAGEYvhfgatsQDIN-----------DTAL-----------ALQLRDALDIILPDLDalidaLAKLalEHKDTPMLGRT 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 201 QLQDAVPMTVGQEFHAWAVTINEEIKNLEYTSKLLLEVNLGAtAIGTGLNAAPgyQGLAV-KHLAEVTGLEC------VA 273
Cdd:cd01595 136 HGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGGISG-AVGTHASLGP--KGPEVeERVAEKLGLKVppittqIE 212
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1589117612 274 AEDLIeatsdcgAYVMThgALKRLAVKLSKICNDLRLLSsgpRTGFNELNLP--ELQAGSSIMPAK 337
Cdd:cd01595 213 PRDRI-------AELLS--ALALIAGTLEKIATDIRLLQ---RTEIGEVEEPfeKGQVGSSTMPHK 266
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
58-471 |
8.11e-11 |
|
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: 63.80 E-value: 8.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 58 VRGMVMTKKAAALANKELGVIPSEVAKYIIQACDLI-LDtgkcMDQFPSDVFQGGagtsvnmnaNEVVANV-AL-ELMGK 134
Cdd:cd01597 21 VQAMLDVEAALARAQAELGVIPKEAAAEIAAAADVErLD----LEALAEATARTG---------HPAIPLVkQLtAACGD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 135 EKGQYefinpndhVNRSQSTNCAYPTGFrisvynsVLKLIDAIEYLKGAFE--------LKSQEFNTILkMGRTQLQDAV 206
Cdd:cd01597 88 AAGEY--------VHWGATTQDIIDTAL-------VLQLRDALDLLERDLDalldalarLAATHRDTPM-VGRTHLQHAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 207 PMTVGQEFHAWAVTINEEIKNLEYTSKLLLEVNLGAtAIGTGlnAAPGYQGLAV-KHLAEVTGLEC------VAAEDLIE 279
Cdd:cd01597 152 PITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGG-AAGTL--ASLGDQGLAVqEALAAELGLGVpaipwhTARDRIAE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 280 ATSdcgayvmthgALKRLAVKLSKICNDLRLLSsgpRTGFNELNLPELQA--GSSIMPAKvNPVVPEVVNQVCFKVLGND 357
Cdd:cd01597 229 LAS----------FLALLTGTLGKIARDVYLLM---QTEIGEVAEPFAKGrgGSSTMPHK-RNPVGCELIVALARRVPGL 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 358 NTVSFAAE-------GGQLQLNvmEPVIAQSMFESLDILTNACVnlrdkCVDGITVNKEVCESHVFNSIG-IVT-----Y 424
Cdd:cd01597 295 AALLLDAMvqeherdAGAWHAE--WIALPEIFLLASGALEQAEF-----LLSGLEVNEDRMRANLDLTGGlILSeavmmA 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1589117612 425 LNPYIGHHEG-DIVGKICAET---GKSVRDVVLE----RGLLSEEELDDIFSVEN 471
Cdd:cd01597 368 LAPKLGRQEAhDLVYEACMRAveeGRPLREVLLEdpevAAYLSDEELDALLDPAN 422
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
145-471 |
2.92e-10 |
|
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: 62.18 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 145 NDHVnrsqstncayPTGFRISVYNSVLKLIDAIEYLKGAF-ELKSQEFNTILKmGRTQLQDAVPMTVGQEFHAWAVTINE 223
Cdd:cd01359 88 NDQV----------ATDLRLYLRDALLELLELLLDLQRALlDRAEEHADTIMP-GYTHLQRAQPITFGHYLLAYAEMLER 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 224 EIKNLEYTSKLLLEVNLGATAI-GTGLNAAPgyqglavKHLAEVTG--------LECVAAED-LIEATSDCgAYVMTHga 293
Cdd:cd01359 157 DLERLADAYKRVNVSPLGAGALaGTTFPIDR-------ERTAELLGfdgptensLDAVSDRDfVLEFLSAA-ALLMVH-- 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 294 lkrlavkLSKICNDLRLLSSGPrtgFNELNLP-ELQAGSSIMPAKvnpvvpevvnqvcfK--------------VLGNDN 358
Cdd:cd01359 227 -------LSRLAEDLILWSTQE---FGFVELPdAYSTGSSIMPQK--------------KnpdvlelirgkagrVIGALA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 359 TVSFAAEGGQLQLN-----VMEPviaqsMFESLDILtNACVNLRDKCVDGITVNKEVCESHVFNSIGIVTYLNPYI---- 429
Cdd:cd01359 283 GLLTTLKGLPLAYNkdlqeDKEP-----LFDAVDTL-IASLRLLTGVISTLTVNPERMREAAEAGFSTATDLADYLvrek 356
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1589117612 430 ------GHHegdIVGKI---CAETGKSVRDVVLER----GLLSEEELDDIFSVEN 471
Cdd:cd01359 357 gvpfreAHH---IVGRAvrlAEEKGKDLSDLTLAElqaiSPLFEEDVREALDPEN 408
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
172-337 |
2.84e-09 |
|
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: 58.90 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 172 KLIDAIEYlkgafelKSQEFNTILKMGRTQLQDAVPMTVGQEFHAWAVTINEEIKNLEYTSKLLLeVNLGATAIGTGLNA 251
Cdd:TIGR00928 122 QLIDRLKE-------LAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQLERLLQAKERIK-VGGISGAVGTHAAA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 252 APGYQGLAvKHLAEVTGLECVAAEDLIEATSDCGAYVMthgALKRLAVKLSKICNDLRLLSsgpRTGFNELNLP--ELQA 329
Cdd:TIGR00928 194 YPLVEEVE-ERVTEFLGLKPVPISTQIEPRDRHAELLD---ALALLATTLEKFAVDIRLLQ---RTEHFEVEEPfgKGQV 266
|
....*...
