|
Name |
Accession |
Description |
Interval |
E-value |
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
6-478 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 867.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 6 EEKKVEIRIEKDFLGIKEVPRSAYYGIQTLRAVENFPITGYPIDKELIKALGMVKKAAALANMDVKRLYEGLGEVIVKAA 85
Cdd:PRK14515 5 TEVKNGVRIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGYKIHEGLIKAFAIVKKAAALANTDVGRLELNKGGAIAEAA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 86 EEVIDGKMDEQFIVDPIQGGAGTSLNMNTNEVICNRALELLGHEKGMYVHLSPNSHVNMSQSTNDVFPTAIHIATLNLLN 165
Cdd:PRK14515 85 QEILDGKWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIATLNALE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 166 RLLITMNNMHDEFNKKAIQFDSIIKMGRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQSYENLYEVNMGATAVGTGLNA 245
Cdd:PRK14515 165 GLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 246 DPYYIKSVVEHLALISKLPLINAEHLVDATQNTDAYTLVSSTLKICMVNMSKISNDLRLMASGPRAGLAEITLPARQPGS 325
Cdd:PRK14515 245 DPEYIEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 326 SIMPGKVNPVMPEMINQVAFQVIGNDHTISLASEAGQLELNVMEPVLVFNLLQSIRIMDNAFSVFTTYCLKDIQANEEQL 405
Cdd:PRK14515 325 SIMPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRL 404
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657210782 406 KEYVERSVGIITAVNPHIGYEVAARIARQAIVEGKSVRDLCLQYDVLTENELDLILDPYEMTNPGISGNSLLY 478
Cdd:PRK14515 405 KEYVEKSVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEMTHPGIAGATLLK 477
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
13-470 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 853.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 13 RIEKDFLGIKEVPRSAYYGIQTLRAVENFPITGYPI--DKELIKALGMVKKAAALANMDVKRLYEGLGEVIVKAAEEVID 90
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPIsdHPELIRALAMVKKAAALANRELGLLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 91 GKMDEQFIVDPIQGGAGTSLNMNTNEVICNRALELLGHEKGMYVHLSPNSHVNMSQSTNDVFPTAIHIATLNLLNRLLIT 170
Cdd:COG1027 81 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLALLLLLRELLEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 171 MNNMHDEFNKKAIQFDSIIKMGRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQSYENLYEVNMGATAVGTGLNADPYYI 250
Cdd:COG1027 161 LERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGYI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 251 KSVVEHLALISKLPLINAEHLVDATQNTDAYTLVSSTLKICMVNMSKISNDLRLMASGPRAGLAEITLPARQPGSSIMPG 330
Cdd:COG1027 241 ELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 331 KVNPVMPEMINQVAFQVIGNDHTISLASEAGQLELNVMEPVLVFNLLQSIRIMDNAFSVFTTYCLKDIQANEEQLKEYVE 410
Cdd:COG1027 321 KVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYVE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 411 RSVGIITAVNPHIGYEVAARIARQAIVEGKSVRDLCLQYDVLTENELDLILDPYEMTNPG 470
Cdd:COG1027 401 NSIGLVTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGLLTEEELDEILDPENMTGPG 460
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
11-473 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 842.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 11 EIRIEKDFLGIKEVPRSAYYGIQTLRAVENFPITGYPIDK--ELIKALGMVKKAAALANMDVKRLYEGLGEVIVKAAEEV 88
Cdd:PRK12273 4 NTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKISDypELIRALAMVKKAAALANKELGLLDEEKADAIVAACDEI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 89 IDGKMDEQFIVDPIQGGAGTSLNMNTNEVICNRALELLGHEKGMYVHLSPNSHVNMSQSTNDVFPTAIHIATLNLLNRLL 168
Cdd:PRK12273 84 LAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIALLLSLRKLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 169 ITMNNMHDEFNKKAIQFDSIIKMGRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQSYENLYEVNMGATAVGTGLNADPY 248
Cdd:PRK12273 164 DALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLNAPPG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 249 YIKSVVEHLALISKLPLINAEHLVDATQNTDAYTLVSSTLKICMVNMSKISNDLRLMASGPRAGLAEITLPARQPGSSIM 328
Cdd:PRK12273 244 YIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAGSSIM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 329 PGKVNPVMPEMINQVAFQVIGNDHTISLASEAGQLELNVMEPVLVFNLLQSIRIMDNAFSVFTTYCLKDIQANEEQLKEY 408
Cdd:PRK12273 324 PGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEERCREY 403
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657210782 409 VERSVGIITAVNPHIGYEVAARIARQAIVEGKSVRDLCLQYDVLTENELDLILDPYEMTNPGISG 473
Cdd:PRK12273 404 VENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTHPGYKG 468
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
8-480 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 813.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 8 KKVEIRIEKDFLGIKEVPRSAYYGIQTLRAVENFPITGYPIDKELIKALGMVKKAAALANMDVKRLYEGLGEVIVKAAEE 87
Cdd:PRK13353 1 TNKNMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYKIHPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQACDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 88 VIDGKMDEQFIVDPIQGGAGTSLNMNTNEVICNRALELLGHEKGMYVHLSPNSHVNMSQSTNDVFPTAIHIATLNLLNRL 167
Cdd:PRK13353 81 ILAGKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLLEGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 168 LITMNNMHDEFNKKAIQFDSIIKMGRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQSYENLYEVNMGATAVGTGLNADP 247
