|
Name |
Accession |
Description |
Interval |
E-value |
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
2-454 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 702.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 2 RTESDSLGSLNIPKVAYYGIHTQRALHNFPISSQ--ATHPELIRAFLEIKQAAAQTNATAGSLDRSVAKHIVSATKTLLS 79
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRpiSDHPELIRALAMVKKAAALANRELGLLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 80 SPLdMSMFPISDIQGGAGTSTNMNVNEVIANVALEQTGRERGDYKYINPNDHVNMGQSTNDTYPSSGKIALLRLLDPLFE 159
Cdd:COG1027 81 GKL-HDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLALLLLLRELLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 160 SLTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAREPLYMLNMGGSAVGSGINVSYHY 239
Cdd:COG1027 160 ALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 240 QVHIVPNLAGITKLPLTQAHDLFDATQNLDGFVALSGALKTLAMNLSKIANDLRLLSSGPRSGLLEINLPAKQAGSSIMP 319
Cdd:COG1027 240 IELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 320 GKVNPVIPEVVNQVAFEMFGFDATITTAAEAGQLELNAFEPIVFRSLFAGIEHLTSAMDTLRLNAIDGINSNKSRLAQDI 399
Cdd:COG1027 320 GKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYV 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 504786530 400 DLSVSFATAMTPIIGYQEAAKMAKESIKTGKSLRQIAQTRNCFTPDQLEHIFRIE 454
Cdd:COG1027 400 ENSIGLVTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGLLTEEELDEILDPE 454
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
2-451 |
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: 699.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 2 RTESDSLGSLNIPKVAYYGIHTQRALHNFPISSQATHPELIRAFLEIKQAAAQTNATAGSLDRSVAKHIVSATKTLLSSP 81
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISGLKIHPELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 82 LdMSMFPISDIQGGAGTSTNMNVNEVIANVALEQTGRERGDYKYINPNDHVNMGQSTNDTYPSSGKIALLRLLDPLFESL 161
Cdd:cd01357 81 L-HDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLALILLLRKLLDAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 162 TALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAREPLYMLNMGGSAVGSGINVSYHYQV 241
Cdd:cd01357 160 AALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGYIE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 242 HIVPNLAGITKLPLTQAHDLFDATQNLDGFVALSGALKTLAMNLSKIANDLRLLSSGPRSGLLEINLPAKQAGSSIMPGK 321
Cdd:cd01357 240 LVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMPGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 322 VNPVIPEVVNQVAFEMFGFDATITTAAEAGQLELNAFEPIVFRSLFAGIEHLTSAMDTLRLNAIDGINSNKSRLAQDIDL 401
Cdd:cd01357 320 VNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYVEN 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 504786530 402 SVSFATAMTPIIGYQEAAKMAKESIKTGKSLRQIAQTRNCFTPDQLEHIF 451
Cdd:cd01357 400 SIGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELDEIL 449
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
1-454 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 666.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 1 MRTESDSLGSLNIPKVAYYGIHTQRALHNFPISSQATH--PELIRAFLEIKQAAAQTNATAGSLDRSVAKHIVSATKTLL 78
Cdd:PRK12273 5 TRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKISdyPELIRALAMVKKAAALANKELGLLDEEKADAIVAACDEIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 79 SSPLdMSMFPISDIQGGAGTSTNMNVNEVIANVALEQTGRERGDYKYINPNDHVNMGQSTNDTYPSSGKIALLRLLDPLF 158
Cdd:PRK12273 85 AGKL-HDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIALLLSLRKLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 159 ESLTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAREPLYMLNMGGSAVGSGINVSYH 238
Cdd:PRK12273 164 DALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLNAPPG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 239 YQVHIVPNLAGITKLPLTQAHDLFDATQNLDGFVALSGALKTLAMNLSKIANDLRLLSSGPRSGLLEINLPAKQAGSSIM 318
Cdd:PRK12273 244 YIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAGSSIM 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 319 PGKVNPVIPEVVNQVAFEMFGFDATITTAAEAGQLELNAFEPIVFRSLFAGIEHLTSAMDTLRLNAIDGINSNKSRLAQD 398
Cdd:PRK12273 324 PGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEERCREY 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 504786530 399 IDLSVSFATAMTPIIGYQEAAKMAKESIKTGKSLRQIAQTRNCFTPDQLEHIFRIE 454
Cdd:PRK12273 404 VENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPE 459
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
2-452 |
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: 645.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 2 RTESDSLGSLNIPKVAYYGIHTQRALHNFPISSQATHPELIRAFLEIKQAAAQTNATAGSLDRSVAKHIVSATKTLLSSP 81
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISGERMPPELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 82 LDmSMFPISDIQGGAGTSTNMNVNEVIANVALEQTGRERGDYKYINPNDHVNMGQSTNDTYPSSGKIALLRLLDPLFESL 161
Cdd:cd01596 81 LD-DQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKGKYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLPAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 162 TALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAREPLYMLNMGGSAVGSGINVSYHYQV 241
Cdd:cd01596 160 EQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGYAE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 242 HIVPNLAGITKLPLTQAHDLFDATQNLDGFVALSGALKTLAMNLSKIANDLRLLSSGPRSGLLEINLPAKQAGSSIMPGK 321
Cdd:cd01596 240 KVAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMPGK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 322 VNPVIPEVVNQVAFEMFGFDATITTAAEAGQLELNAFEPIVFRSLFAGIEHLTSAMDTLRLNAIDGINSNKSRLAQDIDL 401