gi 1589117612 330 GSSIMPAK 337
Cdd:TIGR00928 267 GSSAMPHK 274
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
145-337 |
2.58e-07 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 52.85 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 145 NDHVnrsqstncAypTGFRISVYNSVLKLIDAIEYLKGAF-ELKSQEFNTILKmGRTQLQDAVPMTVGQEFHAWAVTINE 223
Cdd:PRK00855 112 NDQV--------A--TDLRLYLRDEIDEIAELLLELQKALlDLAEEHADTIMP-GYTHLQRAQPVTFGHHLLAYAEMLAR 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 224 EIKNLEYTSKLlleVN---LGATAI-GTGLNAAPgyqglavKHLAEVTGLEC--------VAAED-LIEATSDCgAYVMT 290
Cdd:PRK00855 181 DLERLRDARKR---VNrspLGSAALaGTTFPIDR-------ERTAELLGFDGvtensldaVSDRDfALEFLSAA-SLLMV 249
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1589117612 291 HgalkrlavkLSKICNDLRLLSSgPRTGFNELNlPELQAGSSIMPAK 337
Cdd:PRK00855 250 H---------LSRLAEELILWSS-QEFGFVELP-DAFSTGSSIMPQK 285
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
147-411 |
1.06e-06 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 51.32 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 147 HVNRSQSTNCAypTGFRISVYNSVLKLIDAIEYLKGAF-ELKSQEFNTILKmGRTQLQDAVPMTVGQEFHAWAVTINEEI 225
Cdd:PRK12308 104 HTGRSRNDQVA--TDLKLWCRQQGQQLLLALDQLQQQMvNVAERHQGTVLP-GYTHLQRAQPVTFAHWCLAYVEMFERDY 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 226 KNLEYTSKLLLEVNLGATAIgtglnAAPGY----QGLAVK---HLAEVTGLECVAAEDLIEATSDCGAYVMTHgalkrla 298
Cdd:PRK12308 181 SRLEDALTRLDTCPLGSGAL-----AGTAYpidrEALAHNlgfRRATRNSLDSVSDRDHVMELMSVASISMLH------- 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 299 vkLSKICNDLRLLSSGpRTGFNELNlPELQAGSSIMPAKVNPVVPEVVNQVCFKVLGNDNTVSFAAEGGQLQLNVMEPVI 378
Cdd:PRK12308 249 --LSRLAEDLIFYNSG-ESGFIELA-DTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKDMQED 324
|
250 260 270
....*....|....*....|....*....|...
gi 1589117612 379 AQSMFESLDILtNACVNLRDKCVDGITVNKEVC 411
Cdd:PRK12308 325 KEGLFDALDTW-NDCMEMAALCFDGIKVNGERT 356
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
171-337 |
4.66e-05 |
|
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: 45.62 E-value: 4.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 171 LKLIDAIEYL-KGAFEL------KSQEFNTILKMGRTQLQDAVPMTVGQEFHAWAVTINEEIKNLEYTSKlllEVNLGAT 243
Cdd:cd01360 101 LQLREALDIIlKDLKELlevlkkKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKEARE---RILVGKI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 244 --AIGTGLNAAPGYQglavKHLAEVTGLECVAAEDLIeATSDCGAYVMThgALKRLAVKLSKICNDLRLLSsgpRTGFNE 321
Cdd:cd01360 178 sgAVGTYANLGPEVE----ERVAEKLGLKPEPISTQV-IQRDRHAEYLS--TLALIASTLEKIATEIRHLQ---RTEVLE 247
|
170
....*....|....*...
