|
Name |
Accession |
Description |
Interval |
E-value |
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
8-465 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 880.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 8 RIEKDFLGKKEVPSAAYYGVQTLRAVENFPITGYRI--HPSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEIVD 85
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPIsdHPELIRALAMVKKAAALANRELGLLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 86 GKFHDQFIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGEYAKISPNTHVNMAQSTNDAFPTGIHIATLMMLEELLIT 165
Cdd:COG1027 81 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLALLLLLRELLEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 166 MEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSRQHLYEVNMGATAVGTGLNANPTYI 245
Cdd:COG1027 161 LERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGYI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 246 EQVVKHLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGSSIMPG 325
Cdd:COG1027 241 ELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 326 KVNPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQYVE 405
Cdd:COG1027 321 KVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYVE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 406 KSVGIITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILDPFEMTHPE 465
Cdd:COG1027 401 NSIGLVTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGLLTEEELDEILDPENMTGPG 460
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
3-472 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 876.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 3 ATKDIRIEKDFLGKKEVPSAAYYGVQTLRAVENFPITGYRIH--PSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAA 80
Cdd:PRK12273 1 MMMNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKISdyPELIRALAMVKKAAALANKELGLLDEEKADAIVAAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 81 QEIVDGKFHDQFIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGEYAKISPNTHVNMAQSTNDAFPTGIHIATLMMLE 160
Cdd:PRK12273 81 DEILAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIALLLSLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 161 ELLITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSRQHLYEVNMGATAVGTGLNA 240
Cdd:PRK12273 161 KLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 241 NPTYIEQVVKHLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGS 320
Cdd:PRK12273 241 PPGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 321 SIMPGKVNPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELL 400
Cdd:PRK12273 321 SIMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEERC 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446484317 401 KQYVEKSVGIITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILDPFEMTHPEIAGASLL 472
Cdd:PRK12273 401 REYVENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTHPGYKGKRYT 472
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
4-473 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 869.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 4 TKDIRIEKDFLGKKEVPSAAYYGVQTLRAVENFPITGYRIHPSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEI 83
Cdd:PRK14515 8 KNGVRIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGYKIHEGLIKAFAIVKKAAALANTDVGRLELNKGGAIAEAAQEI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 84 VDGKFHDQFIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGEYAKISPNTHVNMAQSTNDAFPTGIHIATLMMLEELL 163
Cdd:PRK14515 88 LDGKWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIATLNALEGLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 164 ITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSRQHLYEVNMGATAVGTGLNANPT 243
Cdd:PRK14515 168 QTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNADPE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 244 YIEQVVKHLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGSSIM 323
Cdd:PRK14515 248 YIEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSIM 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 324 PGKVNPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQY 403
Cdd:PRK14515 328 PGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKEY 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 404 VEKSVGIITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILDPFEMTHPEIAGASLLK 473
Cdd:PRK14515 408 VEKSVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEMTHPGIAGATLLK 477
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
5-475 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 833.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 5 KDIRIEKDFLGKKEVPSAAYYGVQTLRAVENFPITGYRIHPSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEIV 84
Cdd:PRK13353 3 KNMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYKIHPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQACDEIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 85 DGKFHDQFIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGEYAKISPNTHVNMAQSTNDAFPTGIHIATLMMLEELLI 164
Cdd:PRK13353 83 AGKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLLEGLLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 165 TMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSRQHLYEVNMGATAVGTGLNANPTY 244
Cdd:PRK13353 163 AMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADPEY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 245 IEQVVKHLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGSSIMP 324
Cdd:PRK13353 243 IERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSIMP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 325 GKVNPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQYV 404
Cdd:PRK13353 323 GKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKEYV 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446484317 405 EKSVGIITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILDPFEMTHPEIAGASLLKNK 475
Cdd:PRK13353 403 EKSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMTHPGIAGATLLKKN 473
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
8-457 |
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: 818.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 8 RIEKDFLGKKEVPSAAYYGVQTLRAVENFPITGYRIHPSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEIVDGK 87
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISGLKIHPELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 88 FHDQFIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGEYAKISPNTHVNMAQSTNDAFPTGIHIATLMMLEELLITME 167
Cdd:cd01357 81 LHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLALILLLRKLLDALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 168 ELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSRQHLYEVNMGATAVGTGLNANPTYIEQ 247
Cdd:cd01357 161 ALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGYIEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 248 VVKHLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGSSIMPGKV 327
Cdd:cd01357 241 VVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMPGKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 328 NPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQYVEKS 407
Cdd:cd01357 321 NPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYVENS 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 446484317 408 VGIITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILD 457