Cdd:PRK13353 161 LAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 248 YYIKSVVEHLALISKLPLINAEHLVDATQNTDAYTLVSSTLKICMVNMSKISNDLRLMASGPRAGLAEITLPARQPGSSI 327
Cdd:PRK13353 241 EYIERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 328 MPGKVNPVMPEMINQVAFQVIGNDHTISLASEAGQLELNVMEPVLVFNLLQSIRIMDNAFSVFTTYCLKDIQANEEQLKE 407
Cdd:PRK13353 321 MPGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKE 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 657210782 408 YVERSVGIITAVNPHIGYEVAARIARQAIVEGKSVRDLCLQYDVLTENELDLILDPYEMTNPGISGNSLLYNE 480
Cdd:PRK13353 401 YVEKSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMTHPGIAGATLLKKN 473
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
13-462 |
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: 795.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 13 RIEKDFLGIKEVPRSAYYGIQTLRAVENFPITGYPIDKELIKALGMVKKAAALANMDVKRLYEGLGEVIVKAAEEVIDGK 92
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISGLKIHPELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 93 MDEQFIVDPIQGGAGTSLNMNTNEVICNRALELLGHEKGMYVHLSPNSHVNMSQSTNDVFPTAIHIATLNLLNRLLITMN 172
Cdd:cd01357 81 LHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLALILLLRKLLDALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 173 NMHDEFNKKAIQFDSIIKMGRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQSYENLYEVNMGATAVGTGLNADPYYIKS 252
Cdd:cd01357 161 ALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGYIEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 253 VVEHLALISKLPLINAEHLVDATQNTDAYTLVSSTLKICMVNMSKISNDLRLMASGPRAGLAEITLPARQPGSSIMPGKV 332
Cdd:cd01357 241 VVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMPGKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 333 NPVMPEMINQVAFQVIGNDHTISLASEAGQLELNVMEPVLVFNLLQSIRIMDNAFSVFTTYCLKDIQANEEQLKEYVERS 412
Cdd:cd01357 321 NPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYVENS 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 657210782 413 VGIITAVNPHIGYEVAARIARQAIVEGKSVRDLCLQYDVLTENELDLILD 462
Cdd:cd01357 401 IGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELDEILS 450
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
13-462 |
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: 748.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 13 RIEKDFLGIKEVPRSAYYGIQTLRAVENFPITGYPIDKELIKALGMVKKAAALANMDVKRLYEGLGEVIVKAAEEVIDGK 92
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISGERMPPELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 93 MDEQFIVDPIQGGAGTSLNMNTNEVICNRALELLGHEKGMYVHLSPNSHVNMSQSTNDVFPTAIHIATLNLLNRLLITMN 172
Cdd:cd01596 81 LDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKGKYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLPALE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 173 NMHDEFNKKAIQFDSIIKMGRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQSYENLYEVNMGATAVGTGLNADPYYIKS 252
Cdd:cd01596 161 QLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGYAEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 253 VVEHLALISKLPLINAEHLVDATQNTDAYTLVSSTLKICMVNMSKISNDLRLMASGPRAGLAEITLPARQPGSSIMPGKV 332
Cdd:cd01596 241 VAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMPGKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 333 NPVMPEMINQVAFQVIGNDHTISLASEAGQLELNVMEPVLVFNLLQSIRIMDNAFSVFTTYCLKDIQANEEQLKEYVERS 412
Cdd:cd01596 321 NPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYVENS 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 657210782 413 VGIITAVNPHIGYEVAARIARQAIVEGKSVRDLCLQYDVLTENELDLILD 462
Cdd:cd01596 401 LMLVTALNPHIGYEKAAEIAKEALKEGRTLREAALELGLLTEEELDEILD 450
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
13-477 |
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: 698.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 13 RIEKDFLGIKEVPRSAYYGIQTLRAVENFPITGYPIDK--ELIKALGMVKKAAALANMDVKRLYEGLGEVIVKAAEEVID 90
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKISDipEFVRGMVMVKKAAALANKELGTIPESIANAIVAACDEILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 91 -GKMDEQFIVDPIQGGAGTSLNMNTNEVICNRALELLGHEKGMYVHLSPNSHVNMSQSTNDVFPTAIHIATLNLLNRLLI 169
Cdd:TIGR00839 81 nGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIAVYSSLIKLVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 170 TMNNMHDEFNKKAIQFDSIIKMGRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQSYENLYEVNMGATAVGTGLNADPYY 249
Cdd:TIGR00839 161 AINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 250 IKSVVEHLALISKLPLINAEHLVDATQNTDAYTLVSSTLKICMVNMSKISNDLRLMASGPRAGLAEITLPARQPGSSIMP 329
Cdd:TIGR00839 241 SPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 330 GKVNPVMPEMINQVAFQVIGNDHTISLASEAGQLELNVMEPVLVFNLLQSIRIMDNAFSVFTTYCLKDIQANEEQLKEYV 409
Cdd:TIGR00839 321 AKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGYV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 657210782 410 ERSVGIITAVNPHIGYEVAARIARQAIVEGKSVRDLCLQYDVLTENELDLILDPYEMTNPGISGNSLL 477
Cdd:TIGR00839 401 FNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLMHPAYKAKRYK 468
|
|
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
11-467 |