Cdd:cd01596 320 VNPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYVEN 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 504786530 402 SVSFATAMTPIIGYQEAAKMAKESIKTGKSLRQIAQTRNCFTPDQLEHIFR 452
Cdd:cd01596 400 SLMLVTALNPHIGYEKAAEIAKEALKEGRTLREAALELGLLTEEELDEILD 450
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
1-457 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 619.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 1 MRTESDSLGSLNIPKVAYYGIHTQRALHNFPISSQATHPELIRAFLEIKQAAAQTNATAGSLDRSVAKHIVSATKTLLSS 80
Cdd:PRK13353 5 MRIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYKIHPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQACDEILAG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 81 PLDmSMFPISDIQGGAGTSTNMNVNEVIANVALEQTGRERGDYKYINPNDHVNMGQSTNDTYPSSGKIALLRLLDPLFES 160
Cdd:PRK13353 85 KLH-DQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLLEGLLAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 161 LTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAREPLYMLNMGGSAVGSGINVSYHYQ 240
Cdd:PRK13353 164 MGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADPEYI 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 241 VHIVPNLAGITKLPLTQAHDLFDATQNLDGFVALSGALKTLAMNLSKIANDLRLLSSGPRSGLLEINLPAKQAGSSIMPG 320
Cdd:PRK13353 244 ERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSIMPG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 321 KVNPVIPEVVNQVAFEMFGFDATITTAAEAGQLELNAFEPIVFRSLFAGIEHLTSAMDTLRLNAIDGINSNKSRLAQDID 400
Cdd:PRK13353 324 KVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKEYVE 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 504786530 401 LSVSFATAMTPIIGYQEAAKMAKESIKTGKSLRQIAQTRNCFTPDQLEHIFRIEDIV 457
Cdd:PRK13353 404 KSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMT 460
|
|
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
1-457 |
5.60e-174 |
|
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: 496.47 E-value: 5.60e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 1 MRTESDSLGSLNIPKVAYYGIHTQRALHNFPISSQATHPELIRAFLEIKQAAAQTNATAGSLDRSVAKHIVSATKTLLSS 80
Cdd:COG0114 4 TRIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGERMPREFIRALALIKKAAARANAELGLLDAEKADAIVAAADEVIAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 81 PLDmSMFPISDIQGGAGTSTNMNVNEVIANVALEQTGRERGDYKYINPNDHVNMGQSTNDTYPSSGKIA-LLRLLDPLFE 159
Cdd:COG0114 84 KLD-DHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAaALALEERLLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 160 SLTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAREPLYMLNMGGSAVGSGINVSYHY 239
Cdd:COG0114 163 ALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHPGF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 240 QVHIVPNLAGITKLPLTQAHDLFDATQNLDGFVALSGALKTLAMNLSKIANDLRLLSSGPRSGLLEINLPAKQAGSSIMP 319
Cdd:COG0114 243 AERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSIMP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 320 GKVNPVIPEVVNQVAFEMFGFDATITTAAEAGQLELNAFEPIVFRSLFAGIEHLTSAMDTLRLNAIDGINSNKSRLAQDI 399
Cdd:COG0114 323 GKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEELL 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 504786530 400 DLSVSFATAMTPIIGYQEAAKMAKESIKTGKSLRQIAQTRNCFTPDQLEHIFRIEDIV 457
Cdd:COG0114 403 ERSLMLVTALNPHIGYDKAAKIAKKAHKEGRTLREAALELGLLSEEEFDRLVDPEKMT 460
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
2-457 |
1.24e-173 |
|
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: 495.89 E-value: 1.24e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 2 RTESDSLGSLNIPKVAYYGIHTQRALHNFPISSQATH--PELIRAFLEIKQAAAQTNATAGSLDRSVAKHIVSATKTLLS 79
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKISdiPEFVRGMVMVKKAAALANKELGTIPESIANAIVAACDEILN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 80 SPLDMSMFPISDIQGGAGTSTNMNVNEVIANVALEQTGRERGDYKYINPNDHVNMGQSTNDTYPSSGKIALLRLLDPLFE 159
Cdd:TIGR00839 81 NGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIAVYSSLIKLVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 160 SLTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAREPLYMLNMGGSAVGSGINVSYHY 239
Cdd:TIGR00839 161 AINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPEY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 240 QVHIVPNLAGITKLPLTQAHDLFDATQNLDGFVALSGALKTLAMNLSKIANDLRLLSSGPRSGLLEINLPAKQAGSSIMP 319
Cdd:TIGR00839 241 SPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 320 GKVNPVIPEVVNQVAFEMFGFDATITTAAEAGQLELNAFEPIVFRSLFAGIEHLTSAMDTLRLNAIDGINSNKSRLAQDI 399
Cdd:TIGR00839 321 AKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGYV 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 504786530 400 DLSVSFATAMTPIIGYQEAAKMAKESIKTGKSLRQIAQTRNCFTPDQLEHIFRIEDIV 457
Cdd:TIGR00839 401 FNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLM 458
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
1-457 |
3.20e-169 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 484.59 E-value: 3.20e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 1 MRTESDSLGSLNIPKVAYYGIHTQRALHNFPISSQATHPELIRAFLEIKQAAAQTNATAGSLDRSVAKHIVSATKTLLSS 80
Cdd:PRK00485 4 TRIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALALLKKAAARVNAELGLLDAEKADAIVAAADEVIAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 81 PLDmSMFPISDIQGGAGTSTNMNVNEVIANVALEQTGRERGDYKYINPNDHVNMGQSTNDTYPSSGKIA-LLRLLDPLFE 159
Cdd:PRK00485 84 KHD-DHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAaVLAIVERLLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 160 SLTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAREPLYMLNMGGSAVGSGINVSYHY 239