Cdd:cd01357 401 IGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELDEILS 450
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
8-457 |
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: 762.35 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 8 RIEKDFLGKKEVPSAAYYGVQTLRAVENFPITGYRIHPSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEIVDGK 87
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISGERMPPELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 88 FHDQFIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGEYAKISPNTHVNMAQSTNDAFPTGIHIATLMMLEELLITME 167
Cdd:cd01596 81 LDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKGKYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLPALE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 168 ELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSRQHLYEVNMGATAVGTGLNANPTYIEQ 247
Cdd:cd01596 161 QLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGYAEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 248 VVKHLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGSSIMPGKV 327
Cdd:cd01596 241 VAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMPGKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 328 NPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQYVEKS 407
Cdd:cd01596 321 NPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYVENS 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 446484317 408 VGIITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILD 457
Cdd:cd01596 401 LMLVTALNPHIGYEKAAEIAKEALKEGRTLREAALELGLLTEEELDEILD 450
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
8-472 |
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: 749.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 8 RIEKDFLGKKEVPSAAYYGVQTLRAVENFPITGYRIH--PSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEIVD 85
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKISdiPEFVRGMVMVKKAAALANKELGTIPESIANAIVAACDEILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 86 -GKFHDQFIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGEYAKISPNTHVNMAQSTNDAFPTGIHIATLMMLEELLI 164
Cdd:TIGR00839 81 nGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIAVYSSLIKLVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 165 TMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSRQHLYEVNMGATAVGTGLNANPTY 244
Cdd:TIGR00839 161 AINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 245 IEQVVKHLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGSSIMP 324
Cdd:TIGR00839 241 SPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 325 GKVNPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQYV 404
Cdd:TIGR00839 321 AKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGYV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446484317 405 EKSVGIITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILDPFEMTHPEIAGASLL 472
Cdd:TIGR00839 401 FNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLMHPAYKAKRYK 468
|
|
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
4-463 |
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: 654.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 4 TKDIRIEKDFLGKKEVPSAAYYGVQTLRAVENFPITGYRIHPSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEI 83
Cdd:COG0114 1 MMETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGERMPREFIRALALIKKAAARANAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 84 VDGKFHDQFIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGEYAKISPNTHVNMAQSTNDAFPTGIHIATLMMLEELL 163
Cdd:COG0114 81 IAGKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 164 I-TMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSRQHLYEVNMGATAVGTGLNANP 242
Cdd:COG0114 161 LpALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 243 TYIEQVVKHLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGSSI 322
Cdd:COG0114 241 GFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 323 MPGKVNPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQ 402
Cdd:COG0114 321 MPGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446484317 403 YVEKSVGIITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILDPFEMTH 463
Cdd:COG0114 401 LLERSLMLVTALNPHIGYDKAAKIAKKAHKEGRTLREAALELGLLSEEEFDRLVDPEKMTG 461
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
4-466 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 637.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 4 TKDIRIEKDFLGKKEVPSAAYYGVQTLRAVENFPITGYRIHPSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEI 83
Cdd:PRK00485 1 MMETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALALLKKAAARVNAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 84 VDGKFHDQFIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGEYAKISPNTHVNMAQSTNDAFPTGIHIATLMMLEELL 163
Cdd:PRK00485 81 IAGKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 164 I-TMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSRQHLYEVNMGATAVGTGLNANP 242
Cdd:PRK00485 161 LpALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 243 TYIEQVVKHLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGSSI 322
Cdd:PRK00485 241 GFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 323 MPGKVNPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQ 402
Cdd:PRK00485 321 MPGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446484317 403 YVEKSVGIITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILDPFEMTHPEI 466
Cdd:PRK00485 401 LLERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPGK 464
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
8-461 |
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: 604.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 8 RIEKDFLGKKEVPSAAYYGVQTLRAVENFPITGYRIHPSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEIVDGK 87
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 88 FHDQFIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGEYAKISPNTHVNMAQSTNDAFPTGIHIATLMMLEELLI-TM 166
Cdd:cd01362 81 LDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQERLLpAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 167 EELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSRQHLYEVNMGATAVGTGLNANPTYIE 246
Cdd:cd01362 161 KHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGFAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 247 QVVKHLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGSSIMPGK 326
Cdd:cd01362 241 KVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMPGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 327 VNPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQYVEK 406
Cdd:cd01362 321 VNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELLER 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446484317 407 SVGIITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILDPFEM 461
Cdd:cd01362 401 SLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRLVDPEKM 455
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
14-465 |
0e+00 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 555.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 14 LGKKEVPSAAYYGVQTLRAVENFPITGY--RIHPSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEIVDGKFHDQ 91
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGGEreRMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAEGKLDDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 92 FIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGEYAKISPNTHVNMAQSTNDAFPTGIHIATLMMLEELLI-TMEELH 170
