|
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: 879.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 8 RIEKDFLGEKEVPSAAYYGVQTLRAVENFPITGYRI--HPSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEIVD 85
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPIsdHPELIRALAMVKKAAALANRELGLLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 86 GKFHDQFIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGAYAKISPNTHVNMAQSTNDAFPTGIHIATLMMLEKLLIT 165
Cdd:COG1027 81 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLALLLLLRELLEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 166 MEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRQHLYEVNMGATAVGTGLNANPTYI 245
Cdd:COG1027 161 LERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGYI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 246 EQVVKHLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGSSIMPG 325
Cdd:COG1027 241 ELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMPG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 326 KVNPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQYVE 405
Cdd:COG1027 321 KVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYVE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 406 QSVGIITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILDPFEMTHPE 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: 874.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 3 ATKDIRIEKDFLGEKEVPSAAYYGVQTLRAVENFPITGYRIH--PSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAA 80
Cdd:PRK12273 1 MMMNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKISdyPELIRALAMVKKAAALANKELGLLDEEKADAIVAAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 81 QEIVDGKFHDQFIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGAYAKISPNTHVNMAQSTNDAFPTGIHIATLMMLE 160
Cdd:PRK12273 81 DEILAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIALLLSLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 161 KLLITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRQHLYEVNMGATAVGTGLNA 240
Cdd:PRK12273 161 KLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLNA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 241 NPTYIEQVVKHLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGS 320
Cdd:PRK12273 241 PPGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAGS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 321 SIMPGKVNPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELL 400
Cdd:PRK12273 321 SIMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEERC 400
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446484278 401 KQYVEQSVGIITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILDPFEMTHPEIAGASLL 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: 867.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 4 TKDIRIEKDFLGEKEVPSAAYYGVQTLRAVENFPITGYRIHPSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEI 83
Cdd:PRK14515 8 KNGVRIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGYKIHEGLIKAFAIVKKAAALANTDVGRLELNKGGAIAEAAQEI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 84 VDGKFHDQFIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGAYAKISPNTHVNMAQSTNDAFPTGIHIATLMMLEKLL 163
Cdd:PRK14515 88 LDGKWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIATLNALEGLL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 164 ITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRQHLYEVNMGATAVGTGLNANPT 243
Cdd:PRK14515 168 QTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNADPE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 244 YIEQVVKHLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGSSIM 323
Cdd:PRK14515 248 YIEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSIM 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 324 PGKVNPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQY 403
Cdd:PRK14515 328 PGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKEY 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 404 VEQSVGIITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILDPFEMTHPEIAGASLLK 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: 832.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 5 KDIRIEKDFLGEKEVPSAAYYGVQTLRAVENFPITGYRIHPSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEIV 84
Cdd:PRK13353 3 KNMRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYKIHPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQACDEIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 85 DGKFHDQFIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGAYAKISPNTHVNMAQSTNDAFPTGIHIATLMMLEKLLI 164
Cdd:PRK13353 83 AGKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLLEGLLA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 165 TMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRQHLYEVNMGATAVGTGLNANPTY 244
Cdd:PRK13353 163 AMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADPEY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 245 IEQVVKHLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGSSIMP 324
Cdd:PRK13353 243 IERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSIMP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 325 GKVNPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQYV 404
Cdd:PRK13353 323 GKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKEYV 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446484278 405 EQSVGIITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILDPFEMTHPEIAGASLLKNK 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: 815.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 8 RIEKDFLGEKEVPSAAYYGVQTLRAVENFPITGYRIHPSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEIVDGK 87
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISGLKIHPELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 88 FHDQFIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGAYAKISPNTHVNMAQSTNDAFPTGIHIATLMMLEKLLITME 167
Cdd:cd01357 81 LHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLALILLLRKLLDALA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 168 ELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRQHLYEVNMGATAVGTGLNANPTYIEQ 247
Cdd:cd01357 161 ALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGYIEL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 248 VVKHLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGSSIMPGKV 327
Cdd:cd01357 241 VVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMPGKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 328 NPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQYVEQS 407
Cdd:cd01357 321 NPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYVENS 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 446484278 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: 760.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 8 RIEKDFLGEKEVPSAAYYGVQTLRAVENFPITGYRIHPSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEIVDGK 87