Cdd:PRK00485 163 ALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHPGF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 240 QVHIVPNLAGITKLPLTQAHDLFDATQNLDGFVALSGALKTLAMNLSKIANDLRLLSSGPRSGLLEINLPAKQAGSSIMP 319
Cdd:PRK00485 243 AERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSIMP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 320 GKVNPVIPEVVNQVAFEMFGFDATITTAAEAGQLELNAFEPIVFRSLFAGIEHLTSAMDTLRLNAIDGINSNKSRLAQDI 399
Cdd:PRK00485 323 GKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKELL 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 504786530 400 DLSVSFATAMTPIIGYQEAAKMAKESIKTGKSLRQIAQTRNCFTPDQLEHIFRIEDIV 457
Cdd:PRK00485 403 ERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMT 460
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
2-450 |
7.38e-167 |
|
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: 478.15 E-value: 7.38e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 2 RTESDSLGSLNIPKVAYYGIHTQRALHNFPISSQATHPELIRAFLEIKQAAAQTNATAGSLDRSVAKHIVSATKTLLSSP 81
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMPRELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 82 LDmSMFPISDIQGGAGTSTNMNVNEVIANVALEQTGRERGDYKYINPNDHVNMGQSTNDTYPSSGKIA-LLRLLDPLFES 160
Cdd:cd01362 81 LD-DHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAaALALQERLLPA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 161 LTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAREPLYMLNMGGSAVGSGINVSYHYQ 240
Cdd:cd01362 160 LKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGFA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 241 VHIVPNLAGITKLPLTQAHDLFDATQNLDGFVALSGALKTLAMNLSKIANDLRLLSSGPRSGLLEINLPAKQAGSSIMPG 320
Cdd:cd01362 240 EKVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMPG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 321 KVNPVIPEVVNQVAFEMFGFDATITTAAEAGQLELNAFEPIVFRSLFAGIEHLTSAMDTLRLNAIDGINSNKSRLAQDID 400
Cdd:cd01362 320 KVNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELLE 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 504786530 401 LSVSFATAMTPIIGYQEAAKMAKESIKTGKSLRQIAQTRNCFTPDQLEHI 450
Cdd:cd01362 400 RSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRL 449
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
8-457 |
5.65e-160 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 460.70 E-value: 5.65e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 8 LGSLNIPKVAYYGIHTQRALHNFPIS--SQATHPELIRAFLEIKQAAAQTNATAGSLDRSVAKHIVSATKTLLSSPLDmS 85
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGgeRERMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAEGKLD-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 86 MFPISDIQGGAGTSTNMNVNEVIANVALEQTGRERGDYKYINPNDHVNMGQSTNDTYPSSGKIAL-LRLLDPLFESLTAL 164
Cdd:PLN00134 80 HFPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAaTEIHSRLIPALKEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 165 IDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAREPLYMLNMGGSAVGSGINVSYHYQVHIV 244
Cdd:PLN00134 160 HESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 245 PNLAGITKLPLTQAHDLFDATQNLDGFVALSGALKTLAMNLSKIANDLRLLSSGPRSGLLEINLPAKQAGSSIMPGKVNP 324
Cdd:PLN00134 240 AAVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 325 VIPEVVNQVAFEMFGFDATITTAAEAGQLELNAFEPIVFRSLFAGIEHLTSAMDTLRLNAIDGINSNKSRLAQDIDLSVS 404
Cdd:PLN00134 320 TQCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLM 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 504786530 405 FATAMTPIIGYQEAAKMAKESIKTGKSLRQIAQTRNCFTPDQLEHIFRIEDIV 457
Cdd:PLN00134 400 LVTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMT 452
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
1-451 |
2.16e-156 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 452.53 E-value: 2.16e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 1 MRTESDSLGSLNIPKVAYYGIHTQRALHNFPISSQATHPELIRAFLEIKQAAAQTNATAGSLDRSVAKHIVSATKTLLSS 80
Cdd:PRK14515 11 VRIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGYKIHEGLIKAFAIVKKAAALANTDVGRLELNKGGAIAEAAQEILDG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 81 pLDMSMFPISDIQGGAGTSTNMNVNEVIANVALEQTGRERGDYKYINPNDHVNMGQSTNDTYPSSGKIALLRLLDPLFES 160
Cdd:PRK14515 91 -KWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIATLNALEGLLQT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 161 LTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAREPLYMLNMGGSAVGSGINVSYHYQ 240
Cdd:PRK14515 170 MGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNADPEYI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 241 VHIVPNLAGITKLPLTQAHDLFDATQNLDGFVALSGALKTLAMNLSKIANDLRLLSSGPRSGLLEINLPAKQAGSSIMPG 320
Cdd:PRK14515 250 EAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSIMPG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 321 KVNPVIPEVVNQVAFEMFGFDATITTAAEAGQLELNAFEPIVFRSLFAGIEHLTSAMDTLRLNAIDGINSNKSRLAQDID 400
Cdd:PRK14515 330 KVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKEYVE 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 504786530 401 LSVSFATAMTPIIGYQEAAKMAKESIKTGKSLRQIAQTRNCFTPDQLEHIF 451
Cdd:PRK14515 410 KSVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELIL 460
|
|
| fumC_II |
TIGR00979 |
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ... |
1-457 |
4.42e-139 |
|
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium tuberculosis, Streptomyces coelicolor, Pseudomonas aeruginosa) branch deeply, although within the same branch of a phylogenetic tree rooted by aspartate ammonia-lyase sequences, and score between the trusted and noise cutoffs. [Energy metabolism, TCA cycle]
