|
Name |
Accession |
Description |
Interval |
E-value |
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
5-473 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 910.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 5 ASSRIEKDLLGTLEVPADAYYGIQTLRAVNNFRLSGVPLSHYPKLVVALAMVKQAAADANRQLGHLPEDKHAAISEACAR 84
Cdd:PRK12273 3 MNTRIEKDLLGEREVPADAYYGIHTLRAVENFPISGVKISDYPELIRALAMVKKAAALANKELGLLDEEKADAIVAACDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 85 LIRGDFHEQFVVDMIQGGAGTSTNMNANEVIANIALEAMGHTKGEYKYLHPNNDVNMAQSTNDAYPTAIRLGLLLGHDTL 164
Cdd:PRK12273 83 ILAGKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIALLLSLRKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 165 LASLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDRLRRlAPELLTEVNLGGTAIGTGINAD 244
Cdd:PRK12273 163 LDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYR-AAELLREVNLGATAIGTGLNAP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 245 PGYQKLAVERLAAISGQPLKPAADLIEATSDMGAFVLFSGMLKRTAVKLSKICNDLRLLSSGPRTGINEINLPPRQPGSS 324
Cdd:PRK12273 242 PGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAGSS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 325 IMPGKVNPVIPEAVNQVAFEVIGNDLALTLAAEGGQLQLNVMEPLIAYKIFDSIRLLQRAMDMLREHCITGITANVERCH 404
Cdd:PRK12273 322 IMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEERCR 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15600622 405 ELVEHSIGLVTALNPYIGYENSTRIAKTALESGRGVLELVREEKLLDEATLADILLPENMIAPRLIPLR 473
Cdd:PRK12273 402 EYVENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTHPGYKGKR 470
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
8-468 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 909.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 8 RIEKDLLGTLEVPADAYYGIQTLRAVNNFRLSGVPLSHYPKLVVALAMVKQAAADANRQLGHLPEDKHAAISEACARLIR 87
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPISGRPISDHPELIRALAMVKKAAALANRELGLLDKEKADAIVAACDEIIA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 88 GDFHEQFVVDMIQGGAGTSTNMNANEVIANIALEAMGHTKGEYKYLHPNNDVNMAQSTNDAYPTAIRLGLLLGHDTLLAS 167
Cdd:COG1027 81 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLALLLLLRELLEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 168 LDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDRLRRLApELLTEVNLGGTAIGTGINADPGY 247
Cdd:COG1027 161 LERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAA-ELLREVNLGGTAIGTGLNAPPGY 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 248 QKLAVERLAAISGQPLKPAADLIEATSDMGAFVLFSGMLKRTAVKLSKICNDLRLLSSGPRTGINEINLPPRQPGSSIMP 327
Cdd:COG1027 240 IELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 328 GKVNPVIPEAVNQVAFEVIGNDLALTLAAEGGQLQLNVMEPLIAYKIFDSIRLLQRAMDMLREHCITGITANVERCHELV 407
Cdd:COG1027 320 GKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYV 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600622 408 EHSIGLVTALNPYIGYENSTRIAKTALESGRGVLELVREEKLLDEATLADILLPENMIAPR 468
Cdd:COG1027 400 ENSIGLVTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGLLTEEELDEILDPENMTGPG 460
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
8-459 |
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: 836.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 8 RIEKDLLGTLEVPADAYYGIQTLRAVNNFRLSGVPLshYPKLVVALAMVKQAAADANRQLGHLPEDKHAAISEACARLIR 87
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPISGLKI--HPELIRALAMVKKAAALANAELGLLDEEKAEAIVKACDEIIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 88 GDFHEQFVVDMIQGGAGTSTNMNANEVIANIALEAMGHTKGEYKYLHPNNDVNMAQSTNDAYPTAIRLGLLLGHDTLLAS 167
Cdd:cd01357 79 GKLHDQFVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLALILLLRKLLDA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 168 LDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDRLRRlAPELLTEVNLGGTAIGTGINADPGY 247
Cdd:cd01357 159 LAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYK-ARERLREVNLGGTAIGTGINAPPGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 248 QKLAVERLAAISGQPLKPAADLIEATSDMGAFVLFSGMLKRTAVKLSKICNDLRLLSSGPRTGINEINLPPRQPGSSIMP 327
Cdd:cd01357 238 IELVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 328 GKVNPVIPEAVNQVAFEVIGNDLALTLAAEGGQLQLNVMEPLIAYKIFDSIRLLQRAMDMLREHCITGITANVERCHELV 407
Cdd:cd01357 318 GKVNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 15600622 408 EHSIGLVTALNPYIGYENSTRIAKTALESGRGVLELVREEKLLDEATLADIL 459
Cdd:cd01357 398 ENSIGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELDEIL 449
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
8-459 |
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: 763.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 8 RIEKDLLGTLEVPADAYYGIQTLRAVNNFRLSGVPLshYPKLVVALAMVKQAAADANRQLGHLPEDKHAAISEACARLIR 87
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPISGERM--PPELIRALALVKKAAALANAELGLLDEEKADAIVQACDEVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 88 GDFHEQFVVDMIQGGAGTSTNMNANEVIANIALEAMGHTKGEYKYLHPNNDVNMAQSTNDAYPTAIRLGLLLGHDTLLAS 167
Cdd:cd01596 79 GKLDDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKGKYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLPA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 168 LDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDRLRRLAPELLtEVNLGGTAIGTGINADPGY 247