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISGERMPPELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 88 FHDQFIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGAYAKISPNTHVNMAQSTNDAFPTGIHIATLMMLEKLLITME 167
Cdd:cd01596 81 LDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKGKYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLPALE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 168 ELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRQHLYEVNMGATAVGTGLNANPTYIEQ 247
Cdd:cd01596 161 QLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGYAEK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 248 VVKHLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGSSIMPGKV 327
Cdd:cd01596 241 VAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMPGKV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 328 NPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQYVEQS 407
Cdd:cd01596 321 NPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYVENS 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 446484278 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: 747.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 8 RIEKDFLGEKEVPSAAYYGVQTLRAVENFPITGYRIH--PSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEIVD 85
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKISdiPEFVRGMVMVKKAAALANKELGTIPESIANAIVAACDEILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 86 -GKFHDQFIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGAYAKISPNTHVNMAQSTNDAFPTGIHIATLMMLEKLLI 164
Cdd:TIGR00839 81 nGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIAVYSSLIKLVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 165 TMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRQHLYEVNMGATAVGTGLNANPTY 244
Cdd:TIGR00839 161 AINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 245 IEQVVKHLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGSSIMP 324
Cdd:TIGR00839 241 SPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 325 GKVNPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQYV 404
Cdd:TIGR00839 321 AKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGYV 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446484278 405 EQSVGIITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILDPFEMTHPEIAGASLL 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: 652.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 4 TKDIRIEKDFLGEKEVPSAAYYGVQTLRAVENFPITGYRIHPSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEI 83
Cdd:COG0114 1 MMETRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGERMPREFIRALALIKKAAARANAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 84 VDGKFHDQFIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGAYAKISPNTHVNMAQSTNDAFPTGIHIATLMMLEKLL 163
Cdd:COG0114 81 IAGKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 164 I-TMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRQHLYEVNMGATAVGTGLNANP 242
Cdd:COG0114 161 LpALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 243 TYIEQVVKHLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGSSI 322
Cdd:COG0114 241 GFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 323 MPGKVNPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQ 402
Cdd:COG0114 321 MPGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446484278 403 YVEQSVGIITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILDPFEMTH 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 446484278 4 TKDIRIEKDFLGEKEVPSAAYYGVQTLRAVENFPITGYRIHPSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEI 83
Cdd:PRK00485 1 MMETRIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALALLKKAAARVNAELGLLDAEKADAIVAAADEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 84 VDGKFHDQFIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGAYAKISPNTHVNMAQSTNDAFPTGIHIATLMMLEKLL 163
Cdd:PRK00485 81 IAGKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVERL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 164 I-TMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRQHLYEVNMGATAVGTGLNANP 242
Cdd:PRK00485 161 LpALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 243 TYIEQVVKHLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGSSI 322
Cdd:PRK00485 241 GFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 323 MPGKVNPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQ 402
Cdd:PRK00485 321 MPGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKE 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446484278 403 YVEQSVGIITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILDPFEMTHPEI 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: 602.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 8 RIEKDFLGEKEVPSAAYYGVQTLRAVENFPITGYRIHPSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEIVDGK 87
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 88 FHDQFIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGAYAKISPNTHVNMAQSTNDAFPTGIHIATLMMLEKLLI-TM 166
Cdd:cd01362 81 LDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQERLLpAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 167 EELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRQHLYEVNMGATAVGTGLNANPTYIE 246
Cdd:cd01362 161 KHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGFAE 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 247 QVVKHLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGSSIMPGK 326
Cdd:cd01362 241 KVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMPGK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 327 VNPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQYVEQ 406
Cdd:cd01362 321 VNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELLER 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446484278 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: 553.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 14 LGEKEVPSAAYYGVQTLRAVENFPITGY--RIHPSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEIVDGKFHDQ 91
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGGEreRMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAEGKLDDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 92 FIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGAYAKISPNTHVNMAQSTNDAFPTGIHIAT-LMMLEKLLITMEELH 170
Cdd:PLN00134 81 FPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAaTEIHSRLIPALKELH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 171 SAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRQHLYEVNMGATAVGTGLNANPTYIEQVVK 250
Cdd:PLN00134 161 ESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 251 HLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGSSIMPGKVNPV 330