Pssm-ID: 130052 [Multi-domain] Cd Length: 458 Bit Score: 407.58 E-value: 4.42e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 1 MRTESDSLGSLNIPKVAYYGIHTQRALHNFPISSQATHPELIRAFLEIKQAAAQTNATAGSLDRSVAKHIVSATKTLLSS 80
Cdd:TIGR00979 1 FRIEKDSMGEIQVPADKYWGAQTQRSLENFKIGTEKMPLELIHAFAILKKAAAIVNEDLGKLDAKKADAIVQAADEILAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 81 PLDmSMFPISDIQGGAGTSTNMNVNEVIANVALEQTGRERGDYKYINPNDHVNMGQSTNDTYPSSGKIA-LLRLLDPLFE 159
Cdd:TIGR00979 81 KLD-DHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDTFPTAMHIAaVLAIKNQLIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 160 SLTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAREPLYMLNMGGSAVGSGINVSYHY 239
Cdd:TIGR00979 160 ALENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPGF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 240 QVHIVPNLAGITKLPLTQAHDLFDATQNLDGFVALSGALKTLAMNLSKIANDLRLLSSGPRSGLLEINLPAKQAGSSIMP 319
Cdd:TIGR00979 240 DEKVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIMP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 320 GKVNPVIPEVVNQVAFEMFGFDATITTAAEAGQLELNAFEPIVFRSLFAGIEHLTSAMDTLRLNAIDGINSNKSRLAQDI 399
Cdd:TIGR00979 320 GKVNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQLL 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 504786530 400 DLSVSFATAMTPIIGYQEAAKMAKESIKTGKSLRQIAQTRNCFTPDQLEHIFRIEDIV 457
Cdd:TIGR00979 400 NNSLMLVTALNPHIGYDNAAKIAKKAHKEGITLKEAALELGLLSEEEFDEWVVPEQMV 457
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
2-457 |
1.01e-107 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 327.65 E-value: 1.01e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 2 RTESDSLGSLNIPKVAYYGIHTQRALHNFPISSQATHPELIRAFLEIKQAAAQTNATAGSLDRSVAKHIVSATKTLLSSP 81
Cdd:PRK12425 3 RTETDSLGPIEVPEDAYWGAQTQRSLINFAIGKERMPLAVLHALALIKKAAARVNDRNGDLPADIARLIEQAADEVLDGQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 82 LDmSMFPISDIQGGAGTSTNMNVNEVIANVALEQTGRERGDYKYINPNDHVNMGQSTNDTYPSSGKIALLRLL-DPLFES 160
Cdd:PRK12425 83 HD-DQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVhEQLLPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 161 LTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAREPLYMLNMGGSAVGSGINVSYHYQ 240
Cdd:PRK12425 162 IAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGFA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 241 VHIVPNLAGITKLPLTQAHDLFDATQNLDGFVALSGALKTLAMNLSKIANDLRLLSSGPRSGLLEINLPAKQAGSSIMPG 320
Cdd:PRK12425 242 EAIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMPG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 321 KVNPVIPEVVNQVAFEMFGFDATITTAAEAGQLELNAFEPIVFRSLFAGIEHLTSAMDTLRLNAIDGINSNKSRLAQDID 400
Cdd:PRK12425 322 KVNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHLE 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 504786530 401 LSVSFATAMTPIIGYQEAAKMAKESIKTGKSLRQIAQTRNCFTPDQLEHIFRIEDIV 457
Cdd:PRK12425 402 RGLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENML 458
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
42-388 |
1.31e-94 |
|
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: 289.02 E-value: 1.31e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 42 IRAFLEIKQAAAQTNATAGSLDRSVAKHIVSATKTLLSSPLDMSMFpisdiQGGAGTSTNMNVNEVIANVALEqtgrerg 121
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVE-----QEGSGTHDVMAVEEVLAERAGE------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 122 dykyiNPNDHVNMGQSTNDTYPSSGKIALLRLLDPLFESLTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAW 201
Cdd:cd01334 69 -----LNGGYVHTGRSSNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 202 LKPLRRDVERLNAAREPLYMLNMGGSAVGSGINVSYHYQVHIVPNLaGITKLPLtqahDLFDATQNLDGFVALSGALKTL 281
Cdd:cd01334 144 AAELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAELL-GFFGPAP----NSTQAVSDRDFLVELLSALALL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 282 AMNLSKIANDLRLLSSGprsGLLEINLPA-KQAGSSIMPGKVNPVIPEVVNQVAFEMFGFDATITTAAEAGQLELNAFEP 360
Cdd:cd01334 219 AVSLSKIANDLRLLSSG---EFGEVELPDaKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSP 295
|
330 340
....*....|....*....|....*...
gi 504786530 361 IVFRSLFAGIEHLTSAMDTLRlNAIDGI 388
Cdd:cd01334 296 VEREALPDSFDLLDAALRLLT-GVLEGL 322
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
9-339 |
6.75e-84 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 261.15 E-value: 6.75e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 9 GSLNIPKVAYYGIHTQRALHNFPISSqathpELIRAFLEIKQAAAQTnataGSLDRSVAKHIVSATKTLLSSPLDMSMFP 88
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGE-----EDIKGLAALKKAAAKA----NVILKEEAAAIIKALDEVAEEGKLDDQFP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 89 ISDIQGGAGTSTNMNVNEVIAnvalEQTGRergdykYINPNDHVNMGQSTNDTYPSSGKIAL-LRLLDPLFESLTALIDS 167
Cdd:pfam00206 72 LKVWQEGSGTAVNMNLNEVIG----ELLGQ------LVHPNDHVHTGQSSNDQVPTALRLALkDALSEVLLPALRQLIDA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 168 LGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAREP-LYMLNMGGSAVGSGINVSYHYQVHIVPN 246
Cdd:pfam00206 142 LKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPRlLVLPLGGGTAVGTGLNADPEFAELVAKE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 247 LAGITKLPLTQAHdLFDATQNLDGFVALSGALKTLAMNLSKIANDLRLLSSGPrSGLLEINLPAKQAGSSIMPGKVNPVI 326
Cdd:pfam00206 222 LGFFTGLPVKAPN-SFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPDQ 299
|
330
....*....|...