Cdd:cd01596 159 LEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLR-ELNLGGTAVGTGLNAPPGY 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 248 QKLAVERLAAISGQPLKPAADLIEATSDMGAFVLFSGMLKRTAVKLSKICNDLRLLSSGPRTGINEINLPPRQPGSSIMP 327
Cdd:cd01596 238 AEKVAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 328 GKVNPVIPEAVNQVAFEVIGNDLALTLAAEGGQLQLNVMEPLIAYKIFDSIRLLQRAMDMLREHCITGITANVERCHELV 407
Cdd:cd01596 318 GKVNPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYV 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 15600622 408 EHSIGLVTALNPYIGYENSTRIAKTALESGRGVLELVREEKLLDEATLADIL 459
Cdd:cd01596 398 ENSLMLVTALNPHIGYEKAAEIAKEALKEGRTLREAALELGLLTEEELDEIL 449
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
8-468 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 712.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 8 RIEKDLLGTLEVPADAYYGIQTLRAVNNFRLSGVPLshYPKLVVALAMVKQAAADANRQLGHLPEDKHAAISEACARLIR 87
Cdd:PRK13353 6 RIEHDLLGEKEVPAEAYYGIQTLRAVENFPITGYKI--HPELIRAFAQVKKAAALANADLGLLPRRIAEAIVQACDEILA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 88 GDFHEQFVVDMIQGGAGTSTNMNANEVIANIALEAMGHTKGEYKYLHPNNDVNMAQSTNDAYPTAIRLGLLLGHDTLLAS 167
Cdd:PRK13353 84 GKLHDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLLEGLLAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 168 LDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDRLRRlAPELLTEVNLGGTAIGTGINADPGY 247
Cdd:PRK13353 164 MGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQ-AREHLYEVNLGGTAVGTGLNADPEY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 248 QKLAVERLAAISGQPLKPAADLIEATSDMGAFVLFSGMLKRTAVKLSKICNDLRLLSSGPRTGINEINLPPRQPGSSIMP 327
Cdd:PRK13353 243 IERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSIMP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 328 GKVNPVIPEAVNQVAFEVIGNDLALTLAAEGGQLQLNVMEPLIAYKIFDSIRLLQRAMDMLREHCITGITANVERCHELV 407
Cdd:PRK13353 323 GKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKEYV 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600622 408 EHSIGLVTALNPYIGYENSTRIAKTALESGRGVLELVREEKLLDEATLADILLPENMIAPR 468
Cdd:PRK13353 403 EKSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMTHPG 463
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
8-467 |
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: 646.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 8 RIEKDLLGTLEVPADAYYGIQTLRAVNNFRLSGVPLSHYPKLVVALAMVKQAAADANRQLGHLPEDKHAAISEACARLI- 86
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKISDIPEFVRGMVMVKKAAALANKELGTIPESIANAIVAACDEILn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 87 RGDFHEQFVVDMIQGGAGTSTNMNANEVIANIALEAMGHTKGEYKYLHPNNDVNMAQSTNDAYPTAIRLGLLLGHDTLLA 166
Cdd:TIGR00839 81 NGKCHDQFPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIAVYSSLIKLVD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 167 SLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDRLRRLApELLTEVNLGGTAIGTGINADPG 246
Cdd:TIGR00839 161 AINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTA-ELLLEVNLGATAIGTGLNTPPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 247 YQKLAVERLAAISGQPLKPAADLIEATSDMGAFVLFSGMLKRTAVKLSKICNDLRLLSSGPRTGINEINLPPRQPGSSIM 326
Cdd:TIGR00839 240 YSPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIM 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 327 PGKVNPVIPEAVNQVAFEVIGNDLALTLAAEGGQLQLNVMEPLIAYKIFDSIRLLQRAMDMLREHCITGITANVERCHEL 406
Cdd:TIGR00839 320 PAKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGY 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600622 407 VEHSIGLVTALNPYIGYENSTRIAKTALESGRGVLELVREEKLLDEATLADILLPENMIAP 467
Cdd:TIGR00839 400 VFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLMHP 460
|
|
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
8-465 |
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: 621.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 8 RIEKDLLGTLEVPADAYYGIQTLRAVNNFRLSGVPLShyPKLVVALAMVKQAAADANRQLGHLPEDKHAAISEACARLIR 87
Cdd:COG0114 5 RIEKDSMGEVEVPADAYWGAQTQRSLENFPIGGERMP--REFIRALALIKKAAARANAELGLLDAEKADAIVAAADEVIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 88 GDFHEQFVVDMIQGGAGTSTNMNANEVIANIALEAMGHTKGEYKYLHPNNDVNMAQSTNDAYPTAIRLGLLLG-HDTLLA 166
Cdd:COG0114 83 GKLDDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALAlEERLLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 167 SLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDRLRRLAPELLtEVNLGGTAIGTGINADPG 246
Cdd:COG0114 163 ALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLY-ELALGGTAVGTGLNAHPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 247 YQKLAVERLAAISGQPLKPAADLIEATSDMGAFVLFSGMLKRTAVKLSKICNDLRLLSSGPRTGINEINLPPRQPGSSIM 326
Cdd:COG0114 242 FAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSIM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 327 PGKVNPVIPEAVNQVAFEVIGNDLALTLAAEGGQLQLNVMEPLIAYKIFDSIRLLQRAMDMLREHCITGITANVERCHEL 406
Cdd:COG0114 322 PGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEEL 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600622 407 VEHSIGLVTALNPYIGYENSTRIAKTALESGRGVLELVREEKLLDEATLADILLPENMI 465
Cdd:COG0114 402 LERSLMLVTALNPHIGYDKAAKIAKKAHKEGRTLREAALELGLLSEEEFDRLVDPEKMT 460
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