Cdd:PLN00134 241 AVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 331 MAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQYVEQSVGI 410
Cdd:PLN00134 321 QCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLML 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446484278 411 ITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILDPFEMTHPE 465
Cdd:PLN00134 401 VTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTGPS 455
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
8-461 |
5.64e-142 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 415.47 E-value: 5.64e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 8 RIEKDFLGEKEVPSAAYYGVQTLRAVENFPITGYRIHPSLITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEIVDGK 87
Cdd:PRK12425 3 RTETDSLGPIEVPEDAYWGAQTQRSLINFAIGKERMPLAVLHALALIKKAAARVNDRNGDLPADIARLIEQAADEVLDGQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 88 FHDQFIVDPIQGGAGTSINMNTNEVIANRALERMGYEKGAYAKISPNTHVNMAQSTNDAFPTGIHIATLMML-EKLLITM 166
Cdd:PRK12425 83 HDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVhEQLLPAI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 167 EELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRQHLYEVNMGATAVGTGLNANPTYIE 246
Cdd:PRK12425 163 AELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGFAE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 247 QVVKHLRTFSGFPLVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPARQPGSSIMPGK 326
Cdd:PRK12425 243 AIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMPGK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 327 VNPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFREYCIEGITANEELLKQYVEQ 406
Cdd:PRK12425 323 VNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHLER 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446484278 407 SVGIITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILDPFEM 461
Cdd:PRK12425 403 GLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENM 457
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
15-344 |
1.79e-124 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 365.15 E-value: 1.79e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 15 GEKEVPSAAYYGVQTLRAVENFPITGYRIHpslitAMAIVKKAAALANIDTgylaKDIGHEIAEAAQEIV-DGKFHDQFI 93
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDIK-----GLAALKKAAAKANVIL----KEEAAAIIKALDEVAeEGKLDDQFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 94 VDPIQGGAGTSINMNTNEVIAnralERMGyekgayAKISPNTHVNMAQSTNDAFPTGIHIATLMML-EKLLITMEELHSA 172
Cdd:pfam00206 72 LKVWQEGSGTAVNMNLNEVIG----ELLG------QLVHPNDHVHTGQSSNDQVPTALRLALKDALsEVLLPALRQLIDA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 173 FRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRQ-HLYEVNMGATAVGTGLNANPTYIEQVVKH 251
Cdd:pfam00206 142 LKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPrLLVLPLGGGTAVGTGLNADPEFAELVAKE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 252 LRTFSGFPlVGAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPrVGLAEIQLPARQPGSSIMPGKVNPVM 331
Cdd:pfam00206 222 LGFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPDQ 299
|
330
....*....|...
gi 446484278 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 |
6.40e-117 |
|
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: 346.03 E-value: 6.40e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 48 ITAMAIVKKAAALANIDTGYLAKDIGHEIAEAAQEIVDGKFHDQFIvdpiQGGAGTSINMNTNEVIANRALErmgyekga 127
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVE----QEGSGTHDVMAVEEVLAERAGE-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 128 yakiSPNTHVNMAQSTNDAFPTGIHIATLMMLEKLLITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYS 207
Cdd:cd01334 69 ----LNGGYVHTGRSSNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 208 RVLARDIKRIKQSRQHLYEVNMGATAVGTGLNANPTYIEQVVKHLrtfsGFpLVGAEHLVDATQNTDAYTEVSAALKVCM 287
Cdd:cd01334 145 AELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAELL----GF-FGPAPNSTQAVSDRDFLVELLSALALLA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 288 MNMSKIANDLRIMASGprvGLAEIQLPAR-QPGSSIMPGKVNPVMAEVINQVAFQVIGNDHTICLASEAGQLELNVMEPV 366
Cdd:cd01334 220 VSLSKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPV 296
|
330 340 350
....*....|....*....|....*....|
gi 446484278 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 |
4.06e-55 |
|
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase, which catalyze similar beta-elimination reactions; Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively.
Pssm-ID: 176466 [Multi-domain] Cd Length: 231 Bit Score: 183.58 E-value: 4.06e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 107 MNTNEVIANRALERMGYEKGAYakispntHVNMAQSTNDAFPTGIHIATLMMLEKLLITMEELHSAFRKKAKEFDHVIKM 186
Cdd:cd01594 14 ALVEEVLAGRAGELAGGLHGSA-------LVHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 187 GRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRqhlyevnmgatavgtglnanptyieqvvkhlrtfsgfplvgaehl 266
Cdd:cd01594 87 GRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEAA--------------------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 267 vdatqntdaYTEVSAALKVCMMNMSKIANDLRIMASGPRVGLAEIQLPaRQPGSSIMPGKVNPVMAEVINQVAFQVIGND 346
Cdd:cd01594 122 ---------VAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGNL 191
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446484278 347 HTICLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVFR 386
Cdd:cd01594 192 VAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
65-460 |
5.68e-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: 112.83 E-value: 5.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 65 TGYLAKDIGHEIAEAAQEIVDGKFHDQFIVDPIQggagTSINMNtnevIANRALERMGYEKGAYakispnthVNMAQSTN 144
Cdd:TIGR00838 45 AGILTEEEAAKIIEGLNELKEEGREGPFILDPDD----EDIHMA----IERELIDRVGEDLGGK--------LHTGRSRN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 145 DAFPTGIHIATLMMLEKLLITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRQHL 224
Cdd:TIGR00838 109 DQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLRDYERLQDALKRV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 225 YEVNMGATAV-GTGLNANPTYIeqvvKHLRTFSGFplvgAEHLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASG 303
Cdd:TIGR00838 189 NVSPLGSGALaGTGFPIDREYL----AELLGFDAV----TENSLDAVSDRDFILELLFVAALIMVHLSRFAEDLILWSTG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 304 PrvgLAEIQLPAR-QPGSSIMPGKVNPVMAEVINQVAFQVIGNDHTICLASEAGQLELN-----VMEPVL-----VFNLI 372
Cdd:TIGR00838 261 E---FGFVELPDEfSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNrdlqeDKEPLFdalktVELSL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 373 QSISIMNNGFRVFREYCIEGITAN----EELLKQYVEQSVGIITAvnphigYEAASRIAREAIETGKSVRELCLEHGV-- 446
Cdd:TIGR00838 338 EMATGMLDTITVNKERMEEAASAGfsnaTELADYLVRKGVPFREA------HHIVGELVATAIERGKGLEELTLEELQkf 411
|
410
....*....|....*.