Cdd:PLN00134 81 FPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATEIHSRLIpALKELH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 171 SAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSRQHLYEVNMGATAVGTGLNANPTYIEQVVK 250
Cdd:PLN00134 161 ESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 251 HLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGSSIMPGKVNPV 330
Cdd:PLN00134 241 AVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 331 MAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQYVEKSVGI 410
Cdd:PLN00134 321 QCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLML 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446484317 411 ITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILDPFEMTHPE 465
Cdd:PLN00134 401 VTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTGPS 455
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
8-461 |
8.79e-143 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 417.40 E-value: 8.79e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 8 RIEKDFLGKKEVPSAAYYGVQTLRAVENFPITGYRIHPSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEIVDGK 87
Cdd:PRK12425 3 RTETDSLGPIEVPEDAYWGAQTQRSLINFAIGKERMPLAVLHALALIKKAAARVNDRNGDLPADIARLIEQAADEVLDGQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 88 FHDQFIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGEYAKISPNTHVNMAQSTNDAFPTGIHIATLMML-EELLITM 166
Cdd:PRK12425 83 HDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVhEQLLPAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 167 EELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSRQHLYEVNMGATAVGTGLNANPTYIE 246
Cdd:PRK12425 163 AELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGFAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 247 QVVKHLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGSSIMPGK 326
Cdd:PRK12425 243 AIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMPGK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 327 VNPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQYVEK 406
Cdd:PRK12425 323 VNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHLER 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446484317 407 SVGIITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILDPFEM 461
Cdd:PRK12425 403 GLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENM 457
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
15-344 |
6.04e-125 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 366.31 E-value: 6.04e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 15 GKKEVPSAAYYGVQTLRAVENFPITGYRIHpslitAMAIVKKAAALANIDTgylaKDIGHEIAEAAQEIV-DGKFHDQFI 93
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDIK-----GLAALKKAAAKANVIL----KEEAAAIIKALDEVAeEGKLDDQFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 94 VDPIQGGAGTSINMNTNEVIAnralERMGyekgeyAKISPNTHVNMAQSTNDAFPTGIHIATLMMLEELLIT-MEELHSA 172
Cdd:pfam00206 72 LKVWQEGSGTAVNMNLNEVIG----ELLG------QLVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPaLRQLIDA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 173 FRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSRQ-HLYEVNMGATAVGTGLNANPTYIEQVVKH 251
Cdd:pfam00206 142 LKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPrLLVLPLGGGTAVGTGLNADPEFAELVAKE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 252 LRTFSGFPlVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPrVGLAEIQLPARQPGSSIMPGKVNPVM 331
Cdd:pfam00206 222 LGFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPDQ 299
|
330
....*....|...
gi 446484317 332 AEVINQVAFQVIG 344
Cdd:pfam00206 300 LELLTGKAGRVMG 312
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
48-396 |
6.98e-118 |
|
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: 348.72 E-value: 6.98e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 48 ITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEIVDGKFHDQFIvdpiQGGAGTSINMNTNEVIANRALErmgyekge 127
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVE----QEGSGTHDVMAVEEVLAERAGE-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 128 yakiSPNTHVNMAQSTNDAFPTGIHIATLMMLEELLITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYS 207
Cdd:cd01334 69 ----LNGGYVHTGRSSNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 208 RVLERDIKRIKQSRQHLYEVNMGATAVGTGLNANPTYIEQVVKHLrtfsGFpLVGAEHLVDATQNTDAYTEVSAALKVCM 287
Cdd:cd01334 145 AELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAELL----GF-FGPAPNSTQAVSDRDFLVELLSALALLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 288 MNMSKIANDLRIMASGprvGLAEIQLPAR-QPGSSIMPGKVNPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPV 366
Cdd:cd01334 220 VSLSKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPV 296
|
330 340 350
....*....|....*....|....*....|
gi 446484317 367 LVFNLIQSISIMNNGFRVFREYCiEGITAN 396
Cdd:cd01334 297 EREALPDSFDLLDAALRLLTGVL-EGLEVN 325
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
107-386 |
2.57e-56 |
|
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: 186.66 E-value: 2.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 107 MNTNEVIANRALERMGYEKGEYakispntHVNMAQSTNDAFPTGIHIATLMMLEELLITMEELHSAFRKKAKEFDHVIKM 186
Cdd:cd01594 14 ALVEEVLAGRAGELAGGLHGSA-------LVHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 187 GRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSRqhlyevnmgatavgtglnanptyieqvvkhlrtfsgfplvgaehl 266
Cdd:cd01594 87 GRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEAA--------------------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 267 vdatqntdaYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPaRQPGSSIMPGKVNPVMAEVINQVAFQVIGND 346
Cdd:cd01594 122 ---------VAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGNL 191
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446484317 347 HTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFR 386
Cdd:cd01594 192 VAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
65-460 |
2.44e-28 |
|
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: 117.07 E-value: 2.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 65 TGYLAKDIGHEIAEAAQEIVDGKFHDQFIVDPIQggagTSINMNtnevIANRALERMGYEKGEYakispnthVNMAQSTN 144
Cdd:TIGR00838 45 AGILTEEEAAKIIEGLNELKEEGREGPFILDPDD----EDIHMA----IERELIDRVGEDLGGK--------LHTGRSRN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 145 DAFPTGIHIATLMMLEELLITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSRQHL 224
Cdd:TIGR00838 109 DQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLRDYERLQDALKRV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 225 YEVNMGATAV-GTGLNANPTYIeqvvKHLRTFSGFplvgAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASG 303
Cdd:TIGR00838 189 NVSPLGSGALaGTGFPIDREYL----AELLGFDAV----TENSLDAVSDRDFILELLFVAALIMVHLSRFAEDLILWSTG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 304 PrvgLAEIQLPAR-QPGSSIMPGKVNPVMAEVINQVAFQVIGNDHTICLASEAGQLELN-----VMEPVL-----VFNLI 372
Cdd:TIGR00838 261 E---FGFVELPDEfSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNrdlqeDKEPLFdalktVELSL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 373 QSISIMNNGFRVFREYCIEGITAN----EELLKQYVEKSVGIITAvnphigYEAASRIAREAIETGKSVRELCLEHGV-- 446
Cdd:TIGR00838 338 EMATGMLDTITVNKERMEEAASAGfsnaTELADYLVRKGVPFREA------HHIVGELVATAIERGKGLEELTLEELQkf 411
|
410
....*....|....*.