8-468 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 593.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 8 RIEKDLLGTLEVPADAYYGIQTLRAVNNFRLSGVPLShyPKLVVALAMVKQAAADANRQLGHLPEDKHAAISEACARLIR 87
Cdd:PRK00485 5 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMP--RELIRALALLKKAAARVNAELGLLDAEKADAIVAAADEVIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 88 GDFHEQFVVDMIQGGAGTSTNMNANEVIANIALEAMGHTKGEYKYLHPNNDVNMAQSTNDAYPTAIRLGLLLG-HDTLLA 166
Cdd:PRK00485 83 GKHDDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAiVERLLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 167 SLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDRLRRLAPELLtEVNLGGTAIGTGINADPG 246
Cdd:PRK00485 163 ALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLY-ELALGGTAVGTGLNAHPG 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 247 YQKLAVERLAAISGQPLKPAADLIEATSDMGAFVLFSGMLKRTAVKLSKICNDLRLLSSGPRTGINEINLPPRQPGSSIM 326
Cdd:PRK00485 242 FAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSIM 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 327 PGKVNPVIPEAVNQVAFEVIGNDLALTLAAEGGQLQLNVMEPLIAYKIFDSIRLLQRAMDMLREHCITGITANVERCHEL 406
Cdd:PRK00485 322 PGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKEL 401
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15600622 407 VEHSIGLVTALNPYIGYENSTRIAKTALESGRGVLELVREEKLLDEATLADILLPENMIAPR 468
Cdd:PRK00485 402 LERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPG 463
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
14-471 |
0e+00 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 577.80 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 14 LGTLEVPADAYYGIQTLRAVNNFRLSGVPLSHYPKLVVALAMVKQAAADANRQLGHLPEDKHAAISEACARLIRGDFHEQ 93
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGGERERMPEPIVRAFGIVKKAAAKVNMEYGLLDPDIGKAIMQAADEVAEGKLDDH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 94 FVVDMIQGGAGTSTNMNANEVIANIALEAMGHTKGEYKYLHPNNDVNMAQSTNDAYPTAIRLGLLL-GHDTLLASLDSLI 172
Cdd:PLN00134 81 FPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATeIHSRLIPALKELH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 173 QAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDRLRRLAPELlTEVNLGGTAIGTGINADPGYQKLAV 252
Cdd:PLN00134 161 ESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRL-YELAQGGTAVGTGLNTKKGFDEKIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 253 ERLAAISGQPLKPAADLIEATSDMGAFVLFSGMLKRTAVKLSKICNDLRLLSSGPRTGINEINLPPRQPGSSIMPGKVNP 332
Cdd:PLN00134 240 AAVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 333 VIPEAVNQVAFEVIGNDLALTLAAEGGQLQLNVMEPLIAYKIFDSIRLLQRAMDMLREHCITGITANVERCHELVEHSIG 412
Cdd:PLN00134 320 TQCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLM 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 15600622 413 LVTALNPYIGYENSTRIAKTALESGRGVLELVREEKLLDEATLADILLPENMIAPRLIP 471
Cdd:PLN00134 400 LVTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTGPSDLP 458
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
8-464 |
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: 565.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 8 RIEKDLLGTLEVPADAYYGIQTLRAVNNFRLSGVPLShyPKLVVALAMVKQAAADANRQLGHLPEDKHAAISEACARLIR 87
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIGGERMP--RELIRALGLLKKAAAQANAELGLLDEEKADAIVQAADEVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 88 GDFHEQFVVDMIQGGAGTSTNMNANEVIANIALEAMGHTKGEYKYLHPNNDVNMAQSTNDAYPTAIRLGLLLG-HDTLLA 166
Cdd:cd01362 79 GKLDDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALAlQERLLP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 167 SLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDRLRRLAPELLtEVNLGGTAIGTGINADPG 246
Cdd:cd01362 159 ALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLY-ELALGGTAVGTGLNAHPG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 247 YQKLAVERLAAISGQPLKPAADLIEATSDMGAFVLFSGMLKRTAVKLSKICNDLRLLSSGPRTGINEINLPPRQPGSSIM 326
Cdd:cd01362 238 FAEKVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIM 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 327 PGKVNPVIPEAVNQVAFEVIGNDLALTLAAEGGQLQLNVMEPLIAYKIFDSIRLLQRAMDMLREHCITGITANVERCHEL 406
Cdd:cd01362 318 PGKVNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAEL 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 15600622 407 VEHSIGLVTALNPYIGYENSTRIAKTALESGRGVLELVREEKLLDEATLADILLPENM 464
Cdd:cd01362 398 LERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRLVDPEKM 455
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
8-467 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 520.33 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 8 RIEKDLLGTLEVPADAYYGIQTLRAVNNFRLSGVPLshYPKLVVALAMVKQAAADANRQLGHLPEDKHAAISEACARLIR 87
Cdd:PRK14515 12 RIEKDFLGEKEVPNYAYYGVQTMRAVENFPITGYKI--HEGLIKAFAIVKKAAALANTDVGRLELNKGGAIAEAAQEILD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 88 GDFHEQFVVDMIQGGAGTSTNMNANEVIANIALEAMGHTKGEYKYLHPNNDVNMAQSTNDAYPTAIRLGLLLGHDTLLAS 167
Cdd:PRK14515 90 GKWHDHFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIATLNALEGLLQT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 168 LDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDRLRRlAPELLTEVNLGGTAIGTGINADPGY 247