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: 642.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 11 EIRIEKDFLGIKEVPRSAYYGIQTLRAVENFPITGYPIDKELIKALGMVKKAAALANMDVKRLYEGLGEVIVKAAEEVID 90
Cdd:COG0114 3 ETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGERMPREFIRALALIKKAAARANAELGLLDAEKADAIVAAADEVIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 91 GKMDEQFIVDPIQGGAGTSLNMNTNEVICNRALELLGHEKGMYVHLSPNSHVNMSQSTNDVFPTAIHIAT-LNLLNRLLI 169
Cdd:COG0114 83 GKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAaLALEERLLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 170 TMNNMHDEFNKKAIQFDSIIKMGRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQSYENLYEVNMGATAVGTGLNADPYY 249
Cdd:COG0114 163 ALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHPGF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 250 IKSVVEHLALISKLPLINAEHLVDATQNTDAYTLVSSTLKICMVNMSKISNDLRLMASGPRAGLAEITLPARQPGSSIMP 329
Cdd:COG0114 243 AERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSIMP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 330 GKVNPVMPEMINQVAFQVIGNDHTISLASEAGQLELNVMEPVLVFNLLQSIRIMDNAFSVFTTYCLKDIQANEEQLKEYV 409
Cdd:COG0114 323 GKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEELL 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 657210782 410 ERSVGIITAVNPHIGYEVAARIARQAIVEGKSVRDLCLQYDVLTENELDLILDPYEMT 467
Cdd:COG0114 403 ERSLMLVTALNPHIGYDKAAKIAKKAHKEGRTLREAALELGLLSEEEFDRLVDPEKMT 460
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
11-471 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 631.36 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 11 EIRIEKDFLGIKEVPRSAYYGIQTLRAVENFPITGYPIDKELIKALGMVKKAAALANMDVKRLYEGLGEVIVKAAEEVID 90
Cdd:PRK00485 3 ETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALALLKKAAARVNAELGLLDAEKADAIVAAADEVIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 91 GKMDEQFIVDPIQGGAGTSLNMNTNEVICNRALELLGHEKGMYVHLSPNSHVNMSQSTNDVFPTAIHIA-TLNLLNRLLI 169
Cdd:PRK00485 83 GKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAaVLAIVERLLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 170 TMNNMHDEFNKKAIQFDSIIKMGRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQSYENLYEVNMGATAVGTGLNADPYY 249
Cdd:PRK00485 163 ALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHPGF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 250 IKSVVEHLALISKLPLINAEHLVDATQNTDAYTLVSSTLKICMVNMSKISNDLRLMASGPRAGLAEITLPARQPGSSIMP 329
Cdd:PRK00485 243 AERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSIMP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 330 GKVNPVMPEMINQVAFQVIGNDHTISLASEAGQLELNVMEPVLVFNLLQSIRIMDNAFSVFTTYCLKDIQANEEQLKEYV 409
Cdd:PRK00485 323 GKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKELL 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657210782 410 ERSVGIITAVNPHIGYEVAARIARQAIVEGKSVRDLCLQYDVLTENELDLILDPYEMTNPGI 471
Cdd:PRK00485 403 ERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPGK 464
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
13-466 |
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: 599.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 13 RIEKDFLGIKEVPRSAYYGIQTLRAVENFPITGYPIDKELIKALGMVKKAAALANMDVKRLYEGLGEVIVKAAEEVIDGK 92
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 93 MDEQFIVDPIQGGAGTSLNMNTNEVICNRALELLGHEKGMYVHLSPNSHVNMSQSTNDVFPTAIHIAT-LNLLNRLLITM 171
Cdd:cd01362 81 LDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAaLALQERLLPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 172 NNMHDEFNKKAIQFDSIIKMGRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQSYENLYEVNMGATAVGTGLNADPYYIK 251
Cdd:cd01362 161 KHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGFAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 252 SVVEHLALISKLPLINAEHLVDATQNTDAYTLVSSTLKICMVNMSKISNDLRLMASGPRAGLAEITLPARQPGSSIMPGK 331
Cdd:cd01362 241 KVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMPGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 332 VNPVMPEMINQVAFQVIGNDHTISLASEAGQLELNVMEPVLVFNLLQSIRIMDNAFSVFTTYCLKDIQANEEQLKEYVER 411
Cdd:cd01362 321 VNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELLER 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 657210782 412 SVGIITAVNPHIGYEVAARIARQAIVEGKSVRDLCLQYDVLTENELDLILDPYEM 466
Cdd:cd01362 401 SLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRLVDPEKM 455
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
19-470 |
0e+00 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 545.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 19 LGIKEVPRSAYYGIQTLRAVENFPITGYP--IDKELIKALGMVKKAAALANMDVKRLYEGLGEVIVKAAEEVIDGKMDEQ 96
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGGERerMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAEGKLDDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 97 FIVDPIQGGAGTSLNMNTNEVICNRALELLGHEKGMYVHLSPNSHVNMSQSTNDVFPTAIHIAT-LNLLNRLLITMNNMH 175
Cdd:PLN00134 81 FPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAaTEIHSRLIPALKELH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 176 DEFNKKAIQFDSIIKMGRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQSYENLYEVNMGATAVGTGLNADPYYIKSVVE 255
Cdd:PLN00134 161 ESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 256 HLALISKLPLINAEHLVDATQNTDAYTLVSSTLKICMVNMSKISNDLRLMASGPRAGLAEITLPARQPGSSIMPGKVNPV 335