gi 446484278 447 --LTEEELDIILDPFE 460
Cdd:TIGR00838 412 spEFDEDVYEALDPES 427
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
156-458 |
6.06e-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: 106.71 E-value: 6.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 156 LMM---LEKLLITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRQHLYEVNMGAt 232
Cdd:COG0015 109 LQLreaLELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVGKIGG- 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 233 AVGTgLNANPTYIEQVVKHLrtfsgfplvgAEHL-----VDATQNT--DAYTEVSAALKVCMMNMSKIANDLRIMASgPR 305
Cdd:COG0015 188 AVGT-YAAHGEAWPEVEERV----------AEKLglkpnPVTTQIEprDRHAELFSALALIAGSLEKIARDIRLLQR-TE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 306 VGLAEIQLPARQPGSSIMPGKVNPVMAEVINQVAFQVIGN-DHticlASEAGQLELN----------VMEPVLVFNLIQS 374
Cdd:COG0015 256 VGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALaAA----LLEALASWHErdlsdssverNILPDAFLLLDGA 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 375 ISIMNNGfrvfreycIEGITANEELLKQYVEQSVGII------TAVNPH-IG----YEAASRIAREAIETGKSVRELCLE 443
Cdd:COG0015 332 LERLLKL--------LEGLVVNPERMRANLDLTGGLVlseavlMALVRRgLGreeaYELVKELARGAWEEGNDLRELLAA 403
|
330
....*....|....*....
gi 446484278 444 H----GVLTEEELDIILDP 458
Cdd:COG0015 404 DpeipAELSKEELEALFDP 422
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
56-458 |
1.20e-24 |
|
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: 105.71 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 56 KAAALANIDTGYLAKDIGHEIAEAAQEIVDGKFHDQFIVDPIQGGagtsINMNtnevIANRALERMGYEKGAyakispnt 135
Cdd:cd01359 17 IAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDED----IHMA----IERRLIERIGDVGGK-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 136 hVNMAQSTNDafptgiHIAT---LMMLEKLLITME---ELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRV 209
Cdd:cd01359 81 -LHTGRSRND------QVATdlrLYLRDALLELLElllDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 210 LARDIKRIKQSRQHLYEVNMGATA-VGTGLNANPTYieqvVKHLRTFSGfplvGAEHLVDATQNTDAYTEVSAALKVCMM 288
Cdd:cd01359 154 LERDLERLADAYKRVNVSPLGAGAlAGTTFPIDRER----TAELLGFDG----PTENSLDAVSDRDFVLEFLSAAALLMV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 289 NMSKIANDLrIMASGPRVGLaeIQLPAR-QPGSSIMPGKVNPVMAEVINQVAFQVIGNdHTICLASEAGqLELN------ 361
Cdd:cd01359 226 HLSRLAEDL-ILWSTQEFGF--VELPDAySTGSSIMPQKKNPDVLELIRGKAGRVIGA-LAGLLTTLKG-LPLAynkdlq 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 362 -VMEPVLvfnliQSISIMNNGFRVFREyCIEGITANEELLKQYVEQsvGIITAVN-----------P-HIGYEAASRIAR 428
Cdd:cd01359 301 eDKEPLF-----DAVDTLIASLRLLTG-VISTLTVNPERMREAAEA--GFSTATDladylvrekgvPfREAHHIVGRAVR 372
|
410 420 430
....*....|....*....|....*....|....