Cdd:PRK14515 170 MGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQ-SRQHLYEVNMGATAVGTGLNADPEY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 248 QKLAVERLAAISGQPLKPAADLIEATSDMGAFVLFSGMLKRTAVKLSKICNDLRLLSSGPRTGINEINLPPRQPGSSIMP 327
Cdd:PRK14515 249 IEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSIMP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 328 GKVNPVIPEAVNQVAFEVIGNDLALTLAAEGGQLQLNVMEPLIAYKIFDSIRLLQRAMDMLREHCITGITANVERCHELV 407
Cdd:PRK14515 329 GKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKEYV 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 408 EHSIGLVTALNPYIGYENSTRIAKTALESGRGVLELVREEKLLDEATLADILLPENMIAP 467
Cdd:PRK14515 409 EKSVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEMTHP 468
|
|
| fumC_II |
TIGR00979 |
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ... |
8-466 |
8.84e-166 |
|
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: 475.38 E-value: 8.84e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 8 RIEKDLLGTLEVPADAYYGIQTLRAVNNFRLSgvPLSHYPKLVVALAMVKQAAADANRQLGHLPEDKHAAISEACARLIR 87
Cdd:TIGR00979 2 RIEKDSMGEIQVPADKYWGAQTQRSLENFKIG--TEKMPLELIHAFAILKKAAAIVNEDLGKLDAKKADAIVQAADEILA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 88 GDFHEQFVVDMIQGGAGTSTNMNANEVIANIALEAMGHTKGEYKYLHPNNDVNMAQSTNDAYPTAIRLGLLLG-HDTLLA 166
Cdd:TIGR00979 80 GKLDDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDTFPTAMHIAAVLAiKNQLIP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 167 SLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDRLRRLAPELLtEVNLGGTAIGTGINADPG 246
Cdd:TIGR00979 160 ALENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLY-ELAIGGTAVGTGLNTHPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 247 YQKLAVERLAAISGQPLKPAADLIEATSDMGAFVLFSGMLKRTAVKLSKICNDLRLLSSGPRTGINEINLPPRQPGSSIM 326
Cdd:TIGR00979 239 FDEKVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIM 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 327 PGKVNPVIPEAVNQVAFEVIGNDLALTLAAEGGQLQLNVMEPLIAYKIFDSIRLLQRAMDMLREHCITGITANVERCHEL 406
Cdd:TIGR00979 319 PGKVNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQL 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 407 VEHSIGLVTALNPYIGYENSTRIAKTALESGRGVLELVREEKLLDEATLADILLPENMIA 466
Cdd:TIGR00979 399 LNNSLMLVTALNPHIGYDNAAKIAKKAHKEGITLKEAALELGLLSEEEFDEWVVPEQMVG 458
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
7-467 |
6.34e-122 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 363.86 E-value: 6.34e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 7 SRIEKDLLGTLEVPADAYYGIQTLRAVNNFRLSG--VPLShypkLVVALAMVKQAAADANRQLGHLPEDKHAAISEACAR 84
Cdd:PRK12425 2 SRTETDSLGPIEVPEDAYWGAQTQRSLINFAIGKerMPLA----VLHALALIKKAAARVNDRNGDLPADIARLIEQAADE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 85 LIRGDFHEQFVVDMIQGGAGTSTNMNANEVIANIALEAMGHTKGEYKYLHPNNDVNMAQSTNDAYPTAIRLGLLLG-HDT 163
Cdd:PRK12425 78 VLDGQHDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAvHEQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 164 LLASLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEdLDRLRRLAPELLTEVNLGGTAIGTGINA 243
Cdd:PRK12425 158 LLPAIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDY-AERAIRAALPAVCELAQGGTAVGTGLNA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 244 DPGYQKLAVERLAAISGQPLKPAADLIEATSDMGAFVLFSGMLKRTAVKLSKICNDLRLLSSGPRTGINEINLPPRQPGS 323
Cdd:PRK12425 237 PHGFAEAIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 324 SIMPGKVNPVIPEAVNQVAFEVIGNDLALTLAAEGGQLQLNVMEPLIAYKIFDSIRLLQRAMDMLREHCITGITANVERC 403
Cdd:PRK12425 317 SIMPGKVNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQM 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600622 404 HELVEHSIGLVTALNPYIGYENSTRIAKTALESGRGVLELVREEKLLDEATLADILLPENMIAP 467
Cdd:PRK12425 397 AAHLERGLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEA 460
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
50-399 |
1.19e-116 |
|
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; The Lyase class I family contains class II fumarase, aspartase, adenylosuccinate lyase (ASL), argininosuccinate lyase (ASAL), prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. It belongs to the Lyase_I superfamily. Proteins of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits.
Pssm-ID: 176461 [Multi-domain] Cd Length: 325 Bit Score: 345.26 E-value: 1.19e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 50 VVALAMVKQAAADANRQLGHLPEDKHAAISEACARLIRGDFHEQFvvdmIQGGAGTSTNMNANEVIANIALEAMGHtkge 129
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQV----EQEGSGTHDVMAVEEVLAERAGELNGG---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 130 ykYLHpnndvnMAQSTNDAYPTAIRLGLLLGHDTLLASLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFA 209
Cdd:cd01334 73 --YVH------TGRSSNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 210 TTLGEDLDRLRRLAPELLtEVNLGGTAIGTGINADPGYQKLAVERLAAisgqpLKPAADLIEATSDMGAFVLFSGMLKRT 289
Cdd:cd01334 145 AELERDLERLEEALKRLN-VLPLGGGAVGTGANAPPIDRERVAELLGF-----FGPAPNSTQAVSDRDFLVELLSALALL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 290 AVKLSKICNDLRLLSSGprtGINEINLPPR-QPGSSIMPGKVNPVIPEAVNQVAFEVIGNDLALTLAAEGGQLQLNVMEP 368
Cdd:cd01334 219 AVSLSKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSP 295
|
330 340 350
....*....|....*....|....*....|.