Cdd:PLN00134 241 AVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 336 MPEMINQVAFQVIGNDHTISLASEAGQLELNVMEPVLVFNLLQSIRIMDNAFSVFTTYCLKDIQANEEQLKEYVERSVGI 415
Cdd:PLN00134 321 QCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLML 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 657210782 416 ITAVNPHIGYEVAARIARQAIVEGKSVRDLCLQYDVLTENELDLILDPYEMTNPG 470
Cdd:PLN00134 401 VTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTGPS 455
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
13-473 |
1.19e-138 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 407.00 E-value: 1.19e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 13 RIEKDFLGIKEVPRSAYYGIQTLRAVENFPITGYPIDKELIKALGMVKKAAALANMDVKRLYEGLGEVIVKAAEEVIDGK 92
Cdd:PRK12425 3 RTETDSLGPIEVPEDAYWGAQTQRSLINFAIGKERMPLAVLHALALIKKAAARVNDRNGDLPADIARLIEQAADEVLDGQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 93 MDEQFIVDPIQGGAGTSLNMNTNEVICNRALELLGHEKGMYVHLSPNSHVNMSQSTNDVFPTAIHIATLNLLN-RLLITM 171
Cdd:PRK12425 83 HDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVHeQLLPAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 172 NNMHDEFNKKAIQFDSIIKMGRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQSYENLYEVNMGATAVGTGLNADPYYIK 251
Cdd:PRK12425 163 AELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGFAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 252 SVVEHLALISKLPLINAEHLVDATQNTDAYTLVSSTLKICMVNMSKISNDLRLMASGPRAGLAEITLPARQPGSSIMPGK 331
Cdd:PRK12425 243 AIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMPGK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 332 VNPVMPEMINQVAFQVIGNDHTISLASEAGQLELNVMEPVLVFNLLQSIRIMDNAFSVFTTYCLKDIQANEEQLKEYVER 411
Cdd:PRK12425 323 VNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHLER 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 657210782 412 SVGIITAVNPHIGYEVAARIARQAIVEGKSVRDLCLQYDVLTENELDLILDPYEMTNPGISG 473
Cdd:PRK12425 403 GLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEAGGHG 464
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
20-349 |
7.72e-119 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 350.90 E-value: 7.72e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 20 GIKEVPRSAYYGIQTLRAVENFPITGypidkELIKALGMVKKAAALANMDVKRLyeglGEVIVKAAEEVI-DGKMDEQFI 98
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGE-----EDIKGLAALKKAAAKANVILKEE----AAAIIKALDEVAeEGKLDDQFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 99 VDPIQGGAGTSLNMNTNEVIcnralellGHEKGMYVHlsPNSHVNMSQSTNDVFPTAIHIA-TLNLLNRLLITMNNMHDE 177
Cdd:pfam00206 72 LKVWQEGSGTAVNMNLNEVI--------GELLGQLVH--PNDHVHTGQSSNDQVPTALRLAlKDALSEVLLPALRQLIDA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 178 FNKKAIQFDSIIKMGRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQSY-ENLYEVNMGATAVGTGLNADPYYIKSVVEH 256
Cdd:pfam00206 142 LKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLpRLLVLPLGGGTAVGTGLNADPEFAELVAKE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 257 LALISKLPLINAeHLVDATQNTDAYTLVSSTLKICMVNMSKISNDLRLMASGPrAGLAEITLPARQPGSSIMPGKVNPVM 336
Cdd:pfam00206 222 LGFFTGLPVKAP-NSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPDQ 299
|
330
....*....|...
gi 657210782 337 PEMINQVAFQVIG 349
Cdd:pfam00206 300 LELLTGKAGRVMG 312
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
53-401 |
2.66e-116 |
|
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: 344.49 E-value: 2.66e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 53 IKALGMVKKAAALANMDVKRLYEGLGEVIVKAAEEVIDGKMDEQFIvdpiQGGAGTSLNMNTNEVICNRALELLGHekgm 132
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVE----QEGSGTHDVMAVEEVLAERAGELNGG---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 133 yvhlspnsHVNMSQSTNDVFPTAIHIATLNLLNRLLITMNNMHDEFNKKAIQFDSIIKMGRTHLQDAVPIRLGQEFKAYA 212
Cdd:cd01334 73 --------YVHTGRSSNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 213 RVIKRDIKRIEQSYENLYEVNMGATAVGTGLNADPYYIKSVVEHLALISKlplinAEHLVDATQNTDAYTLVSSTLKICM 292
Cdd:cd01334 145 AELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAELLGFFGP-----APNSTQAVSDRDFLVELLSALALLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 293 VNMSKISNDLRLMASGpraGLAEITLPAR-QPGSSIMPGKVNPVMPEMINQVAFQVIGNDHTISLASEAGQLELNVMEPV 371
Cdd:cd01334 220 VSLSKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPV 296
|
330 340 350
....*....|....*....|....*....|
gi 657210782 372 LVFNLLQSIRIMDNAFSVFTTYClKDIQAN 401
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 ... |
109-391 |
2.34e-58 |
|
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: 192.05 E-value: 2.34e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 109 SLNMNTNEVICNRALELLGHEKGMYvhlspnsHVNMSQSTNDVFPTAIHIATLNLLNRLLITMNNMHDEFNKKAIQFDSI 188
Cdd:cd01594 11 AALALVEEVLAGRAGELAGGLHGSA-------LVHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 189 IKMGRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQSYenlyevnmgatavgtglnadpyyiksVVEhlalisklplina 268
Cdd:cd01594 84 VMPGRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEAA--------------------------VAE------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 269 ehlvdatqntdaytlVSSTLKICMVNMSKISNDLRLMASGPRAGLAEITLPaRQPGSSIMPGKVNPVMPEMINQVAFQVI 348