gi 446484278 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 |
6.85e-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: 6.85e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 446484278 410 IITAVNPHIGYEAASRIAREAIETGKSVRELCLEHGVLTEEELDIILDPFEM 461
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
139-460 |
9.75e-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: 97.48 E-value: 9.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 139 MAQSTNDAfptgihIATLMML---EKLLITMEELH---SAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLAR 212
Cdd:COG0165 106 TGRSRNDQ------VATDFRLylrDEILELIEALLalqEALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLLR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 213 DIKRIKQSRQHLYEVNMGATAV-GTGLNANPtyiEQVVKHLrtfsGFPLVgAEHLVDATQNTDAYTEVSAALKVCMMNMS 291
Cdd:COG0165 180 DRERLADAYKRLNVSPLGAAALaGTTFPIDR---ERTAELL----GFDGP-TENSLDAVSDRDFALEFLSAASLIMVHLS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 292 KIANDLRIMASgPRVGLaeIQLPARQ-PGSSIMPGKVNPVMAEVINQVAFQVIGNDHTIclaseagqleLNVM------- 363
Cdd:COG0165 252 RLAEELILWSS-SEFGF--VELPDAFsTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGL----------LTTMkglplay 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 364 --------EPvlVFNLIQSISIMnngFRVFREyCIEGITANEELLKQYVEQsvgiitavnphiGYEAASRIA-------- 427
Cdd:COG0165 319 nkdlqedkEP--LFDAVDTLKLC---LRLFAG-MIATLKVNRERMREAAGA------------GFSTATDLAdylvrkgv 380
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 446484278 428 --REAIE-TGKSVReLCLEHGV----LTEEELDIILDPFE 460
Cdd:COG0165 381 pfREAHEiVGRLVR-YAEEKGKdledLTLEELQAFSPLIE 419
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
140-455 |
1.37e-21 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 97.14 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 140 AQSTNDafptgiHIATLMML---EKLLITMEELHSAFR---KKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARD 213
Cdd:PRK00855 108 GRSRND------QVATDLRLylrDEIDEIAELLLELQKallDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARD 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 214 IKRIKQSRQHlyeVNM---GATA-VGTGLNANPtyiEQVVKHLrtfsGFPLVgAEHLVDATQNTDAYTEVSAALKVCMMN 289
Cdd:PRK00855 182 LERLRDARKR---VNRsplGSAAlAGTTFPIDR---ERTAELL----GFDGV-TENSLDAVSDRDFALEFLSAASLLMVH 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 290 MSKIANDLrIMASGPRVGLaeIQLPAR-QPGSSIMPGKVNPVMAEVINQVAFQVIGNDHTIclaseagqleLNVM----- 363
Cdd:PRK00855 251 LSRLAEEL-ILWSSQEFGF--VELPDAfSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGL----------LTVMkglpl 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 364 ----------EPVL--VFNLIQSISIMNngfrvfreYCIEGITANEELLKQYVEQsvGIITA-------VNPHI----GY 420
Cdd:PRK00855 318 aynrdlqedkEPLFdaVDTLKLSLEAMA--------GMLETLTVNKERMREAAGK--GFSTAtdladylVRKGVpfreAH 387
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 446484278 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 |
2.08e-17 |
|
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: 83.71 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 154 ATLMML-EKLLITMEELH---SAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRQHLYeVNM 229
Cdd:cd01595 96 ALALQLrDALDIILPDLDaliDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVL-VGG 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 230 GATAVGTGLNANPTyIEQVVKHLRTFSGFPLVGAehlvdATQNT--DAYTEVSAALKVCMMNMSKIANDLRIMAsgpRVG 307
Cdd:cd01595 175 ISGAVGTHASLGPK-GPEVEERVAEKLGLKVPPI-----TTQIEprDRIAELLSALALIAGTLEKIATDIRLLQ---RTE 245
|
170 180 190
....*....|....*....|....*....|
gi 446484278 308 LAEIQLPAR--QPGSSIMPGKVNPVMAEVI 335
Cdd:cd01595 246 IGEVEEPFEkgQVGSSTMPHKRNPIDSENI 275
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
154-458 |
1.79e-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: 81.52 E-value: 1.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 154 ATLMMLEKLLitmEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRQHLYEVNMGAtA 233
Cdd:cd01597 113 DALDLLERDL---DALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGG-A 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 234 VGTgLNANPTYIEQVVKHLrtfsgfplvgAEHLVDATQNT------DAYTEVSAALKVCMMNMSKIANDLRIMAsgpRVG 307
Cdd:cd01597 189 AGT-LASLGDQGLAVQEAL----------AAELGLGVPAIpwhtarDRIAELASFLALLTGTLGKIARDVYLLM---QTE 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 308 LAEIQLPAR--QPGSSIMPGKVNPVMAEVINQVAFQVIGNDHTIcLASEAGQLELNVMEPVLVFNLIQSISIMNNGFRVF 385
Cdd:cd01597 255 IGEVAEPFAkgRGGSSTMPHKRNPVGCELIVALARRVPGLAALL-LDAMVQEHERDAGAWHAEWIALPEIFLLASGALEQ 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 386 REYCIEGITANEELLKQYVEQSVGIITA------VNPHIG----YEAASRIAREAIETGKSVRELCLEH----GVLTEEE 451
Cdd:cd01597 334 AEFLLSGLEVNEDRMRANLDLTGGLILSeavmmaLAPKLGrqeaHDLVYEACMRAVEEGRPLREVLLEDpevaAYLSDEE 413
|
....*..