gi 15600622 369 LIAYKIFDSIRLLQRAMDMLREHCiTGITAN 399
Cdd:cd01334 296 VEREALPDSFDLLDAALRLLTGVL-EGLEVN 325
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
15-347 |
1.07e-106 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 319.31 E-value: 1.07e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 15 GTLEVPADAYYGIQTLRAVNNFRLSGVPlshypklVVALAMVKQAAADANRqlghLPEDKHAAISEACARLIR-GDFHEQ 93
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEED-------IKGLAALKKAAAKANV----ILKEEAAAIIKALDEVAEeGKLDDQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 94 FVVDMIQGGAGTSTNMNANEVIAnialEAMGhtkgeyKYLHPNNDVNMAQSTNDAYPTAIRLGLLLG-HDTLLASLDSLI 172
Cdd:pfam00206 70 FPLKVWQEGSGTAVNMNLNEVIG----ELLG------QLVHPNDHVHTGQSSNDQVPTALRLALKDAlSEVLLPALRQLI 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 173 QAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDRLRRLAPELLTEVNLGGTAIGTGINADPGYQKLAV 252
Cdd:pfam00206 140 DALKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEFAELVA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 253 ERLAAISGQPlKPAADLIEATSDMGAFVLFSGMLKRTAVKLSKICNDLRLLSSGPrTGINEINLPPRQPGSSIMPGKVNP 332
Cdd:pfam00206 220 KELGFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNP 297
|
330
....*....|....*
gi 15600622 333 VIPEAVNQVAFEVIG 347
Cdd:pfam00206 298 DQLELLTGKAGRVMG 312
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
109-389 |
1.57e-57 |
|
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: 189.74 E-value: 1.57e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 109 MNANEVIANIALEamghtkgEYKYLHPNNDVNMAQSTNDAYPTAIRLGLLLGHDTLLASLDSLIQAFAAKGVEFAGVLKM 188
Cdd:cd01594 14 ALVEEVLAGRAGE-------LAGGLHGSALVHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 189 GRTQLQDAVPMTLGQEFHAFATTLGEDLDRLRRLApelltevnlggtaigtginadpgyqklaverlaaisgqplkpaad 268
Cdd:cd01594 87 GRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEAA--------------------------------------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 269 lieatsdmgaFVLFSGMLKRTAVKLSKICNDLRLLSSGPRTGINEINLPPrQPGSSIMPGKVNPVIPEAVNQVAFEVIGN 348
Cdd:cd01594 122 ----------VAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLPG-QPGSSIMPQKVNPVAAELVRGLAGLVIGN 190
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15600622 349 DLALTLAAEGGQLQLNVMEPLIAYKIFDSIRLLQRAMDMLR 389
Cdd:cd01594 191 LVAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
131-468 |
5.05e-23 |
|
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: 101.08 E-value: 5.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 131 KYLHpnndvnMAQSTNDAYPTAIRLGLLLGHDTLLASLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFAT 210
Cdd:cd01359 79 GKLH------TGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAE 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 211 TLGEDLDRLRrlapELLTEVN---LGGTAI-GTGINADPgyqklavERLAAISG--QPLKPAADlieATSDMGAFVLFSG 284
Cdd:cd01359 153 MLERDLERLA----DAYKRVNvspLGAGALaGTTFPIDR-------ERTAELLGfdGPTENSLD---AVSDRDFVLEFLS 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 285 MLKRTAVKLSKICNDLRLLSSGPRtGIneINLPPR-QPGSSIMPGKVNPVIPEAVNQVAFEVIGNdLALTLAAEGGQlql 363
Cdd:cd01359 219 AAALLMVHLSRLAEDLILWSTQEF-GF--VELPDAySTGSSIMPQKKNPDVLELIRGKAGRVIGA-LAGLLTTLKGL--- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 364 nvmePLIAYK--------IFDSIRLLQRAMDMLREhCITGITANVERCHELVEHSIGLVTALNPYI----------GYEN 425
Cdd:cd01359 292 ----PLAYNKdlqedkepLFDAVDTLIASLRLLTG-VISTLTVNPERMREAAEAGFSTATDLADYLvrekgvpfreAHHI 366
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 15600622 426 STRIAKTALESGRGVLELVREE----KLLDEATLADILLPENMIAPR 468
Cdd:cd01359 367 VGRAVRLAEEKGKDLSDLTLAElqaiSPLFEEDVREALDPENSVERR 413
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
49-470 |
1.64e-20 |
|
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: 93.46 E-value: 1.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 49 LVVALAMVKQAAADANRQLGHLPEDKHAAISEACaRLIRGDFhEQFVVDMIQGGagtstnmnaNEVIANIA--LEAMGHT 126
Cdd:cd01597 20 RVQAMLDVEAALARAQAELGVIPKEAAAEIAAAA-DVERLDL-EALAEATARTG---------HPAIPLVKqlTAACGDA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 127 KGEYkylhpnndVNMAQSTNDAYPTAIRLGLLLGHDTLLASLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFH 206
Cdd:cd01597 89 AGEY--------VHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 207 AFATTLGEDLDRLRRLAPELLTeVNLGGtAIGTGinADPGYQKLAVERLAAisgQPLKPAADLIEATSDMGAFVLFSGML 286
Cdd:cd01597 161 VWLSELLRHRERLDELRPRVLV-VQFGG-AAGTL--ASLGDQGLAVQEALA---AELGLGVPAIPWHTARDRIAELASFL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 287 KRTAVKLSKICNDLRLLSsgpRTGINEINLP--PRQPGSSIMPGKVNPVIPEAVnQVAFEVIGNDLALTLAAEGGQLQln 364
Cdd:cd01597 234 ALLTGTLGKIARDVYLLM---QTEIGEVAEPfaKGRGGSSTMPHKRNPVGCELI-VALARRVPGLAALLLDAMVQEHE-- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 365 vmEPLIAYKIF-----DSIRLLQRAMDMLrEHCITGITANVERCHELVEHSIGLVTA------LNPYIG----YENSTRI 429
Cdd:cd01597 308 --RDAGAWHAEwialpEIFLLASGALEQA-EFLLSGLEVNEDRMRANLDLTGGLILSeavmmaLAPKLGrqeaHDLVYEA 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 15600622 430 AKTALESGRGVLELVREE----KLLDEATLADILLPENMI--APRLI 470
Cdd:cd01597 385 CMRAVEEGRPLREVLLEDpevaAYLSDEELDALLDPANYLgsAPALV 431
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
151-338 |
4.39e-20 |
|
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: 91.80 E-value: 4.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 151 TAIRLGLLLGHDTLLASLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDRLRRLAPELLTeV 230
Cdd:cd01595 95 TALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLV-G 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 231 NLGGtAIGTGINA---DPGYQKLAVERL----AAISGQ--PLKPAADLIEAtsdmgafvlfsgmLKRTAVKLSKICNDLR 301
Cdd:cd01595 174 GISG-AVGTHASLgpkGPEVEERVAEKLglkvPPITTQiePRDRIAELLSA-------------LALIAGTLEKIATDIR 239
|
170 180 190
....*....|....*....|....*....|....*....