gi 446484317 447 --LTEEELDIILDPFE 460
Cdd:TIGR00838 412 spEFDEDVYEALDPES 427
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
156-458 |
1.38e-25 |
|
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: 108.63 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 156 LMM---LEELLITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSRQHLYEVNMGAt 232
Cdd:COG0015 109 LQLreaLELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVGKIGG- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 233 AVGTgLNANPTYIEQVVKHLrtfsgfplvgAEHL-----VDATQNT--DAYTEVSAALKVCMMNMSKIANDLRIMASgPR 305
Cdd:COG0015 188 AVGT-YAAHGEAWPEVEERV----------AEKLglkpnPVTTQIEprDRHAELFSALALIAGSLEKIARDIRLLQR-TE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 306 VGLAEIQLPARQPGSSIMPGKVNPVMAEVINQVAFQVIGN-DHticlASEAGQLELN----------VMEPVLVFNLIQS 374
Cdd:COG0015 256 VGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALaAA----LLEALASWHErdlsdssverNILPDAFLLLDGA 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 375 ISIMNNGfrvfreycIEGITANEELLKQYVEKSVGII------TAVNPH-IG----YEAASRIAREAIETGKSVRELCLE 443
Cdd:COG0015 332 LERLLKL--------LEGLVVNPERMRANLDLTGGLVlseavlMALVRRgLGreeaYELVKELARGAWEEGNDLRELLAA 403
|
330
....*....|....*....
gi 446484317 444 H----GVLTEEELDIILDP 458
Cdd:COG0015 404 DpeipAELSKEELEALFDP 422
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
56-458 |
2.09e-25 |
|
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: 108.02 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 56 KAAALANIDTGYLAKDIGHEIAEAAQEIVDGKFHDQFIVDPIQGGagtsINMNtnevIANRALERMGyekgEYAKispNT 135
Cdd:cd01359 17 IAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDED----IHMA----IERRLIERIG----DVGG---KL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 136 HvnMAQSTNDafptgiHIAT---LMMLEELLITME---ELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRV 209
Cdd:cd01359 82 H--TGRSRND------QVATdlrLYLRDALLELLElllDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 210 LERDIKRIKQSRQHLYEVNMGATA-VGTGLNANPTYieqvVKHLRTFSGfplvGAEHLVDATQNTDAYTEVSAALKVCMM 288
Cdd:cd01359 154 LERDLERLADAYKRVNVSPLGAGAlAGTTFPIDRER----TAELLGFDG----PTENSLDAVSDRDFVLEFLSAAALLMV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 289 NMSKIANDLrIMASGPRVGLaeIQLPAR-QPGSSIMPGKVNPVMAEVINQVAFQVIGNdHTICLASEAGqLELN------ 361
Cdd:cd01359 226 HLSRLAEDL-ILWSTQEFGF--VELPDAySTGSSIMPQKKNPDVLELIRGKAGRVIGA-LAGLLTTLKG-LPLAynkdlq 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 362 -VMEPVLvfnliQSISIMNNGFRVFREyCIEGITANEELLKQYVEKsvGIITAVN-----------P-HIGYEAASRIAR 428
Cdd:cd01359 301 eDKEPLF-----DAVDTLIASLRLLTG-VISTLTVNPERMREAAEA--GFSTATDladylvrekgvPfREAHHIVGRAVR 372
|
410 420 430
....*....|....*....|....*....|....