gi 446484278 452 LDIILDP 458
Cdd:cd01597 414 LDALLDP 420
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
159-460 |
2.65e-15 |
|
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: 77.77 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 159 LEKLLITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRQhLYEVNMGATAVGTGL 238
Cdd:TIGR00928 113 LEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQLERLLQAKE-RIKVGGISGAVGTHA 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 239 NANPTyIEQVVKHLRTFSGFPLVGAehlvdATQ--NTDAYTEVSAALKVCMMNMSKIANDLRIMAsGPRVGLAEIQLPAR 316
Cdd:TIGR00928 192 AAYPL-VEEVEERVTEFLGLKPVPI-----STQiePRDRHAELLDALALLATTLEKFAVDIRLLQ-RTEHFEVEEPFGKG 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 317 QPGSSIMPGKVNPVMAEVINQVAfqVIGNDHTICLASEAGQLE---------LNVMEPVLVFNLIQSISIMNNG---FRV 384
Cdd:TIGR00928 265 QVGSSAMPHKRNPIDFENVCGLA--RVIRGYASPALENAPLWHerdltdssvERVILPDAFILADIMLKTTLKVvkkLVV 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 385 FREYCIE------GITANEELLKQYVEQSVGIITAvnphigYEAASRIAREAIETGK-SVRELCLEHGVLT----EEELD 453
Cdd:TIGR00928 343 NPENILRnldltlGLIASERVLIALVERGMGREEA------YEIVRELAMGAAEVDEpDLLEFLLEDERITkylkEEELA 416
|
....*..
gi 446484278 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 |
1.67e-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: 1.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 167 EELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRQhlyEVNMGAT--AVGTGLNANPTY 244
Cdd:cd01360 115 KELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKEARE---RILVGKIsgAVGTYANLGPEV 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 245 IEQVVKHLrtfsgfplvGAEHLVDATQ--NTDAYTEVSAALKVCMMNMSKIANDLRIMaSGPRVGLAEIQLPARQPGSSI 322
Cdd:cd01360 192 EERVAEKL---------GLKPEPISTQviQRDRHAEYLSTLALIASTLEKIATEIRHL-QRTEVLEVEEPFSKGQKGSSA 261
|
170
....*....|...
gi 446484278 323 MPGKVNPVMAEVI 335
Cdd:cd01360 262 MPHKRNPILSENI 274
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
134-456 |
2.61e-13 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 71.94 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 134 NTHVnmAQSTNDafpTGIHIATLMMLEKLLITMEE---LHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVL 210
Cdd:PRK06705 109 NMHI--GRSRND---MGVTMYRMSLRRYVLRLMEHhllLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTM 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 211 ARDIKRIKQSRQHLYEVNMGATAVGTglNANPTYIEQVVKHLrtfsGFPLVgAEHLVDATQNTDAYTEVSAALKVCMMNM 290
Cdd:PRK06705 184 QRDLERMKKTYKLLNQSPMGAAALST--TSFPIKRERVADLL----GFTNV-IENSYDAVAGADYLLEVSSLLMVMMTNT 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 291 SKIANDLRIMASGPRVGLAeIQLPARQPgSSIMPGKVNPVMAEVINQVAFQVIGNDHTIClaseagQLELNV-------- 362
Cdd:PRK06705 257 SRWIHDFLLLATKEYDGIT-VARPYVQI-SSIMPQKRNPVSIEHARAITSSALGEAFTVF------QMIHNTpfgdivdt 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 363 ---MEPVL---VFNLIQSISIMNNGFRVFReyciegitANEELLKQYVEQSVGIITAV------NPHI----GYEAASRI 426
Cdd:PRK06705 329 eddLQPYLykgIEKAIRVFCIMNAVIRTMK--------VEEDTLKRRSYKHAITITDFadvltkNYGIpfrhAHHAASVI 400
|
330 340 350
....*....|....*....|....*....|.