gi 15600622 302 LLSsgpRTGINEINLP--PRQPGSSIMPGKVNPVIPEAV 338
Cdd:cd01595 240 LLQ---RTEIGEVEEPfeKGQVGSSTMPHKRNPIDSENI 275
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
413-464 |
7.69e-20 |
|
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: 82.75 E-value: 7.69e-20
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 15600622 413 LVTALNPYIGYENSTRIAKTALESGRGVLELVREEKLLDEATLADILLPENM 464
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
151-470 |
1.51e-18 |
|
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: 87.45 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 151 TAIRLGLLLGHDTLLASLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDRLRRLAPELLTeV 230
Cdd:COG0015 105 TALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLV-G 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 231 NLGGtAIGTG---INADPGYQKLAVERL----AAISGQplkpaadlIEATSDMGAFVLFsgmLKRTAVKLSKICNDLRLL 303
Cdd:COG0015 184 KIGG-AVGTYaahGEAWPEVEERVAEKLglkpNPVTTQ--------IEPRDRHAELFSA---LALIAGSLEKIARDIRLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 304 SsgpRTGINEINLP--PRQPGSSIMPGKVNPVIPEAVNQVAFEVIGNdlaLTLAAEGGQLQL------NVMEPLIaykIF 375
Cdd:COG0015 252 Q---RTEVGEVEEPfaKGQVGSSAMPHKRNPIDSENIEGLARLARAL---AAALLEALASWHerdlsdSSVERNI---LP 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 376 DSIRL----LQRAMDMLRehcitGITANVERCHELVEHSIGLV------TALNPY-IGYENS----TRIAKTALESGRGV 440
Cdd:COG0015 323 DAFLLldgaLERLLKLLE-----GLVVNPERMRANLDLTGGLVlseavlMALVRRgLGREEAyelvKELARGAWEEGNDL 397
|
330 340 350
....*....|....*....|....*....|....*.
gi 15600622 441 LELVREE----KLLDEATLADILLPENMI--APRLI 470
Cdd:COG0015 398 RELLAADpeipAELSKEELEALFDPANYLgaADEIV 433
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
48-447 |
5.92e-16 |
|
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: 79.71 E-value: 5.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 48 KLVVALAMVKQAAADANRQLGHLPEDKHAAIseacarlirgdfhEQFVVDMIQGGAGtstnmnanevianialeamghtk 127
Cdd:TIGR00838 55 KIIEGLNELKEEGREGPFILDPDDEDIHMAI-------------ERELIDRVGEDLG----------------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 128 geyKYLHpnndvnMAQSTNDAYPTAIRLGLLLGHDTLLASL----DSLIQAfAAKGVEFagvLKMGRTQLQDAVPMTLGQ 203
Cdd:TIGR00838 99 ---GKLH------TGRSRNDQVATDLRLYLRDHVLELAEALldlqDALIEL-AEKHVET---LMPGYTHLQRAQPITLAH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 204 EFHAFATTLGEDLDRLRrlapELLTEVN---LGGTAI-GTGINADPgyqklavERLAAISGqplkpAADLIE----ATSD 275
Cdd:TIGR00838 166 HLLAYAEMLLRDYERLQ----DALKRVNvspLGSGALaGTGFPIDR-------EYLAELLG-----FDAVTEnsldAVSD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 276 MGAFVLFSGMLKRTAVKLSKICNDLRLLSSGPrtgINEINLPPR-QPGSSIMPGKVNPVIPEAVNQVAFEVIGNDLALTL 354
Cdd:TIGR00838 230 RDFILELLFVAALIMVHLSRFAEDLILWSTGE---FGFVELPDEfSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 355 AAEGGQLQLN-----VMEPLiaykiFDSIRLLQRAMDMLReHCITGITANVERCHELVEHSIGLVTALNPYI-------- 421
Cdd:TIGR00838 307 TLKALPLAYNrdlqeDKEPL-----FDALKTVELSLEMAT-GMLDTITVNKERMEEAASAGFSNATELADYLvrkgvpfr 380
|
410 420
....*....|....*....|....*..