gi 504786530 327 PEVVNQVAFEMFG 339
Cdd:pfam00206 300 LELLTGKAGRVMG 312
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
102-381 |
5.46e-52 |
|
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: 175.49 E-value: 5.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 102 MNVNEVIANVALEQTGRERGDYkyinpndHVNMGQSTNDTYPSSGKIALLRLLDPLFESLTALIDSLGNKADEFSSTYKM 181
Cdd:cd01594 14 ALVEEVLAGRAGELAGGLHGSA-------LVHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 182 GRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAReplymlnmggsavgsginvsyhyqvhivpnlagitklpltqahdl 261
Cdd:cd01594 87 GRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEAA--------------------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 262 fdatqnldgFVALSGALKTLAMNLSKIANDLRLLSSGPRSGLLEINLPaKQAGSSIMPGKVNPVIPEVVNQVAFEMFGFD 341
Cdd:cd01594 122 ---------VAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGNL 191
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 504786530 342 ATITTAAEAGQLELNAFEPIVFRSLFAGIEHLTSAMDTLR 381
Cdd:cd01594 192 VAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
151-451 |
4.52e-26 |
|
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: 109.79 E-value: 4.52e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 151 LRLLDPLfesLTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAREPLYMLNMGGsAVG 230
Cdd:COG0015 115 LELLLPD---LDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVGKIGG-AVG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 231 sginvSYHYQVHIVPNLA-------GITKLPLTqahdlfdaTQNL--DGFVALSGALKTLAMNLSKIANDLRLLSsgpRS 301
Cdd:COG0015 191 -----TYAAHGEAWPEVEervaeklGLKPNPVT--------TQIEprDRHAELFSALALIAGSLEKIARDIRLLQ---RT 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 302 GLLEINLP--AKQAGSSIMPGKVNPVIPE-------VVNQVAfemfgfdatiTTAAEAGQLEL------NAFEPIVFRSL 366
Cdd:COG0015 255 EVGEVEEPfaKGQVGSSAMPHKRNPIDSEnieglarLARALA----------AALLEALASWHerdlsdSSVERNILPDA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 367 FAgieHLTSAMDTLrLNAIDGINSNKSRLAQDIDLS--VSFA----TAMTPI-IGYQEA----AKMAKESIKTGKSLRQI 435
Cdd:COG0015 325 FL---LLDGALERL-LKLLEGLVVNPERMRANLDLTggLVLSeavlMALVRRgLGREEAyelvKELARGAWEEGNDLREL 400
|
330 340
....*....|....*....|
gi 504786530 436 AQT----RNCFTPDQLEHIF 451
Cdd:COG0015 401 LAAdpeiPAELSKEELEALF 420
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
161-452 |
2.66e-24 |
|
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: 105.02 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 161 LTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAREPLYMLNMGGsAVGS-------GI 233
Cdd:cd01597 122 LDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGG-AAGTlaslgdqGL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 234 NVSYHYQVHI---VPNLAGITklpltqahdlfdatqNLDGFVALSGALKTLAMNLSKIANDLRLLSsgpRSGLLEINLPA 310
Cdd:cd01597 201 AVQEALAAELglgVPAIPWHT---------------ARDRIAELASFLALLTGTLGKIARDVYLLM---QTEIGEVAEPF 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 311 KQA--GSSIMPGKVNPVIPEVVNQVAFEMFGfDATITTAAEAGQLELNAFEPIVFRSLFAGIEHLTSAMDTLRLNAIDGI 388
Cdd:cd01597 263 AKGrgGSSTMPHKRNPVGCELIVALARRVPG-LAALLLDAMVQEHERDAGAWHAEWIALPEIFLLASGALEQAEFLLSGL 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 389 NSNKSRLAQDIDLS--------VSFATAmtPIIGYQEA----AKMAKESIKTGKSLRQI----AQTRNCFTPDQLEHIFR 452
Cdd:cd01597 342 EVNEDRMRANLDLTgglilseaVMMALA--PKLGRQEAhdlvYEACMRAVEEGRPLREVlledPEVAAYLSDEELDALLD 419
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
154-425 |
6.69e-24 |
|
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: 102.97 E-value: 6.69e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 154 LDPLFESLTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAREPLYMLNMGGsAVGSGI 233
Cdd:cd01595 105 LDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGGISG-AVGTHA 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 234 NVSYHyqvhiVPNLAGI--TKLPL------TQahdlfdaTQNLDGFVALSGALKTLAMNLSKIANDLRLLSsgpRSGLLE 305
Cdd:cd01595 184 SLGPK-----GPEVEERvaEKLGLkvppitTQ-------IEPRDRIAELLSALALIAGTLEKIATDIRLLQ---RTEIGE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 306 INLP--AKQAGSSIMPGKVNPVIPE-------VVNQVAfemfgfdatiTTAAEAGQLElnaFE-PI----VFRSLFAGIE 371
Cdd:cd01595 249 VEEPfeKGQVGSSTMPHKRNPIDSEnieglarLVRALA----------APALENLVQW---HErDLsdssVERNILPDAF 315
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504786530 372 HLTSAMDTLRLNAIDGINSNKSRLAQDIDLSVSF------ATAMTP-IIGYQEAAKMAKES 425
Cdd:cd01595 316 LLLDAALSRLQGLLEGLVVNPERMRRNLDLTWGLilseavMMALAKkGLGRQEAYELVKEE 376
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
151-451 |
1.30e-18 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 88.15 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 151 LRLLDPLfesLTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAREPLYMLNMGGSAvg 230
Cdd:PRK09053 124 LDLLEPD---LDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGGAA-- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 231 sGINVSYHYQVHIVPN-LAGITKLPLTQA--HdlfdaTQNlDGFVALSGALKTLAMNLSKIANDLRLLSSGPRSGLLEIN 307
Cdd:PRK09053 199 -GTLASLGEQALPVAQaLAAELQLALPALpwH-----TQR-DRIAEFASALGLLAGTLGKIARDVSLLMQTEVGEVFEPA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 308 LPAKqAGSSIMPGKVNPVipevvnqvafemfGFDATITTAAEAgqlelnafePIVFRSLFAGI--EHLTSA------MDT 379
Cdd:PRK09053 272 AAGK-GGSSTMPHKRNPV-------------GCAAVLTAATRA---------PGLVATLFAAMpqEHERALggwhaeWDT 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 380 L----RLNA---------IDGINSNKSRLAQDIDL--------SVSFATAmtPIIGYQEAAKM----AKESIKTGKSLRQ 434
Cdd:PRK09053 329 LpelaCLAAgalaqmaqiVEGLEVDAARMRANLDLthglilaeAVMLALA--DRIGRLDAHHLveqaSKRAVAEGRHLRD 406
|
330 340
....*....|....*....|.