Cdd:cd01594 125 ---------------ALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVI 188
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 657210782 349 GNDHTISLASEAGQLELNVMEPVLVFNLLQSIRIMDNAFSVFT 391
Cdd:cd01594 189 GNLVAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
47-465 |
4.24e-27 |
|
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: 113.22 E-value: 4.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 47 PIDKELIKA--LG------MVKKAAALANMDVKRLYEGLGEVivkaAEEVIDGKMDEQFIVDPIqggagtslnmntNEVI 118
Cdd:TIGR00838 22 SFDKELAEYdiEGsiahtkMLKKAGILTEEEAAKIIEGLNEL----KEEGREGPFILDPDDEDI------------HMAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 119 CNRALELLGHEKGMYVHlspnshvnMSQSTNDVFPTAIHIATLNLLNRLLITMNNMHDEFNKKAIQFDSIIKMGRTHLQD 198
Cdd:TIGR00838 86 ERELIDRVGEDLGGKLH--------TGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 199 AVPIRLGQEFKAYARVIKRDIKRIEQSYENLYEVNMGATAV-GTGLNADPYYIKSVVEHLALIsklplinaEHLVDATQN 277
Cdd:TIGR00838 158 AQPITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALaGTGFPIDREYLAELLGFDAVT--------ENSLDAVSD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 278 TDAYTLVSSTLKICMVNMSKISNDLRLMASGpRAGLaeITLPAR-QPGSSIMPGKVNPVMPEMINQVAFQVIGNDHTISL 356
Cdd:TIGR00838 230 RDFILELLFVAALIMVHLSRFAEDLILWSTG-EFGF--VELPDEfSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 357 ASEAGQLELN-----VMEPVL--VFNLLQSIRIMdnafsvftTYCLKDIQANEEQLKEYVERSVGIITAVNPHI------ 423
Cdd:TIGR00838 307 TLKALPLAYNrdlqeDKEPLFdaLKTVELSLEMA--------TGMLDTITVNKERMEEAASAGFSNATELADYLvrkgvp 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 657210782 424 ---GYEVAARIARQAIVEGKSVRDLCL----QYDVLTENELDLILDPYE 465
Cdd:TIGR00838 379 freAHHIVGELVATAIERGKGLEELTLeelqKFSPEFDEDVYEALDPES 427
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
47-466 |
2.46e-20 |
|
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: 92.99 E-value: 2.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 47 PIDKELIKALGMVKKAAALANMDVKRLYEGLGEVIVKAAEEVIDGKMDEQFIVDPIQGGagtsLNMNtNEvicNRALELL 126
Cdd:cd01359 3 SFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDED----IHMA-IE---RRLIERI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 127 GhEKGMYVHLSpnshvnmsQSTNDVFPTAIHIATLNLLNRLLITMNNMHDEFNKKAIQFDSIIKMGRTHLQDAVPIRLGQ 206
Cdd:cd01359 75 G-DVGGKLHTG--------RSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 207 EFKAYARVIKRDIKRIEQSYENLYEVNMGATA-VGTGLNADPyyiksvvEHLAlisKL-----PLINAehlVDATQNTDa 280
Cdd:cd01359 146 YLLAYAEMLERDLERLADAYKRVNVSPLGAGAlAGTTFPIDR-------ERTA---ELlgfdgPTENS---LDAVSDRD- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 281 YTL-VSSTLKICMVNMSKISNDLRLMASGPRAGlaeITLPAR-QPGSSIMPGKVNPVMPEMINQVAFQVIGNdhTISLAS 358
Cdd:cd01359 212 FVLeFLSAAALLMVHLSRLAEDLILWSTQEFGF---VELPDAySTGSSIMPQKKNPDVLELIRGKAGRVIGA--LAGLLT 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 359 EAGQLELN-------VMEPV--LVFNLLQSIRIMdnafsvftTYCLKDIQANEEQLKEYVERsvGIITAVN--------- 420
Cdd:cd01359 287 TLKGLPLAynkdlqeDKEPLfdAVDTLIASLRLL--------TGVISTLTVNPERMREAAEA--GFSTATDladylvrek 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 657210782 421 --P-HIGYEVAARIARQAIVEGKSVRDLCL----QYDVLTENELDLILDPYEM 466
Cdd:cd01359 357 gvPfREAHHIVGRAVRLAEEKGKDLSDLTLaelqAISPLFEEDVREALDPENS 409
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
124-463 |
3.35e-20 |
|
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: 92.84 E-value: 3.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 124 ELLGHEKGMYVHLSPNShvnmsqstNDVFPTAIHIATLNLLNRLLITMNNMHDEFNKKAIQFDSIIKMGRTHLQDAVPIR 203
Cdd:COG0015 83 EKVGAEAGEYIHFGATS--------QDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTT 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 204 LGQEFKAYARVIKRDIKRIEQSYENLYEVNMGAtAVGTGLNADPYYI---KSVVEHLALisklplinaEHLVDATQNT-- 278
Cdd:COG0015 155 FGKKLAVWAAELLRQLERLEEARERVLVGKIGG-AVGTYAAHGEAWPeveERVAEKLGL---------KPNPVTTQIEpr 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 279 DAYTLVSSTLKICMVNMSKISNDLRLMASGPRAGLAEITlPARQPGSSIMPGKVNPVMPEMINQVAFQVIGNdhtISLAS 358
Cdd:COG0015 225 DRHAELFSALALIAGSLEKIARDIRLLQRTEVGEVEEPF-AKGQVGSSAMPHKRNPIDSENIEGLARLARAL---AAALL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 359 EAGQLEL------NVMEPVLvfnLLQSIRIMDNAFSVFTTyCLKDIQANEEQLKEYVERSVGII------TAVNPH-IG- 424
Cdd:COG0015 301 EALASWHerdlsdSSVERNI---LPDAFLLLDGALERLLK-LLEGLVVNPERMRANLDLTGGLVlseavlMALVRRgLGr 376
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 657210782 425 ---YEVAARIARQAIVEGKSVRDLCLQY----DVLTENELDLILDP 463
Cdd:COG0015 377 eeaYELVKELARGAWEEGNDLRELLAADpeipAELSKEELEALFDP 422
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
415-466 |
3.07e-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: 78.13 E-value: 3.07e-18
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 657210782 415 IITAVNPHIGYEVAARIARQAIVEGKSVRDLCLQYDVLTENELDLILDPYEM 466
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
147-465 |
3.53e-18 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 86.74 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 147 STNDVFPTAIHIATLNLLNRLLITMNNMHDEFNKKAIQFDSIIKMGRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQSY 226