gi 446484317 429 EAIETGKSVRELCLE----HGVLTEEELDIILDP 458
Cdd:cd01359 373 LAEEKGKDLSDLTLAelqaISPLFEEDVREALDP 406
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
410-461 |
7.06e-23 |
|
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: 91.23 E-value: 7.06e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 446484317 410 IITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILDPFEM 461
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
139-460 |
2.67e-22 |
|
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: 99.02 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 139 MAQSTNDAfptgihIATLMML---EELLITMEELH---SAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLER 212
Cdd:COG0165 106 TGRSRNDQ------VATDFRLylrDEILELIEALLalqEALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLLR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 213 DIKRIKQSRQHLYEVNMGATAV-GTGLNANPtyiEQVVKHLrtfsGFPLVgAEHLVDATQNTDAYTEVSAALKVCMMNMS 291
Cdd:COG0165 180 DRERLADAYKRLNVSPLGAAALaGTTFPIDR---ERTAELL----GFDGP-TENSLDAVSDRDFALEFLSAASLIMVHLS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 292 KIANDLRIMASgPRVGLaeIQLPARQ-PGSSIMPGKVNPVMAEVINQVAFQVIGNDHTIclaseagqleLNVM------- 363
Cdd:COG0165 252 RLAEELILWSS-SEFGF--VELPDAFsTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGL----------LTTMkglplay 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 364 --------EPvlVFNLIQSISIMnngFRVFREyCIEGITANEELLKQYVEKsvgiitavnphiGYEAASRIA-------- 427
Cdd:COG0165 319 nkdlqedkEP--LFDAVDTLKLC---LRLFAG-MIATLKVNRERMREAAGA------------GFSTATDLAdylvrkgv 380
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 446484317 428 --REAIE-TGKSVReLCLEHGV----LTEEELDIILDPFE 460
Cdd:COG0165 381 pfREAHEiVGRLVR-YAEEKGKdledLTLEELQAFSPLIE 419
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
140-455 |
8.73e-22 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 97.53 E-value: 8.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 140 AQSTNDafptgiHIATLMML---EELLITMEELHSAFR---KKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERD 213
Cdd:PRK00855 108 GRSRND------QVATDLRLylrDEIDEIAELLLELQKallDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARD 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 214 IKRIKQSRQHlyeVNM---GATA-VGTGLNANPtyiEQVVKHLrtfsGFPLVgAEHLVDATQNTDAYTEVSAALKVCMMN 289
Cdd:PRK00855 182 LERLRDARKR---VNRsplGSAAlAGTTFPIDR---ERTAELL----GFDGV-TENSLDAVSDRDFALEFLSAASLLMVH 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 290 MSKIANDLrIMASGPRVGLaeIQLPAR-QPGSSIMPGKVNPVMAEVINQVAFQVIGNDHTIclaseagqleLNVM----- 363
Cdd:PRK00855 251 LSRLAEEL-ILWSSQEFGF--VELPDAfSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGL----------LTVMkglpl 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 364 ----------EPVL--VFNLIQSISIMNngfrvfreYCIEGITANEELLKQYVEKsvGIITA-------VNPHI----GY 420
Cdd:PRK00855 318 aynrdlqedkEPLFdaVDTLKLSLEAMA--------GMLETLTVNKERMREAAGK--GFSTAtdladylVRKGVpfreAH 387
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 446484317 421 EAASRIAREAIETGKSVRELCLE-----HGVLTEEELDII 455
Cdd:PRK00855 388 EIVGKAVREAEERGVDLADLSLEelqafSPLITEDVYEVL 427
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
154-335 |
4.55e-18 |
|
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: 85.63 E-value: 4.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 154 ATLMML----EELLITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSRQHLYeVNM 229
Cdd:cd01595 96 ALALQLrdalDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVL-VGG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 230 GATAVGTGLNANPTyIEQVVKHLRTFSGFPLVGAehlvdATQNT--DAYTEVSAALKVCMMNMSKIANDLRIMAsgpRVG 307
Cdd:cd01595 175 ISGAVGTHASLGPK-GPEVEERVAEKLGLKVPPI-----TTQIEprDRIAELLSALALIAGTLEKIATDIRLLQ---RTE 245
|
170 180 190
....*....|....*....|....*....|
gi 446484317 308 LAEIQLPAR--QPGSSIMPGKVNPVMAEVI 335
Cdd:cd01595 246 IGEVEEPFEkgQVGSSTMPHKRNPIDSENI 275
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
46-458 |
2.80e-17 |
|
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: 83.83 E-value: 2.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 46 SLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAqeivdgkfhDQFIVDPIQGGAGTSINMNTneVIAN-RALER-MGY 123