gi 1589117612 322 LNLP--ELQAGSSIMPAK 337
Cdd:cd01360 248 VEEPfsKGQKGSSAMPHK 265
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
160-471 |
7.14e-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: 45.09 E-value: 7.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 160 TGFRISVYNSVLKLIDAIEYLKGAF-ELKSQEFNTIlkM-GRTQLQDAVPMTVGQEFHAWAVTINEEIKNLEYTSKlllE 237
Cdd:COG0165 116 TDFRLYLRDEILELIEALLALQEALlDLAEEHADTI--MpGYTHLQRAQPVTFGHHLLAYAEMLLRDRERLADAYK---R 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 238 VN---LGATAI-GTGLNAAPGYqglaVKHL---AEVT--GLECVAAED-LIEATSDCgAYVMTHgalkrlavkLSKICND 307
Cdd:COG0165 191 LNvspLGAAALaGTTFPIDRER----TAELlgfDGPTenSLDAVSDRDfALEFLSAA-SLIMVH---------LSRLAEE 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 308 LRLLSSGPrtgFNELNLPELQA-GSSIMPAKvnpvvpevvnqvcfK--------------VLGNDNTVsfaaeggqlqLN 372
Cdd:COG0165 257 LILWSSSE---FGFVELPDAFStGSSIMPQK--------------KnpdvaelirgktgrVIGNLTGL----------LT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 373 VM---------------EPViaqsmFESLDILTnACVNLRDKCVDGITVNKEVCESHV----FNSIGIVTYLN----PY- 428
Cdd:COG0165 310 TMkglplaynkdlqedkEPL-----FDAVDTLK-LCLRLFAGMIATLKVNRERMREAAgagfSTATDLADYLVrkgvPFr 383
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1589117612 429 IGHHegdIVGKI---CAETGKSVRDVVLER----GLLSEEELDDIFSVEN 471
Cdd:COG0165 384 EAHE---IVGRLvryAEEKGKDLEDLTLEElqafSPLIEEDVYEALDPEG 430
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
58-270 |
1.30e-04 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 43.89 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 58 VRGMVMTKKAAALANKELGVIPSEVAKYIIQACDlildtgkcmdQFPSDVFQGGAGTSVN-MNANEVVANVALELmGKEK 136
Cdd:PRK05975 30 IAAMLAFEAALAEAEAEHGIIPAEAAERIAAACE----------TFEPDLAALRHATARDgVVVPALVRQLRAAV-GEEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 137 GQyefinpndHVNRSQSTNCAYPTGFRISVYNSVLKLIDAIEYLKGAFELKSQEFNTILKMGRTQLQDAVPMTVGQEFHA 216
Cdd:PRK05975 99 AA--------HVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLAS 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1589117612 217 WAVTINEEIKNLEYTSKLLLEVNLGAtAIGTGLNAAPgyQGLAVK-HLAEVTGLE 270
Cdd:PRK05975 171 WRAPLLRHRDRLEALRADVFPLQFGG-AAGTLEKLGG--KAAAVRaRLAKRLGLE 222
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
40-471 |
8.11e-04 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 41.63 E-value: 8.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 40 AVENFNISnvtISdvpeFVRGM----VMTKKAAALANKELGVIPSEVAKYIIQACDLIldtgkcMDQFPSDVFQGGAG-T 114
Cdd:PLN02646 30 AVEKFNES---IS----FDKRLykedIMGSKAHASMLAKQGIITDEDRDSILDGLDEI------EKEIEAGKFEWRPDrE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 115 SVNMNaNEVvanvAL-ELMGKEKGQYefinpndHVNRSQSTNCAypTGFRISVYNSVLKLIDAIEYLKGAFELKSQEFNT 193
Cdd:PLN02646 97 DVHMN-NEA----RLtELIGEPAKKL-------HTARSRNDQVA--TDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 194 ILKMGRTQLQDAVPMTvgqeFHAWAVTINEEI-KNLEYTSKLLLEVN---LGATAI-GTGLnaapgyqGLAVKHLAEVTG 268
Cdd:PLN02646 163 LVVPGYTHLQRAQPVL----LSHWLLSHVEQLeRDAGRLVDCRPRVNfcpLGSCALaGTGL-------PIDRFMTAKDLG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 269 LECVAAEDlIEATSDCGAYVMTHGALKRLAVKLSKICNDLRLLSSGPrTGFNELNlPELQAGSSIMPAKVNPVVPEVVNQ 348