gi 15600622 422 -GYENSTRIAKTALESGRGVLELVREE 447
Cdd:TIGR00838 381 eAHHIVGELVATAIERGKGLEELTLEE 407
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
113-336 |
7.56e-16 |
|
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: 79.13 E-value: 7.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 113 EVIA---NIAlEAMGHTKgeyKYLHpnndvnMAQSTNDAYPTAIRLGLLLGHDTLLASLDSLIQAFAAKGVEFAGVLKMG 189
Cdd:cd01360 66 DVIAfvtAIA-EYCGEAG---RYIH------FGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 190 RTQLQDAVPMTLGQEFHAFATTLGEDLDRLRRLAPELLTeVNLGGtAIGTGINADPGYQKLAVERLAaisgqpLKPAadl 269
Cdd:cd01360 136 RTHGIHAEPTTFGLKFALWYAEFKRHLERLKEARERILV-GKISG-AVGTYANLGPEVEERVAEKLG------LKPE--- 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15600622 270 iEATS-----DMGAFVLFSgmLKRTAVKLSKICNDLRLLSsgpRTGINEINLP--PRQPGSSIMPGKVNPVIPE 336
Cdd:cd01360 205 -PISTqviqrDRHAEYLST--LALIASTLEKIATEIRHLQ---RTEVLEVEEPfsKGQKGSSAMPHKRNPILSE 272
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
131-468 |
2.66e-15 |
|
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: 77.83 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 131 KYLHpnndvnMAQSTNDAYPTAIRLGLLLGHDTLLASLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFAT 210
Cdd:COG0165 102 GKLH------TGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAE 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 211 TLGEDLDRLRrlapELLTEVN---LGGTAI-GTGINADPgyqklavERLAAISGQPlKPAADLIEATSDMgAFVL-FSGM 285
Cdd:COG0165 176 MLLRDRERLA----DAYKRLNvspLGAAALaGTTFPIDR-------ERTAELLGFD-GPTENSLDAVSDR-DFALeFLSA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 286 LKRTAVKLSKICNDLRLLSSGPRtgiNEINLPPRQ-PGSSIMPGKVNPVIPEAVNQVAFEVIGNDLALtlaaeggqlqLN 364
Cdd:COG0165 243 ASLIMVHLSRLAEELILWSSSEF---GFVELPDAFsTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGL----------LT 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 365 VME--PLiAY---------KIFDSIRLLQRAMDMLREhCITGITANVERCHELVEHSIGLVTALNPYI---------GYE 424
Cdd:COG0165 310 TMKglPL-AYnkdlqedkePLFDAVDTLKLCLRLFAG-MIATLKVNRERMREAAGAGFSTATDLADYLvrkgvpfreAHE 387
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15600622 425 NSTRIAKTALESGRGV----LELVREEKLLDEATLADILLPENMIAPR 468
Cdd:COG0165 388 IVGRLVRYAEEKGKDLedltLEELQAFSPLIEEDVYEALDPEGSVAAR 435
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
131-468 |
3.74e-15 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 77.50 E-value: 3.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 131 KYLHpnndvnMAQSTNDAYPTAIRLGLLLGHDTLLASLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFAT 210
Cdd:PRK00855 103 GKLH------TGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAE 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 211 TLGEDLDRLRrlapELLTEVN---LGGTAI-GTGINADPgyqklavERLAAISGQPlKPAADLIEATSDMgAFVL-FSGM 285
Cdd:PRK00855 177 MLARDLERLR----DARKRVNrspLGSAALaGTTFPIDR-------ERTAELLGFD-GVTENSLDAVSDR-DFALeFLSA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 286 LKRTAVKLSKICNDLRLLSSgPRTGIneINLPPR-QPGSSIMPGKVNPVIPEAVNQVAFEVIGNDLALtlaaeggqlqLN 364
Cdd:PRK00855 244 ASLLMVHLSRLAEELILWSS-QEFGF--VELPDAfSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGL----------LT 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 365 VME--PLiAY-------K--IFDSIRLLQRAMDMLREhCITGITANVERCHELVEHSIGLVTALNPYI---------GYE 424
Cdd:PRK00855 311 VMKglPL-AYnrdlqedKepLFDAVDTLKLSLEAMAG-MLETLTVNKERMREAAGKGFSTATDLADYLvrkgvpfreAHE 388
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 15600622 425 NSTRIAKTALESGRGVLELVREE-KLLDEATLADI---LLPENMIAPR 468
Cdd:PRK00855 389 IVGKAVREAEERGVDLADLSLEElQAFSPLITEDVyevLTPEGSVAAR 436
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
139-339 |
5.12e-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: 77.00 E-value: 5.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 139 VNMAQSTNDAYPTAIRLGLLLGHDTLLASLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDR 218
Cdd:TIGR00928 91 IHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQLER 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 219 LRRLAPELLtevnLGGT--AIGTGINADPGYQKLAvERLAAISGQPLKPAADLIEATSDMGAFVLFsgmLKRTAVKLSKI 296
Cdd:TIGR00928 171 LLQAKERIK----VGGIsgAVGTHAAAYPLVEEVE-ERVTEFLGLKPVPISTQIEPRDRHAELLDA---LALLATTLEKF 242
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15600622 297 CNDLRLLSsgpRTGINEINLP--PRQPGSSIMPGKVNPVIPEAVN 339
Cdd:TIGR00928 243 AVDIRLLQ---RTEHFEVEEPfgKGQVGSSAMPHKRNPIDFENVC 284
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
56-333 |
1.37e-12 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 69.27 E-value: 1.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 56 VKQAAADANRQLGHLPEDKHAAISEACARlirgdfhEQFVVDMIQGGAGTSTNMNANEVIANIALEAMGHTKGEyKYLHp 135