Cdd:cd01597 19 NRVQAMLDVEAALARAQAELGVIPKEAAAEIAAAA---------DVERLDLEALAEATARTGHP--AIPLvKQLTAaCGD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 124 EKGEYakispnthVNMAQSTNDAFPTGIhiaTLMMLEELLITMEELH---SAFRKKAKEFDHVIKMGRTHLQDAVPIRLG 200
Cdd:cd01597 88 AAGEY--------VHWGATTQDIIDTAL---VLQLRDALDLLERDLDallDALARLAATHRDTPMVGRTHLQHALPITFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 201 QEFEAYSRVLERDIKRIKQSRQHLYEVNMGAtAVGTgLNANPTYIEQVVKHLrtfsgfplvgAEHLVDATQNT------D 274
Cdd:cd01597 157 LKVAVWLSELLRHRERLDELRPRVLVVQFGG-AAGT-LASLGDQGLAVQEAL----------AAELGLGVPAIpwhtarD 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 275 AYTEVSAALKVCMMNMSKIANDLRIMAsgpRVGLAEIQLPAR--QPGSSIMPGKVNPVMAEVINQVAFQVIGNDHTIcLA 352
Cdd:cd01597 225 RIAELASFLALLTGTLGKIARDVYLLM---QTEIGEVAEPFAkgRGGSSTMPHKRNPVGCELIVALARRVPGLAALL-LD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 353 SEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQYVEKSVGIITA------VNPHIG----YEA 422
Cdd:cd01597 301 AMVQEHERDAGAWHAEWIALPEIFLLASGALEQAEFLLSGLEVNEDRMRANLDLTGGLILSeavmmaLAPKLGrqeaHDL 380
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 446484317 423 ASRIAREAIETGKSVRELCLEH----GVLTEEELDIILDP 458
Cdd:cd01597 381 VYEACMRAVEEGRPLREVLLEDpevaAYLSDEELDALLDP 420
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
159-460 |
3.19e-16 |
|
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: 80.47 E-value: 3.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 159 LEELLITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSRQhLYEVNMGATAVGTGL 238
Cdd:TIGR00928 113 LEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQLERLLQAKE-RIKVGGISGAVGTHA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 239 NANPTyIEQVVKHLRTFSGFPLVGAehlvdATQ--NTDAYTEVSAALKVCMMNMSKIANDLRIMAsGPRVGLAEIQLPAR 316
Cdd:TIGR00928 192 AAYPL-VEEVEERVTEFLGLKPVPI-----STQiePRDRHAELLDALALLATTLEKFAVDIRLLQ-RTEHFEVEEPFGKG 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 317 QPGSSIMPGKVNPVMAEVINQVAfqVIGNDHTICLASEAGQLE---------LNVMEPVLVFNLIQSISIMNNG---FRV 384
Cdd:TIGR00928 265 QVGSSAMPHKRNPIDFENVCGLA--RVIRGYASPALENAPLWHerdltdssvERVILPDAFILADIMLKTTLKVvkkLVV 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 385 FREYCIE------GITANEELLKQYVEKSVGIITAvnphigYEAASRIAREAIETGK-SVRELCLEHGVLT----EEELD 453
Cdd:TIGR00928 343 NPENILRnldltlGLIASERVLIALVERGMGREEA------YEIVRELAMGAAEVDEpDLLEFLLEDERITkylkEEELA 416
|
....*..
gi 446484317 454 IILDPFE 460
Cdd:TIGR00928 417 ELLDPET 423
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
167-335 |
1.64e-14 |
|
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: 74.90 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 167 EELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSRQhlyEVNMGAT--AVGTGLNANPTY 244
Cdd:cd01360 115 KELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKEARE---RILVGKIsgAVGTYANLGPEV 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 245 IEQVVKHLrtfsgfplvGAEHLVDATQ--NTDAYTEVSAALKVCMMNMSKIANDLRIMaSGPRVGLAEIQLPARQPGSSI 322
Cdd:cd01360 192 EERVAEKL---------GLKPEPISTQviQRDRHAEYLSTLALIASTLEKIATEIRHL-QRTEVLEVEEPFSKGQKGSSA 261
|
170
....*....|...
gi 446484317 323 MPGKVNPVMAEVI 335
Cdd:cd01360 262 MPHKRNPILSENI 274
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
134-456 |
1.23e-13 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 72.71 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 134 NTHVnmAQSTNDafpTGIHIATLMMLEELLITMEE---LHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVL 210
Cdd:PRK06705 109 NMHI--GRSRND---MGVTMYRMSLRRYVLRLMEHhllLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTM 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 211 ERDIKRIKQSRQHLYEVNMGATAVGTglNANPTYIEQVVKHLrtfsGFPLVgAEHLVDATQNTDAYTEVSAALKVCMMNM 290
Cdd:PRK06705 184 QRDLERMKKTYKLLNQSPMGAAALST--TSFPIKRERVADLL----GFTNV-IENSYDAVAGADYLLEVSSLLMVMMTNT 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 291 SKIANDLRIMASGPRVGLAeIQLPARQPgSSIMPGKVNPVMAEVINQVAFQVIGNDHTIClaseagQLELNV-------- 362
Cdd:PRK06705 257 SRWIHDFLLLATKEYDGIT-VARPYVQI-SSIMPQKRNPVSIEHARAITSSALGEAFTVF------QMIHNTpfgdivdt 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 363 ---MEPVLVFNLIQSISIMNNGFRVFREYCIEgitanEELLKQYVEKSVGIITAV------NPHI----GYEAASRIARE 429
Cdd:PRK06705 329 eddLQPYLYKGIEKAIRVFCIMNAVIRTMKVE-----EDTLKRRSYKHAITITDFadvltkNYGIpfrhAHHAASVIANM 403
|
330 340
....*....|....*....|....*...