Cdd:PRK00855 110 SRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLERLRDAR 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 227 ENlyeVNM---GATA-VGTGLNADPYYIksvvehlalisklplinAEHL--VDATQNT-DAytlVS---------STLKI 290
Cdd:PRK00855 190 KR---VNRsplGSAAlAGTTFPIDRERT-----------------AELLgfDGVTENSlDA---VSdrdfaleflSAASL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 291 CMVNMSKISNDLRLMASgPRAGLaeITLPAR-QPGSSIMPGKVNPVMPEMINQVAFQVIGndHTISLaseagqleLNVM- 368
Cdd:PRK00855 247 LMVHLSRLAEELILWSS-QEFGF--VELPDAfSTGSSIMPQKKNPDVAELIRGKTGRVYG--NLTGL--------LTVMk 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 369 --------------EPVL--VFNLLQSIRIMdnafsvftTYCLKDIQANEEQLKEYVERsvGIITA-------VNPHI-- 423
Cdd:PRK00855 314 glplaynrdlqedkEPLFdaVDTLKLSLEAM--------AGMLETLTVNKERMREAAGK--GFSTAtdladylVRKGVpf 383
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 657210782 424 --GYEVAARIARQAIVEGKSVRDLCL----QYDVLTENELDLILDPYE 465
Cdd:PRK00855 384 reAHEIVGKAVREAEERGVDLADLSLeelqAFSPLITEDVYEVLTPEG 431
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
191-463 |
1.00e-16 |
|
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: 82.29 E-value: 1.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 191 MGRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQSYENLYEVNMGAtAVGT--GLNADPYYI-KSVVEHLALIskLPLIn 267
Cdd:cd01597 142 VGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGG-AAGTlaSLGDQGLAVqEALAAELGLG--VPAI- 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 268 AEHlvdaTQNtDAYTLVSSTLKICMVNMSKISNDLRLMAsgpRAGLAEITLPAR--QPGSSIMPGKVNPVMPEMINQVAF 345
Cdd:cd01597 218 PWH----TAR-DRIAELASFLALLTGTLGKIARDVYLLM---QTEIGEVAEPFAkgRGGSSTMPHKRNPVGCELIVALAR 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 346 QVIGNdhtISLASEAGQLELN------VMEPVLvfnLLQSIRIMDNAFSVfTTYCLKDIQANEEQLKEYVERSVGIITA- 418
Cdd:cd01597 290 RVPGL---AALLLDAMVQEHErdagawHAEWIA---LPEIFLLASGALEQ-AEFLLSGLEVNEDRMRANLDLTGGLILSe 362
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 657210782 419 -----VNPHIG----YEVAARIARQAIVEGKSVRDLCLQYD----VLTENELDLILDP 463
Cdd:cd01597 363 avmmaLAPKLGrqeaHDLVYEACMRAVEEGRPLREVLLEDPevaaYLSDEELDALLDP 420
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
192-445 |
1.20e-16 |
|
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: 82.07 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 192 GRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQSYEnlyEVN---MGATAV-GTGLNADPYYIksvvehlalisklplin 267
Cdd:COG0165 154 GYTHLQRAQPVTFGHHLLAYAEMLLRDRERLADAYK---RLNvspLGAAALaGTTFPIDRERT----------------- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 268 AEHL--VDATQNT-DAytlVS---------STLKICMVNMSKISNDLRLMASgPRAGLaeITLPAR--QpGSSIMPGKVN 333
Cdd:COG0165 214 AELLgfDGPTENSlDA---VSdrdfaleflSAASLIMVHLSRLAEELILWSS-SEFGF--VELPDAfsT-GSSIMPQKKN 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 334 PVMPEMINQVAFQVIGndHTISLaseagqleLNVM---------------EPVL--VFNLLQSIRIMdnafsvftTYCLK 396
Cdd:COG0165 287 PDVAELIRGKTGRVIG--NLTGL--------LTTMkglplaynkdlqedkEPLFdaVDTLKLCLRLF--------AGMIA 348
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 397 DIQANEEQLKEYVERsvGIITA-----------VNPHIGYEVAARIARQAIVEGKSVRDL 445
Cdd:COG0165 349 TLKVNRERMREAAGA--GFSTAtdladylvrkgVPFREAHEIVGRLVRYAEEKGKDLEDL 406
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
180-365 |
1.48e-16 |
|
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: 81.01 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 180 KKAIQFDSIIKMGRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQSYENLYeVNMGATAVGTGLNADPYYI---KSVVEH 256
Cdd:cd01595 121 KLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVL-VGGISGAVGTHASLGPKGPeveERVAEK 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 257 LALisKLPLInaehlvdATQNT--DAYTLVSSTLKICMVNMSKISNDLRLMAsgpRAGLAEITLPAR--QPGSSIMPGKV 332
Cdd:cd01595 200 LGL--KVPPI-------TTQIEprDRIAELLSALALIAGTLEKIATDIRLLQ---RTEIGEVEEPFEkgQVGSSTMPHKR 267
|
170 180 190
....*....|....*....|....*....|...
gi 657210782 333 NPVMPEMINQVAFQVIGNdhtISLASEAGQLEL 365
Cdd:cd01595 268 NPIDSENIEGLARLVRAL---AAPALENLVQWH 297
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
141-463 |
2.36e-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: 80.85 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 141 HVNMSQSTNDVFPTAIHIATLNLLNRLLITMNNMHDEFNKKAIQFDSIIKMGRTHLQDAVPIRLGQEFKAYARVIKRDIK 220
Cdd:TIGR00928 90 FIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQLE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 221 RIEQSyENLYEVNMGATAVGTGLNADPYYIKS---VVEHLALISKLPLINAEHLVDATQNTDAYTLVSSTLkicmvnmSK 297
Cdd:TIGR00928 170 RLLQA-KERIKVGGISGAVGTHAAAYPLVEEVeerVTEFLGLKPVPISTQIEPRDRHAELLDALALLATTL-------EK 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 298 ISNDLRLMAsgpRAGLAEITLPA--RQPGSSIMPGKVNPVMPEMINQVAfqVIGNDHTISLASEAGQLE---------LN 366
Cdd:TIGR00928 242 FAVDIRLLQ---RTEHFEVEEPFgkGQVGSSAMPHKRNPIDFENVCGLA--RVIRGYASPALENAPLWHerdltdssvER 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 367 VMEPVLVFNLLQSIRIMDNAFSVFTTYcLKDIQANEEQLKEYVERSVGIITAVNPHIGYEVAARIARQ-----AIVEGKS 441
Cdd:TIGR00928 317 VILPDAFILADIMLKTTLKVVKKLVVN-PENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRElamgaAEVDEPD 395
|
330 340
....*....|....*....|....*.