gi 446484278 427 AREAIETGKSVRELCL-EHGVLTEEELDIIL 456
Cdd:PRK06705 401 ANMSLEQKKELHELCFkDVNIYLQEKFKIQL 431
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
140-460 |
1.94e-11 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 65.90 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 140 AQSTNDAFPTGIHIATLMMLEKLLITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQ 219
Cdd:PLN02646 120 ARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVD 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 220 SRQHLYEVNMGATAV-GTGLnanPTYIEQVVKHLrtfsGFPLVGAEHLvDATQNTDAYTEVSAALKVCMMNMSKIANDLR 298
Cdd:PLN02646 200 CRPRVNFCPLGSCALaGTGL---PIDRFMTAKDL----GFTAPMRNSI-DAVSDRDFVLEFLFANSITAIHLSRLGEEWV 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 299 IMASGPrVGLAEIQlPARQPGSSIMPGKVNPVMAEVINQVAFQVIGNDHTICLASEAGQLELN-----VMEPvlvfnLIQ 373
Cdd:PLN02646 272 LWASEE-FGFVTPS-DAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTAYNrdlqeDKEP-----LFD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 374 SISIMNNGFRVFREyCIEGITANEELLKQYVeqSVGIITA-------VNPHIGYEAASRIareaieTGKSVReLCLEHGV 446
Cdd:PLN02646 345 SVDTVSDMLEVATE-FAQNITFNPERIKKSL--PAGMLDAttladylVRKGVPFRETHHI------VGAAVA-LAESKGC 414
|
330
....*....|....*...
gi 446484278 447 ----LTEEELDIILDPFE 460
Cdd:PLN02646 415 elsdLTLEDLKSINPVFE 432
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
162-335 |
4.45e-10 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 61.54 E-value: 4.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 162 LLITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRQHLYEVNMGATAV-GTglnA 240
Cdd:PRK04833 128 LLTALRQLQSALVETAENNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGALaGT---A 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 241 NPTYIEQVVKHLrtfsGFPLVGAEHLvDATQNTDAYTEVSAALKVCMMNMSKIANDLRIMASGPRvglAEIQLPAR-QPG 319
Cdd:PRK04833 205 YEIDREQLAGWL----GFASATRNSL-DSVSDRDHVLELLSDASISMVHLSRFAEDLIFFNSGEA---GFVELSDRvTSG 276
|
170
....*....|....*.
gi 446484278 320 SSIMPGKVNPVMAEVI 335
Cdd:PRK04833 277 SSLMPQKKNPDALELI 292
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
141-344 |
1.02e-09 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 60.57 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 141 QSTNDAFPTGIHIATLMMLEKLLITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQS 220
Cdd:PRK12308 107 RSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYSRLEDA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 221 RQHLYEVNMGATAV-GTglnANPTYIEQVVKHLrtfsGFPLVGAEHLvDATQNTDAYTEVSAALKVCMMNMSKIANDLRI 299
Cdd:PRK12308 187 LTRLDTCPLGSGALaGT---AYPIDREALAHNL----GFRRATRNSL-DSVSDRDHVMELMSVASISMLHLSRLAEDLIF 258
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446484278 300 MASGpRVGLAEIQlPARQPGSSIMPGKVNPVMAEVINQVAFQVIG 344
Cdd:PRK12308 259 YNSG-ESGFIELA-DTVTSGSSLMPQKKNPDALELIRGKTGRVYG 301
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
289-458 |
1.13e-07 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 52.34 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 289 NMSKIANDLRIMAsGPRVGLAEIQLPARQPGSSIMPGKVNPVMAEVINQVAFQVIGNdhtICLASEA------GQLELNV 362
Cdd:PRK08937 29 SLEKFANEIRLLQ-RSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSY---LVTALENvplwheRDLSHSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 363 MEPVLVFNLIQSISIMNNGFRvfreYCIEGITANEELLKQYVEQSVGII-------TAVNPHIG----YEAASRIAREAI 431
Cdd:PRK08937 105 AERIALPDAFLALDYILNRFV----NILENLVVFPENIERNLDKTLGFIatervllELVEKGMGreeaHELIREKAMEAW 180
|
170 180 190
....*....|....*....|....*....|.
gi 446484278 432 ETGKSVRELCLEH----GVLTEEELDIILDP 458
Cdd:PRK08937 181 KNQKDLRELLEADerftKQLTKEELDELFDP 211
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
118-344 |
2.32e-07 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 53.31 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 118 LERMGYEKGAYakispnthVNMAQSTNDafptgIHIATLmmlekLLITMEELHSAFRK----------KAKEFDHVIKMG 187
Cdd:PRK02186 499 IERLGEDVGGV--------LQTARSRND-----INATTT-----KLHLREATSRAFDAlwrlrralvfKASANVDCALPI 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 188 RTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRQHLYEVNMGATA-VGTGLNANPtyieQVVKHLRTFSgfplVGAEHL 266
Cdd:PRK02186 561 YSQYQPALPGSLGHYLLAVDGALARETHALFALFEHIDVCPLGAGAgGGTTFPIDP----EFVARLLGFE----QPAPNS 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 267 VDATQNTDAYTEVSAALKVCMMNMSKIANDLRI--MASgprvgLAEIQLPAR-QPGSSIMPGKVNPVMAEVINQVAFQVI 343
Cdd:PRK02186 633 LDAVASRDGVLHFLSAMAAISTVLSRLAQDLQLwtTRE-----FALVSLPDAlTGGSSMLPQKKNPFLLEFVKGRAGVVA 707
|
.