gi 446484317 430 AIETGKSVRELCL-EHGVLTEEELDIIL 456
Cdd:PRK06705 404 SLEQKKELHELCFkDVNIYLQEKFKIQL 431
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
140-460 |
3.49e-12 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 68.21 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 140 AQSTNDAFPTGIHIATLMMLEELLITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQ 219
Cdd:PLN02646 120 ARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVD 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 220 SRQHLYEVNMGATAV-GTGLnanPTYIEQVVKHLrtfsGFPLVGAEHLvDATQNTDAYTEVSAALKVCMMNMSKIANDLR 298
Cdd:PLN02646 200 CRPRVNFCPLGSCALaGTGL---PIDRFMTAKDL----GFTAPMRNSI-DAVSDRDFVLEFLFANSITAIHLSRLGEEWV 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 299 IMASGPrVGLAEIQlPARQPGSSIMPGKVNPVMAEVINQVAFQVIGNDHTICLASEAGQLELN-----VMEPvlvfnLIQ 373
Cdd:PLN02646 272 LWASEE-FGFVTPS-DAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTAYNrdlqeDKEP-----LFD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 374 SISIMNNGFRVFREyCIEGITANEELLKQYVekSVGIITA-------VNPHIGYEAASRIareaieTGKSVReLCLEHGV 446
Cdd:PLN02646 345 SVDTVSDMLEVATE-FAQNITFNPERIKKSL--PAGMLDAttladylVRKGVPFRETHHI------VGAAVA-LAESKGC 414
|
330
....*....|....*...
gi 446484317 447 ----LTEEELDIILDPFE 460
Cdd:PLN02646 415 elsdLTLEDLKSINPVFE 432
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
141-344 |
6.67e-11 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 64.42 E-value: 6.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 141 QSTNDAFPTGIHIATLMMLEELLITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQS 220
Cdd:PRK12308 107 RSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYSRLEDA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 221 RQHLYEVNMGATAV-GTglnANPTYIEQVVKHLrtfsGFPLVGAEHLvDATQNTDAYTEVSAALKVCMMNMSKIANDLRI 299
Cdd:PRK12308 187 LTRLDTCPLGSGALaGT---AYPIDREALAHNL----GFRRATRNSL-DSVSDRDHVMELMSVASISMLHLSRLAEDLIF 258
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446484317 300 MASGpRVGLAEIQlPARQPGSSIMPGKVNPVMAEVINQVAFQVIG 344
Cdd:PRK12308 259 YNSG-ESGFIELA-DTVTSGSSLMPQKKNPDALELIRGKTGRVYG 301
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
142-335 |
7.88e-11 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 63.85 E-value: 7.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 142 STNDAFPTGIHIATLMMLEELLITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSR 221
Cdd:PRK04833 108 SRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDAL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 222 QHLYEVNMGATAV-GTglnANPTYIEQVVKHLrtfsGFPLVGAEHLvDATQNTDAYTEVSAALKVCMMNMSKIANDLRIM 300
Cdd:PRK04833 188 KRLDVSPLGSGALaGT---AYEIDREQLAGWL----GFASATRNSL-DSVSDRDHVLELLSDASISMVHLSRFAEDLIFF 259
|
170 180 190
....*....|....*....|....*....|....*.
gi 446484317 301 ASGPRvglAEIQLPAR-QPGSSIMPGKVNPVMAEVI 335
Cdd:PRK04833 260 NSGEA---GFVELSDRvTSGSSLMPQKKNPDALELI 292
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
289-458 |
4.92e-08 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 53.49 E-value: 4.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 289 NMSKIANDLRIMAsGPRVGLAEIQLPARQPGSSIMPGKVNPVMAEVINQVAFQVIGNdhtICLASEA------GQLELNV 362
Cdd:PRK08937 29 SLEKFANEIRLLQ-RSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSY---LVTALENvplwheRDLSHSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 363 MEPVLVFNLIQSISIMNNGFRvfreYCIEGITANEELLKQYVEKSVGII-------TAVNPHIG----YEAASRIAREAI 431
Cdd:PRK08937 105 AERIALPDAFLALDYILNRFV----NILENLVVFPENIERNLDKTLGFIatervllELVEKGMGreeaHELIREKAMEAW 180
|
170 180 190
....*....|....*....|....*....|.