gi 657210782 442 VRDLCLQYDVLT----ENELDLILDP 463
Cdd:TIGR00928 396 LLEFLLEDERITkylkEEELAELLDP 421
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
129-340 |
1.97e-13 |
|
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: 71.81 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 129 EKGMYVHLSPNShvnmsqstNDVFPTAihiatLNLL----NRLLIT-MNNMHDEFNKKAIQFDSIIKMGRTHLQDAVPIR 203
Cdd:cd01360 80 EAGRYIHFGLTS--------SDVVDTA-----LALQlreaLDIILKdLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 204 LGQEFKAYARVIKRDIKRIEQSYENLyEVNMGATAVGTGLNADPYYIKSVVEHLALISklplinaeHLVdATQ--NTDAY 281
Cdd:cd01360 147 FGLKFALWYAEFKRHLERLKEARERI-LVGKISGAVGTYANLGPEVEERVAEKLGLKP--------EPI-STQviQRDRH 216
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 657210782 282 TLVSSTLKICMVNMSKISNDLRLMAsgpRAGLAEITLP--ARQPGSSIMPGKVNPVMPEMI 340
Cdd:cd01360 217 AEYLSTLALIASTLEKIATEIRHLQ---RTEVLEVEEPfsKGQKGSSAMPHKRNPILSENI 274
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
140-354 |
3.32e-11 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 65.39 E-value: 3.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 140 SHVNMSQSTNDVFPTAIHIATLNLLNRLLITMNNMHDEFNKKAIQFDSIIKMGRTHLQDAVPIRLGQEFKAYARVIKRDI 219
Cdd:PRK06705 108 SNMHIGRSRNDMGVTMYRMSLRRYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDL 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 220 KRIEQSYENLYEVNMGATAVGTglNADPYYIKSVVEHLALISKLplinaEHLVDATQNTDAYTLVSSTLKICMVNMSKIS 299
Cdd:PRK06705 188 ERMKKTYKLLNQSPMGAAALST--TSFPIKRERVADLLGFTNVI-----ENSYDAVAGADYLLEVSSLLMVMMTNTSRWI 260
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 657210782 300 NDLRLMASGPRAGLAeITLPARQPgSSIMPGKVNPVMPEMINQVAFQVIGNDHTI 354
Cdd:PRK06705 261 HDFLLLATKEYDGIT-VARPYVQI-SSIMPQKRNPVSIEHARAITSSALGEAFTV 313
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
58-407 |
8.26e-10 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 60.89 E-value: 8.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 58 MVKKAAALANMDVKRLYEGLGEVivkaAEEVIDGKmdeqFIVDPiqggAGTSLNMNtNEvicnRAL-ELLGhekgmyvhl 136
Cdd:PLN02646 58 MLAKQGIITDEDRDSILDGLDEI----EKEIEAGK----FEWRP----DREDVHMN-NE----ARLtELIG--------- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 137 SPNSHVNMSQSTNDVFPTAIHIATLNLLNRLLITMNNMHDEFNKKAIQFDSIIKMGRTHLQDAVPIRLGQEFKAYARVIK 216
Cdd:PLN02646 112 EPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 217 RDIKRIEQSYENLYEVNMGATAV-GTGLNADPYYIKSvvehlALISKLPLINAehlVDATQNTDAYTLVSSTLKICMVNM 295
Cdd:PLN02646 192 RDAGRLVDCRPRVNFCPLGSCALaGTGLPIDRFMTAK-----DLGFTAPMRNS---IDAVSDRDFVLEFLFANSITAIHL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 296 SKISNDLRLMASGPRAGLaeITLPARQPGSSIMPGKVNPVMPEMINQVAFQVIGNDHTISLASEAGQLELN-----VMEP 370
Cdd:PLN02646 264 SRLGEEWVLWASEEFGFV--TPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTAYNrdlqeDKEP 341
|
330 340 350
....*....|....*....|....*....|....*..