Cdd:PLN02646 232 FTAPMRNS-IDAVSDRDFVLEFLFANSITAIHLSRLGEEWVLWASEE-FGFVTPS-DAVSTGSSIMPQKKNPDPMELVRG 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 349 VCFKVLGNDNTVSFAAEGGQLQLN-----VMEPviaqsMFESLDILtNACVNLRDKCVDGITVNKE-----VCESHVfNS 418
Cdd:PLN02646 309 KSARVIGDLVTVLALCKGLPTAYNrdlqeDKEP-----LFDSVDTV-SDMLEVATEFAQNITFNPErikksLPAGML-DA 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1589117612 419 IGIVTYLN----PYIGHHegDIVG---KICAETGKSVRDVVLERgLLS-----EEELDDIFSVEN 471
Cdd:PLN02646 382 TTLADYLVrkgvPFRETH--HIVGaavALAESKGCELSDLTLED-LKSinpvfEEDVYEVLGVEN 443
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
58-337 |
4.57e-03 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 39.23 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 58 VRGMVMTKKAAALANKELGVIPSEVAKYIIQACDlildtgkcMDQFPSDVFQGGAGTSVNMN---ANEVVANVALELMGK 134
Cdd:PRK09053 27 VQRMLDFEAALARAEAACGVIPAAAVAPIEAACD--------AERLDLDALAQAAALAGNLAiplVKQLTAQVAARDAEA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 135 EKgqyefinpndHVNRSQSTNCAYPTGfrisvynSVLKLIDAIEYL--------KGAFELKSQEFNTILkMGRTQLQDAV 206
Cdd:PRK09053 99 AR----------YVHWGATSQDIIDTG-------LVLQLRDALDLLepdldrlcDALATLAARHRATPM-VGRTWLQQAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 207 PMTVGQEFHAWAVTINEEIKNLEYTSKLLLEVNLGATAigtGLNAAPGYQGLAV-KHLAEVTGLECVAA------EDLIE 279
Cdd:PRK09053 161 PVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGGAA---GTLASLGEQALPVaQALAAELQLALPALpwhtqrDRIAE 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 280 ATSdcgayvmthgALKRLAVKLSKICNDLRLLSsgpRTGFNELNLP--ELQAGSSIMPAK 337
Cdd:PRK09053 238 FAS----------ALGLLAGTLGKIARDVSLLM---QTEVGEVFEPaaAGKGGSSTMPHK 284
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
140-337 |
6.29e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 39.20 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 140 EFINpNDHVNRSQstNCAYPTGFRISVYNSVLKLIDAIEYLKGA-FELKSQEFNTILKmGRTQLQDAVPMTVGQEFHAWA 218
Cdd:PRK06705 105 DFVS-NMHIGRSR--NDMGVTMYRMSLRRYVLRLMEHHLLLQESiLQLAADHKETIMP-AYTHTQPAQPTTFGHYTLAIY 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 219 VTINEEIKNLEYTSKLLLEVNLGATAIGTglNAAPgyqgLAVKHLAEVTGLECVAaEDLIEATSDCGAYVMTHGALKRLA 298
Cdd:PRK06705 181 DTMQRDLERMKKTYKLLNQSPMGAAALST--TSFP----IKRERVADLLGFTNVI-ENSYDAVAGADYLLEVSSLLMVMM 253
|
170 180 190
....*....|....*....|....*....|....*....
gi 1589117612 299 VKLSKICNDLRLLSSGPRTGFNELNlPELQAgSSIMPAK 337
Cdd:PRK06705 254 TNTSRWIHDFLLLATKEYDGITVAR-PYVQI-SSIMPQK 290
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
293-471 |
8.29e-03 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 37.70 E-value: 8.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 293 ALKRLAVKLSKICNDLRLLSsgpRTGFNELNLP--ELQAGSSIMPAKVNPVVpevvnqvCFKVLGNDNTV-SFAAEGGQ- 368
Cdd:PRK08937 22 VLALIATSLEKFANEIRLLQ---RSEIREVEEPfaKGQKGSSAMPHKRNPIG-------SERITGLARVLrSYLVTALEn 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1589117612 369 --------LQLNVMEPVIAQSMFESLDILTNACVNlrdkCVDGITVNKEVCESHVFNSIG-------IVTYLNPYIGHHE 433
Cdd:PRK08937 92 vplwherdLSHSSAERIALPDAFLALDYILNRFVN----ILENLVVFPENIERNLDKTLGfiatervLLELVEKGMGREE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1589117612 434 G-DIVGK---ICAETGKSVRDVVLE----RGLLSEEELDDIFSVEN 471
Cdd:PRK08937 168 AhELIREkamEAWKNQKDLRELLEAderfTKQLTKEELDELFDPEA 213
|
|
| |