gi 504786530 435 I----AQTRNCFTPDQLEHIF 451
Cdd:PRK09053 407 VlaedPQVSAHLSPAALDRLL 427
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
100-331 |
1.45e-18 |
|
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: 87.79 E-value: 1.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 100 TNMNVNEVIANVAlEQTGRERGdykyinpndHVNMGQSTNDTYPSSGKIALLRLLDPLFESLTALIDSLGNKADEFSSTY 179
Cdd:TIGR00928 69 TRHDVKAVVYALK-EKCGAEGE---------FIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 180 KMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAREpLYMLNMGGSAVGSGINVSYHYQ-VH-IVPNLAGITKLPLTq 257
Cdd:TIGR00928 139 MLGRTHGQHAEPTTLGKRFALWAEEMLRQLERLLQAKE-RIKVGGISGAVGTHAAAYPLVEeVEeRVTEFLGLKPVPIS- 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504786530 258 ahdlfdaTQNL--DGFVALSGALKTLAMNLSKIANDLRLLSsgpRSGLLEINLPA--KQAGSSIMPGKVNPVIPEVVN 331
Cdd:TIGR00928 217 -------TQIEprDRHAELLDALALLATTLEKFAVDIRLLQ---RTEHFEVEEPFgkGQVGSSAMPHKRNPIDFENVC 284
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
116-330 |
3.39e-18 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 86.74 E-value: 3.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 116 TGRERgdykyinpNDHVnmgqsTNDTypssgKIALLRLLDPLFESLTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLG 195
Cdd:PRK00855 107 TGRSR--------NDQV-----ATDL-----RLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFG 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 196 NSFHAWLKPLRRDVERLNAARE-----PLymlnmgGSAVgsginvsyhyqvhivpnLAGiTKLPL----TqAHDL-FDA- 264
Cdd:PRK00855 169 HHLLAYAEMLARDLERLRDARKrvnrsPL------GSAA-----------------LAG-TTFPIdrerT-AELLgFDGv 223
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504786530 265 TQN-LDG-----FV--ALSgALKTLAMNLSKIANDLRLLSSgPRSGLleINLPAKQA-GSSIMPGKVNPVIPEVV 330
Cdd:PRK00855 224 TENsLDAvsdrdFAleFLS-AASLLMVHLSRLAEELILWSS-QEFGF--VELPDAFStGSSIMPQKKNPDVAELI 294
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
115-465 |
6.34e-17 |
|
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: 82.59 E-value: 6.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 115 QTGRERgdykyinpNDHVnmgqsTNDTypssgKIALLRLLDPLFESLTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTL 194
Cdd:cd01359 82 HTGRSR--------NDQV-----ATDL-----RLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 195 GNSFHAWLKPLRRDVERLNAARE-----PLymlnmgGSAVGSGinvsyhyqvhivpnlagiTKLPL----TqAHDL-F-- 262
Cdd:cd01359 144 GHYLLAYAEMLERDLERLADAYKrvnvsPL------GAGALAG------------------TTFPIdrerT-AELLgFdg 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 263 ------DATQNLDGFVALSGALKTLAMNLSKIANDLRLLSSGPRsGLLEinLPAKQA-GSSIMPGKVNPVIPEVVNQVAF 335
Cdd:cd01359 199 ptenslDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQEF-GFVE--LPDAYStGSSIMPQKKNPDVLELIRGKAG 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 336 EMFGFDATITTAAEA-----GQLELNAFEPI--VFRSLFAGIEHLTSAMDTLRLN------AIDGINSNKSRLAQDI--D 400
Cdd:cd01359 276 RVIGALAGLLTTLKGlplayNKDLQEDKEPLfdAVDTLIASLRLLTGVISTLTVNpermreAAEAGFSTATDLADYLvrE 355
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504786530 401 LSVSFATAmtpiigYQEAAKMAKESIKTGKSLRQiaqtrncFTPDQLEHIF-RIEDIVINARTPEH 465
Cdd:cd01359 356 KGVPFREA------HHIVGRAVRLAEEKGKDLSD-------LTLAELQAISpLFEEDVREALDPEN 408
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
106-328 |
7.99e-17 |
|
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: 81.83 E-value: 7.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 106 EVIA---NVAlEQTGRERgdyKYInpndHvnMGQSTNDTYPSSGKIALLRLLDPLFESLTALIDSLGNKADEFSSTYKMG 182
Cdd:cd01360 66 DVIAfvtAIA-EYCGEAG---RYI----H--FGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 183 RTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAREPLYMLNMGGsAVGSGINVSyhYQVH-IVPNLAGITKLPLtqahdl 261
Cdd:cd01360 136 RTHGIHAEPTTFGLKFALWYAEFKRHLERLKEARERILVGKISG-AVGTYANLG--PEVEeRVAEKLGLKPEPI------ 206
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504786530 262 fdATQ--NLDGFVALSGALKTLAMNLSKIANDLRLLSsgpRSGLLEINLP--AKQAGSSIMPGKVNPVIPE 328
Cdd:cd01360 207 --STQviQRDRHAEYLSTLALIASTLEKIATEIRHLQ---RTEVLEVEEPfsKGQKGSSAMPHKRNPILSE 272
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
147-330 |
5.80e-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: 79.76 E-value: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 147 KIALLRLLDPLFESLTALIDSLGNKADEFSSTYkM-GRTQLQDAVPTTLGnsFH--AWLKPLRRDVERLNAARE-----P 218
Cdd:COG0165 119 RLYLRDEILELIEALLALQEALLDLAEEHADTI-MpGYTHLQRAQPVTFG--HHllAYAEMLLRDRERLADAYKrlnvsP 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 219 LymlnmgGSAVgsginvsyhyqvhivpnLAGiTKLPL----TqAHDL-FDA-TQN-LDG-----FVA-LSGALKTLAMNL 285
Cdd:COG0165 196 L------GAAA-----------------LAG-TTFPIdrerT-AELLgFDGpTENsLDAvsdrdFALeFLSAASLIMVHL 250
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504786530 286 SKIANDLRLLSSGPRsGLLEinLPAKQA-GSSIMPGKVNPVIPEVV 330
Cdd:COG0165 251 SRLAEELILWSSSEF-GFVE--LPDAFStGSSIMPQKKNPDVAELI 293
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
135-397 |
3.93e-15 |
|
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: 77.39 E-value: 3.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 135 GQSTNDTYPSSGKIALLRLLDPLFESLTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNA 214
Cdd:TIGR00838 104 GRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLRDYERLQD 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 215 AREPLYMLNMGGSAV-GSGINVSYHYQVHIVpNLAGITKLPLtqahdlfDATQNLDGFVALSGALKTLAMNLSKIANDLR 293
Cdd:TIGR00838 184 ALKRVNVSPLGSGALaGTGFPIDREYLAELL-GFDAVTENSL-------DAVSDRDFILELLFVAALIMVHLSRFAEDLI 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 294 LLSSGpRSGLLEinLPAKQA-GSSIMPGKVNPVIPEVVNQVAFEMFGFDATITTAAEAGQLELNafepivfRSLFAGIEH 372
Cdd:TIGR00838 256 LWSTG-EFGFVE--LPDEFSsGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYN-------RDLQEDKEP 325
|
250 260 270
....*....|....*....|....*....|.