gi 657210782 371 vlvfnLLQSIRIMDNAFSVfTTYCLKDIQANEEQLKE 407
Cdd:PLN02646 342 -----LFDSVDTVSDMLEV-ATEFAQNITFNPERIKK 372
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
146-349 |
1.61e-08 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 57.10 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 146 QSTNDVFPTAIHIATLNLLNRLLITMNNMHDEFNKKAIQFDSIIKMGRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQS 225
Cdd:PRK12308 107 RSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYSRLEDA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 226 YENLYEVNMGATAV-GTGLNADpyyiksvveHLALISKLPLINA-EHLVDATQNTDAYTLVSSTLKICMVNMSKISNDLR 303
Cdd:PRK12308 187 LTRLDTCPLGSGALaGTAYPID---------REALAHNLGFRRAtRNSLDSVSDRDHVMELMSVASISMLHLSRLAEDLI 257
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 657210782 304 LMASGpRAGLAEITlPARQPGSSIMPGKVNPVMPEMINQVAFQVIG 349
Cdd:PRK12308 258 FYNSG-ESGFIELA-DTVTSGSSLMPQKKNPDALELIRGKTGRVYG 301
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
192-340 |
6.46e-07 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 51.53 E-value: 6.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 192 GRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQSYENLYEVNMGATAV-GTGLNADPyyiksvvEHLA--LISKLPLINA 268
Cdd:PRK04833 153 GYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGALaGTAYEIDR-------EQLAgwLGFASATRNS 225
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 657210782 269 ehlVDATQNTDAYTLVSSTLKICMVNMSKISNDLRLMASGpRAGLAE----ITlparqPGSSIMPGKVNPVMPEMI 340
Cdd:PRK04833 226 ---LDSVSDRDHVLELLSDASISMVHLSRFAEDLIFFNSG-EAGFVElsdrVT-----SGSSLMPQKKNPDALELI 292
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
294-463 |
5.10e-06 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 47.33 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 294 NMSKISNDLRLMAsGPRAGLAEITLPARQPGSSIMPGKVNPVMPEMINQVAFQVIGNdhtISLASEA------GQLELNV 367
Cdd:PRK08937 29 SLEKFANEIRLLQ-RSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSY---LVTALENvplwheRDLSHSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 368 MEPVlvfNLLQSIRIMDNAFSVFTTyCLKDIQANEEQLKEYVERSVGII-------TAVNPHIG----YEVAARIARQAI 436
Cdd:PRK08937 105 AERI---ALPDAFLALDYILNRFVN-ILENLVVFPENIERNLDKTLGFIatervllELVEKGMGreeaHELIREKAMEAW 180
|
170 180 190
....*....|....*....|....*....|.
gi 657210782 437 VEGKSVRDLCLQ----YDVLTENELDLILDP 463
Cdd:PRK08937 181 KNQKDLRELLEAderfTKQLTKEELDELFDP 211
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
197-349 |
1.77e-05 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 47.53 E-value: 1.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 197 QDAVPIRLGQEFKAYARVIKRDIKRIEQSYENLYEVNMGATA-VGTGLNADPYYIKSVvehlaLISKLPLINAehlVDAT 275
Cdd:PRK02186 565 QPALPGSLGHYLLAVDGALARETHALFALFEHIDVCPLGAGAgGGTTFPIDPEFVARL-----LGFEQPAPNS---LDAV 636
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 657210782 276 QNTDAYTLVSSTLKICMVNMSKISNDLRLMASgprAGLAEITLPAR-QPGSSIMPGKVNPVMPEMINQVAFQVIG 349
Cdd:PRK02186 637 ASRDGVLHFLSAMAAISTVLSRLAQDLQLWTT---REFALVSLPDAlTGGSSMLPQKKNPFLLEFVKGRAGVVAG 708
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
163-363 |
4.07e-05 |
|
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: 45.77 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 163 LLNRLLITMNNMhdefNKKAIQFDSIIKMGRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQSYENLYEVNMGATaVGTG 242
Cdd:cd03302 115 ILPKLAAVIDRL----AEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGVKGT-TGTQ 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 243 ------LNADpyyiKSVVEHL-ALISKLPLINAEHLVdaTQNTdaYT-----LVSSTLKICMVNMSKISNDLRLMAsgpr 310
Cdd:cd03302 190 asfldlFEGD----HDKVEALdELVTKKAGFKKVYPV--TGQT--YSrkvdiDVLNALSSLGATAHKIATDIRLLA---- 257
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 657210782 311 aGLAEITLP--ARQPGSSIMPGKVNPVMPEMINQVAfqvignDHTISLASEAGQL 363
Cdd:cd03302 258 -NLKEVEEPfeKGQIGSSAMPYKRNPMRSERCCSLA------RHLMNLASNAAQT 305
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
192-335 |
2.77e-04 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 43.08 E-value: 2.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 192 GRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQSYENLYEVNMGAtAVGT----GLNADPyyiksVVEHLALISKLPLIN 267
Cdd:PRK09053 152 GRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGG-AAGTlaslGEQALP-----VAQALAAELQLALPA 225
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 657210782 268 AE-HlvdaTQNtDAYTLVSSTLKICMVNMSKISNDLRLMASGPRAGLAEITLPARQpGSSIMPGKVNPV 335
Cdd:PRK09053 226 LPwH----TQR-DRIAEFASALGLLAGTLGKIARDVSLLMQTEVGEVFEPAAAGKG-GSSTMPHKRNPV 288
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
167-335 |
6.25e-04 |
|
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the product of the purB gene in Escherichia coli, and related proteins. It is a member of the Lyase class I family of the Lyase_I superfamily. Members of the Lyase class I family function as homotetramers to catalyze similar beta-elimination reactions in which a Calpha-N or Calpha-O bond is cleaved with the subsequent release of fumarate as one of the products. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two non-sequential steps in the de novo purine biosynthesis pathway: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylosuccinate (SAMP) into adenosine monophosphate (AMP).
Pssm-ID: 176470 [Multi-domain] Cd Length: 425 Bit Score: 42.22 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 167 LLITMNNMHDEFNKKAIQFDSIIKMGRTHLQDAVPIRLGQEFKAYARVIKRDIKRIEQSyENLYEVNmGATavGTgLNA- 245
Cdd:cd01598 121 ILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLKQI-EILGKFN-GAV--GN-FNAh 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 657210782 246 ---DP-----YYIKSVVEHLALISKLPLINAEHLVDATQNTDAYTLVSSTLKICMVNM-SKISndLRLMASGPRAGlaEI 316
Cdd:cd01598 196 lvaYPdvdwrKFSEFFVTSLGLTWNPYTTQIEPHDYIAELFDALARINTILIDLCRDIwGYIS--LGYFKQKVKKG--EV 271
|
170
....*....|....*....
gi 657210782 317 tlparqpGSSIMPGKVNPV 335
Cdd:cd01598 272 -------GSSTMPHKVNPI 283
|
|
| |