gi 446484278 344 G 344
Cdd:PRK02186 708 G 708
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
135-335 |
1.89e-06 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 49.67 E-value: 1.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 135 THVNMAQSTNDAFPTGIHIATLMMLEKLLITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDI 214
Cdd:PRK05975 100 AHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRHR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 215 KRIKQSRQHLYEVNMGAtAVGTGLNANPTyIEQVVKHLRTFSGfplvgaehLVDATQ---NTDAYTEVSAALKVCMMNMS 291
Cdd:PRK05975 180 DRLEALRADVFPLQFGG-AAGTLEKLGGK-AAAVRARLAKRLG--------LEDAPQwhsQRDFIADFAHLLSLVTGSLG 249
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446484278 292 KIANDLRIMASGPRvglaEIQLpARQPGSSIMPGKVNPVMAEVI 335
Cdd:PRK05975 250 KFGQDIALMAQAGD----EISL-SGGGGSSAMPHKQNPVAAETL 288
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
175-358 |
3.93e-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: 49.24 E-value: 3.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 175 KKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRQHLYEVNMGATaVGTG------LNANPTYIEQV 248
Cdd:cd03302 128 EFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGVKGT-TGTQasfldlFEGDHDKVEAL 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 249 VKHLRTFSGFPLVgaehlVDATQNTdaYT-----EVSAALKVCMMNMSKIANDLRIMAsgprvGLAEIQLP--ARQPGSS 321
Cdd:cd03302 207 DELVTKKAGFKKV-----YPVTGQT--YSrkvdiDVLNALSSLGATAHKIATDIRLLA-----NLKEVEEPfeKGQIGSS 274
|
170 180 190
....*....|....*....|....*....|....*..
gi 446484278 322 IMPGKVNPVMAEVINQVAFQVIGndhticLASEAGQL 358
Cdd:cd03302 275 AMPYKRNPMRSERCCSLARHLMN------LASNAAQT 305
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
156-330 |
1.32e-05 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 47.43 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 156 LMMLE----KLLITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSRqhlYEVNMgA 231
Cdd:PLN02848 136 LMLKEgvnsVVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMANFAYRLSRQRKQLSEVK---IKGKF-A 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 232 TAVGtglNANptyieqvvKHLRTFS--GFPLVGAEHLVDATQNTDAYT------EVSAALKVCMMNMSKIANDL-RIMAS 302
Cdd:PLN02848 212 GAVG---NYN--------AHMSAYPevDWPAVAEEFVTSLGLTFNPYVtqiephDYMAELFNAVSRFNNILIDFdRDIWS 280
|
170 180
....*....|....*....|....*...
gi 446484278 303 GPRVGLAEIQLPARQPGSSIMPGKVNPV 330
Cdd:PLN02848 281 YISLGYFKQITKAGEVGSSTMPHKVNPI 308
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
144-330 |
4.85e-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: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 144 NDAFPTGIHIAtlmMLEKLLITMEELHSAFRKKAKEFDHVIKMGRTHLQDAVPIRLGQEFEAYSRVLARDIKRIKQSrQH 223
Cdd:cd01598 106 NLAYALMIKEA---RNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLKQI-EI 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446484278 224 LYEVNmGATavGTgLNAnptyieqvvkHLRTFSGFP-LVGAEHLVDA---------TQ--NTDAYTEVSAALK---VCMM 288
Cdd:cd01598 182 LGKFN-GAV--GN-FNA----------HLVAYPDVDwRKFSEFFVTSlgltwnpytTQiePHDYIAELFDALArinTILI 247
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446484278 289 NMSKIA---NDLRIMASGPRVGlaEIqlparqpGSSIMPGKVNPV 330
Cdd:cd01598 248 DLCRDIwgyISLGYFKQKVKKG--EV-------GSSTMPHKVNPI 283
|
|
| ADSL_C |
smart00998 |
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ... |
406-458 |
1.65e-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: 37.43 E-value: 1.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446484278 406 QSVgIITAVNPHIG----YEAASRIAREAIETGKSVRELCLEH----GVLTEEELDIILDP 458
Cdd:smart00998 7 ERV-LLALVEKGLGreeaYELVQRAAMKAWEEGKDLRELLLADpevtAYLSEEELEELFDP 66
|
|
| |