gi 504786530 373 LTSAMDTLRLN------AIDGINSNKSRLAQ 397
Cdd:TIGR00838 326 LFDALKTVELSlematgMLDTITVNKERMEE 356
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
130-329 |
7.20e-15 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 75.86 E-value: 7.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 130 DHVNMGQSTNDTYPSSGKIALLRLLDPLFESLTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDV 209
Cdd:PRK05975 100 AHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRHR 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 210 ERLNAAREPLYMLNMGGsAVGSGINVSYHyqvhivpnlAGITKLPLTQAHDLFDATQ---NLDGFVALSGALKTLAMNLS 286
Cdd:PRK05975 180 DRLEALRADVFPLQFGG-AAGTLEKLGGK---------AAAVRARLAKRLGLEDAPQwhsQRDFIADFAHLLSLVTGSLG 249
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504786530 287 KIANDLRLLSSGPRsgllEINLpAKQAGSSIMPGKVNPVIPEV 329
Cdd:PRK05975 250 KFGQDIALMAQAGD----EISL-SGGGGSSAMPHKQNPVAAET 287
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
406-454 |
5.58e-12 |
|
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: 60.41 E-value: 5.58e-12
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 504786530 406 ATAMTPIIGYQEAAKMAKESIKTGKSLRQIAQTRNCFTPDQLEHIFRIE 454
Cdd:pfam10415 2 VTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPE 50
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
132-437 |
6.26e-12 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 67.95 E-value: 6.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 132 VNMGQSTNDTYPSSGKIALLRLLDPLFESLTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVER 211
Cdd:PRK02186 510 LQTARSRNDINATTTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHA 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 212 LNAAREPLYMLNMGGsavGSGINVSYHYQVHIVPNLAGITKLPLTQahdlFDATQNLDGFVALSGALKTLAMNLSKIAND 291
Cdd:PRK02186 590 LFALFEHIDVCPLGA---GAGGGTTFPIDPEFVARLLGFEQPAPNS----LDAVASRDGVLHFLSAMAAISTVLSRLAQD 662
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 292 LRLLSSgpRSGLLeINLPAKQAG-SSIMPGKVNPVIPEVVNQVAFEMFGFDATITTAA---------EAGQlelNAFEPI 361
Cdd:PRK02186 663 LQLWTT--REFAL-VSLPDALTGgSSMLPQKKNPFLLEFVKGRAGVVAGALASASAALgktpfsnsfEAGS---PMNGPI 736
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504786530 362 VFRSlfagiEHLTSAMDTLRLnAIDGINSNKSRLAQDIDLSVSFATAMTpiigyqeAAKMAKESIKTGKSLRQIAQ 437
Cdd:PRK02186 737 AQAC-----AAIEDAAAVLVL-LIDGLEADQARMRAHLEDGGVSATAVA-------ESLVVRRSISFRSAHTQVGQ 799
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
148-334 |
1.74e-11 |
|
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: 65.80 E-value: 1.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 148 IALLRLLDPLFESLTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAREPLYMLNMGGs 227
Cdd:cd03302 106 IQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGVKG- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 228 AVGSGINV-----SYHYQV----HIVPNLAGITK-LPLT-QAHdlfdaTQNLDGFVAlsGALKTLAMNLSKIANDLRLLs 296
Cdd:cd03302 185 TTGTQASFldlfeGDHDKVealdELVTKKAGFKKvYPVTgQTY-----SRKVDIDVL--NALSSLGATAHKIATDIRLL- 256
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504786530 297 sgprSGLLEINLP--AKQAGSSIMPGKVNPVIPEVVNQVA 334
Cdd:cd03302 257 ----ANLKEVEEPfeKGQIGSSAMPYKRNPMRSERCCSLA 292
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
131-325 |
1.38e-10 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 63.46 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 131 HVNMGQSTNDTYPSSGKIALLRLLDPLFESLTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVE 210
Cdd:PRK06705 109 NMHIGRSRNDMGVTMYRMSLRRYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLE 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 211 RLNAAREPLYMLNMGGSAVGSginVSYHYQVHIVPNLAGITKLpltqAHDLFDATQNLDGFVALSGALKTLAMNLSKIAN 290
Cdd:PRK06705 189 RMKKTYKLLNQSPMGAAALST---TSFPIKRERVADLLGFTNV----IENSYDAVAGADYLLEVSSLLMVMMTNTSRWIH 261
|
170 180 190
....*....|....*....|....*....|....*
gi 504786530 291 DLRLLSSGPRSGLLEINlPAKQAgSSIMPGKVNPV 325
Cdd:PRK06705 262 DFLLLATKEYDGITVAR-PYVQI-SSIMPQKRNPV 294
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
135-394 |
9.57e-09 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 57.49 E-value: 9.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 135 GQSTNDTYPSSGKIALLRLLDPLFESLTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNA 214
Cdd:PRK12308 106 GRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYSRLED 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 215 ArepLYMLNMggSAVGSGInvsyhyqvhivpnLAGiTKLPLTQ---AHDL---------FDATQNLDGFVALSGALKTLA 282
Cdd:PRK12308 186 A---LTRLDT--CPLGSGA-------------LAG-TAYPIDRealAHNLgfrratrnsLDSVSDRDHVMELMSVASISM 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 283 MNLSKIANDLRLLSSGpRSGLLEINlPAKQAGSSIMPGKVNPVIPEVVNQVAFEMFGFDATITTAAEAGQLELNafepiv 362
Cdd:PRK12308 247 LHLSRLAEDLIFYNSG-ESGFIELA-DTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYN------ 318
|
250 260 270
....*....|....*....|....*....|....*...