gi 446484317 432 ETGKSVRELCLEH----GVLTEEELDIILDP 458
Cdd:PRK08937 181 KNQKDLRELLEADerftKQLTKEELDELFDP 211
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
135-335 |
5.12e-07 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 51.59 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 135 THVNMAQSTNDAFPTGIHIAtLMMLEELLIT-MEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERD 213
Cdd:PRK05975 100 AHVHFGATSQDVIDTSLMLR-LKAASEILAArLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 214 IKRIKQSRQHLYEVNMGAtAVGTGLNANPTyIEQVVKHLRTFSGfplvgaehLVDATQ---NTDAYTEVSAALKVCMMNM 290
Cdd:PRK05975 179 RDRLEALRADVFPLQFGG-AAGTLEKLGGK-AAAVRARLAKRLG--------LEDAPQwhsQRDFIADFAHLLSLVTGSL 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446484317 291 SKIANDLRIMASGPRvglaEIQLpARQPGSSIMPGKVNPVMAEVI 335
Cdd:PRK05975 249 GKFGQDIALMAQAGD----EISL-SGGGGSSAMPHKQNPVAAETL 288
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
192-344 |
7.37e-07 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 51.77 E-value: 7.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 192 QDAVPIRLGQEFEAYSRVLERDIKRIKQSRQHLYEVNMGATA-VGTGLNANPtyieQVVKHLRTFSgfplVGAEHLVDAT 270
Cdd:PRK02186 565 QPALPGSLGHYLLAVDGALARETHALFALFEHIDVCPLGAGAgGGTTFPIDP----EFVARLLGFE----QPAPNSLDAV 636
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446484317 271 QNTDAYTEVSAALKVCMMNMSKIANDLRI--MASgprvgLAEIQLPAR-QPGSSIMPGKVNPVMAEVINQVAFQVIG 344
Cdd:PRK02186 637 ASRDGVLHFLSAMAAISTVLSRLAQDLQLwtTRE-----FALVSLPDAlTGGSSMLPQKKNPFLLEFVKGRAGVVAG 708
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
175-358 |
6.31e-06 |
|
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: 48.47 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 175 KKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSRQHLYEVNMGATaVGTG------LNANPTYIEQV 248
Cdd:cd03302 128 EFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGVKGT-TGTQasfldlFEGDHDKVEAL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 249 VKHLRTFSGFPLVgaehlVDATQNTdaYT-----EVSAALKVCMMNMSKIANDLRIMAsgprvGLAEIQLP--ARQPGSS 321
Cdd:cd03302 207 DELVTKKAGFKKV-----YPVTGQT--YSrkvdiDVLNALSSLGATAHKIATDIRLLA-----NLKEVEEPfeKGQIGSS 274
|
170 180 190
....*....|....*....|....*....|....*..
gi 446484317 322 IMPGKVNPVMAEVINQVAFQVIGndhticLASEAGQL 358
Cdd:cd03302 275 AMPYKRNPMRSERCCSLARHLMN------LASNAAQT 305
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
157-330 |
1.20e-05 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 47.43 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 157 MMLEE-----LLITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSRqhlYEVNMgA 231
Cdd:PLN02848 136 LMLKEgvnsvVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMANFAYRLSRQRKQLSEVK---IKGKF-A 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 232 TAVGtglNANptyieqvvKHLRTFS--GFPLVGAEHLVDATQNTDAYT------EVSAALKVCMMNMSKIANDL-RIMAS 302
Cdd:PLN02848 212 GAVG---NYN--------AHMSAYPevDWPAVAEEFVTSLGLTFNPYVtqiephDYMAELFNAVSRFNNILIDFdRDIWS 280
|
170 180
....*....|....*....|....*...
gi 446484317 303 GPRVGLAEIQLPARQPGSSIMPGKVNPV 330
Cdd:PLN02848 281 YISLGYFKQITKAGEVGSSTMPHKVNPI 308
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
157-219 |
2.55e-05 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 46.67 E-value: 2.55e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446484317 157 MMLEE-----LLITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQ 219
Cdd:PRK09285 133 LMLKEareevLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLEA 200
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
144-330 |
7.75e-05 |
|
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: 44.92 E-value: 7.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 144 NDAFPTGIHIAtlmmLEELLI-TMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLERDIKRIKQSrQ 222
Cdd:cd01598 106 NLAYALMIKEA----RNEVILpLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLKQI-E 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484317 223 HLYEVNmGATavGTgLNAnptyieqvvkHLRTFSGFP-LVGAEHLVDA---------TQ--NTDAYTEVSAALK---VCM 287
Cdd:cd01598 181 ILGKFN-GAV--GN-FNA----------HLVAYPDVDwRKFSEFFVTSlgltwnpytTQiePHDYIAELFDALArinTIL 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446484317 288 MNMSKIA---NDLRIMASGPRVGlaEIqlparqpGSSIMPGKVNPV 330
Cdd:cd01598 247 IDLCRDIwgyISLGYFKQKVKKG--EV-------GSSTMPHKVNPI 283
|
|
| ADSL_C |
smart00998 |
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ... |
413-458 |
1.84e-03 |
|
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis of purine nucleotides: the conversion of succinylaminoimidazole-carboxamide ribotide into aminoimidazole-carboxamide ribotide (the fifth step of de novo IMP biosynthesis); the formation of adenosine monophosphate (AMP) from adenylosuccinate (the final step in the synthesis of AMP from IMP). This entry represents the C-terminal, seven alpha-helical, domain of adenylosuccinate lyase.
Pssm-ID: 198066 [Multi-domain] Cd Length: 81 Bit Score: 37.04 E-value: 1.84e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 446484317 413 AVNPHIG----YEAASRIAREAIETGKSVRELCLEH----GVLTEEELDIILDP 458
Cdd:smart00998 13 LVEKGLGreeaYELVQRAAMKAWEEGKDLRELLLADpevtAYLSEEELEELFDP 66
|
|
| |