gi 504786530 363 fRSLFAGIEHLTSAMDT------LRLNAIDGINSNKSR 394
Cdd:PRK12308 319 -KDMQEDKEGLFDALDTwndcmeMAALCFDGIKVNGER 355
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
135-324 |
7.18e-07 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 51.65 E-value: 7.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 135 GQSTNDTYPSSGKIALLRLLDPLFESLTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNA 214
Cdd:PLN02646 120 ARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVD 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 215 AREPLYMLNMGGSAvgsginvsyhyqvhivpnLAGiTKLPLTQ---AHDL---------FDATQNLDGFVALSGALKTLA 282
Cdd:PLN02646 200 CRPRVNFCPLGSCA------------------LAG-TGLPIDRfmtAKDLgftapmrnsIDAVSDRDFVLEFLFANSITA 260
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504786530 283 MNLSKIANDLRLLSSGPrSGLLEINlPAKQAGSSIMPGKVNP 324
Cdd:PLN02646 261 IHLSRLGEEWVLWASEE-FGFVTPS-DAVSTGSSIMPQKKNP 300
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
161-400 |
7.22e-06 |
|
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: 48.00 E-value: 7.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 161 LTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAArepLYMLNMGGsAVGSginvsyhYQ 240
Cdd:cd01598 125 LKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLKQI---EILGKFNG-AVGN-------FN 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 241 VHIV--PNL------------AGITKLPLTqahdlfdaTQ--NLDGFVALSGALKTLAMNLSKIANDLRLLSSgprSGLL 304
Cdd:cd01598 194 AHLVayPDVdwrkfseffvtsLGLTWNPYT--------TQiePHDYIAELFDALARINTILIDLCRDIWGYIS---LGYF 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 305 EINLPAKQAGSSIMPGKVNPvipevvnqVAFEmfgfdatittAAEaGQLEL-NA-FE------PI-----------VFRS 365
Cdd:cd01598 263 KQKVKKGEVGSSTMPHKVNP--------IDFE----------NAE-GNLGLsNAlLNhlsaklPIsrlqrdltdstVLRN 323
|
250 260 270
....*....|....*....|....*....|....*
gi 504786530 366 LFAGIEHLTSAMDTLrLNAIDGINSNKSRLAQDID 400
Cdd:cd01598 324 IGVAFGHSLIAYKSL-LRGLDKLELNEARLLEDLD 357
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
157-324 |
3.92e-05 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 45.75 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 157 LFESLTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAArepLYMLNMggSAVGSGInvs 236
Cdd:PRK04833 128 LLTALRQLQSALVETAENNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDA---LKRLDV--SPLGSGA--- 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 237 yhyqvhivpnLAGiTKLPLTQ---AHDL-FD-ATQN-LDG------FVALSGALKTLAMNLSKIANDLRLLSSGpRSGLL 304
Cdd:PRK04833 200 ----------LAG-TAYEIDReqlAGWLgFAsATRNsLDSvsdrdhVLELLSDASISMVHLSRFAEDLIFFNSG-EAGFV 267
|
170 180
....*....|....*....|
gi 504786530 305 EINlPAKQAGSSIMPGKVNP 324
Cdd:PRK04833 268 ELS-DRVTSGSSLMPQKKNP 286
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
277-457 |
8.39e-05 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 43.86 E-value: 8.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 277 ALKTLAMNLSKIANDLRLLSsGPRSGLLEINLPAKQAGSSIMPGKVNPVIPEVVNQVAFEMFGFdatITTAAEAGQL--E 354
Cdd:PRK08937 22 VLALIATSLEKFANEIRLLQ-RSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSY---LVTALENVPLwhE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 355 LNAFEPIVFRSLFAGIEHLTSAMDTLRLNAIDGINSNKSRLAQDIDLSVSFATAMTPIIGY-------QEAAKM----AK 423
Cdd:PRK08937 98 RDLSHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELvekgmgrEEAHELirekAM 177
|
170 180 190
....*....|....*....|....*....|....*...
gi 504786530 424 ESIKTGKSLRQ----IAQTRNCFTPDQLEHIFRIEDIV 457
Cdd:PRK08937 178 EAWKNQKDLRElleaDERFTKQLTKEELDELFDPEAFV 215
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
157-400 |
3.03e-04 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 43.19 E-value: 3.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 157 LFESLTALIDSLGNKADEFSSTYKMGRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAArePLYMlNMGGsAVGSginvs 236
Cdd:PLN02848 146 VLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMANFAYRLSRQRKQLSEV--KIKG-KFAG-AVGN----- 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 237 yhYQVHIV-------PNLAG--ITKLPLT--------QAHD----LFDATQNLDgfvalsgalktlamnlsKIANDL-RL 294
Cdd:PLN02848 217 --YNAHMSaypevdwPAVAEefVTSLGLTfnpyvtqiEPHDymaeLFNAVSRFN-----------------NILIDFdRD 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 295 LSSGPRSGLLEINLPAKQAGSSIMPGKVNPvipevvnqVAFEMFGFDATITTAAEAGqleLNAFEPI-----------VF 363
Cdd:PLN02848 278 IWSYISLGYFKQITKAGEVGSSTMPHKVNP--------IDFENSEGNLGLANAELSH---LSMKLPIsrmqrdltdstVL 346
|
250 260 270
....*....|....*....|....*....|....*...
gi 504786530 364 RSLFAGIEH-LTSAMDTLRlnAIDGINSNKSRLAQDID 400
Cdd:PLN02848 347 RNMGVGLGHsLLAYKSTLR--GIGKLQVNEARLAEDLD 382
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
182-380 |
1.72e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 40.65 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 182 GRTQLQDAVPTTLGNSFHAWLKPLRRDVERLNAAREPLYMLNMG-GSAVGSGINVSYHyqvhIVPNLAGITKlplTQAHD 260
Cdd:PRK06389 147 GYTHFRQAMPMTVNTYINYIKSILYHHINNLDSFLMDLREMPYGyGSGYGSPSSVKFN----QMSELLGMEK---NIKNP 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504786530 261 LFDATQNLDGFVALSGALKTLAMNLSKIANDLRLLSsgpRSGLLEINlPAKQAGSSIMPGKVNPVIPEVVNQVAFEMFGF 340
Cdd:PRK06389 220 VYSSSLYIKTIENISYLISSLAVDLSRICQDIIIYY---ENGIITIP-DEFTTGSSLMPNKRNPDYLELFQGIAAESISV 295
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504786530 341 DATITTAAEAGQLELNAFEPIVFRSLFAGIEHLTSAMDTL 380
Cdd:PRK06389 296 LSFIAQSELNKTTGYHRDFQIVKDSTISFINNFERILLGL 335
|
|
| |