Cdd:PRK09053 33 FEAALARAEAACGVIPAAAVAPIEAACDA-------ERLDLDALAQAAALAGNLAIPLVKQLTAQVAARDAEAA-RYVH- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 136 nndvnMAQSTNDAYPTAIRLGLLLGHDTLLASLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGED 215
Cdd:PRK09053 104 -----WGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRH 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 216 LDRLRRLAPELLTeVNLGGTAigtGINADPGYQKLAV-ERLAAISGQPLkPAADLIEATSDMGAFVLFSGMLKRTavkLS 294
Cdd:PRK09053 179 RQRLAALRPRALV-LQFGGAA---GTLASLGEQALPVaQALAAELQLAL-PALPWHTQRDRIAEFASALGLLAGT---LG 250
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 15600622 295 KICNDLRLLSsgpRTGINEINLP--PRQPGSSIMPGKVNPV 333
Cdd:PRK09053 251 KIARDVSLLM---QTEVGEVFEPaaAGKGGSSTMPHKRNPV 288
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
142-402 |
4.40e-11 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 64.75 E-value: 4.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 142 AQSTNDAYPTAIRLGLLLGHDTLLASLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDRLRR 221
Cdd:PLN02646 120 ARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVD 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 222 LAPELLTeVNLGGTAI-GTGINADpgYQKLAVErlAAISGqplkPAADLIEATSDMGAFVLFSGMLKRTAVKLSKICNDL 300
Cdd:PLN02646 200 CRPRVNF-CPLGSCALaGTGLPID--RFMTAKD--LGFTA----PMRNSIDAVSDRDFVLEFLFANSITAIHLSRLGEEW 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 301 RLLSSGPRTGIneinlpprQP------GSSIMPGKVNPVIPEAVNQVAFEVIGNDLALTLAAEGGQLQLN-----VMEPL 369
Cdd:PLN02646 271 VLWASEEFGFV--------TPsdavstGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTAYNrdlqeDKEPL 342
|
250 260 270
....*....|....*....|....*....|....*
gi 15600622 370 iaykiFDSIRLLqraMDMLR--EHCITGITANVER 402
Cdd:PLN02646 343 -----FDSVDTV---SDMLEvaTEFAQNITFNPER 369
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
59-336 |
2.91e-08 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 55.45 E-value: 2.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 59 AAADANRQLGHLPEDKHAAISEACArlirgdfheQFVVDMIQGGAGTSTN-MNANEVIANIALeAMGHTKGEYkylhpnn 137
Cdd:PRK05975 39 ALAEAEAEHGIIPAEAAERIAAACE---------TFEPDLAALRHATARDgVVVPALVRQLRA-AVGEEAAAH------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 138 dVNMAQSTNDAYPTAIRLGLLLGHDTLLASLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLD 217
Cdd:PRK05975 102 -VHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRHRD 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 218 RLRRLAPELLTeVNLGGtAIGTGINADPGYQKLAvERLAAISGQPLKPaadliEATSDMGAFVLFSGMLKRTAVKLSKIC 297
Cdd:PRK05975 181 RLEALRADVFP-LQFGG-AAGTLEKLGGKAAAVR-ARLAKRLGLEDAP-----QWHSQRDFIADFAHLLSLVTGSLGKFG 252
|
250 260 270
....*....|....*....|....*....|....*....
gi 15600622 298 NDLRLLSSGPRtginEINLPPrQPGSSIMPGKVNPVIPE 336
Cdd:PRK05975 253 QDIALMAQAGD----EISLSG-GGGSSAMPHKQNPVAAE 286
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
152-347 |
3.88e-08 |
|
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: 55.40 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 152 AIRLGLLLghdtLLASLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDRLRRLapelLTEVN 231
Cdd:cd03302 107 QIRDALDL----ILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERL----RDDLR 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 232 LGGTAIGTGINAD-----PGY------------QKLAVERLAAISGQ--PLKPAADLIEATSDMGAFVlfsgmlkrtavk 292
Cdd:cd03302 179 FRGVKGTTGTQASfldlfEGDhdkvealdelvtKKAGFKKVYPVTGQtySRKVDIDVLNALSSLGATA------------ 246
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600622 293 lSKICNDLRLLSsgprtGINEINLP--PRQPGSSIMPGKVNPVIPEAVNQVAFEVIG 347
Cdd:cd03302 247 -HKIATDIRLLA-----NLKEVEEPfeKGQIGSSAMPYKRNPMRSERCCSLARHLMN 297
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
143-430 |
2.00e-07 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 53.63 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 143 QSTNDAYPTAIRLGLLLGHDTLLASLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDRLRRL 222
Cdd:PRK12308 107 RSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYSRLEDA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 223 APELLTevnlggTAIGTGINADPGYqklAVERLAAISGQPLKPAA-DLIEATSDMGAFVLFSGMLKRTAVKLSKICNDLR 301
Cdd:PRK12308 187 LTRLDT------CPLGSGALAGTAY---PIDREALAHNLGFRRATrNSLDSVSDRDHVMELMSVASISMLHLSRLAEDLI 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 302 LLSSGPRTGINEINLPprQPGSSIMPGKVNPVIPEAVNQVAFEVIGNDLALTLAAEGGQLQLNVMEPLIAYKIFDSIRLL 381
Cdd:PRK12308 258 FYNSGESGFIELADTV--TSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKDMQEDKEGLFDALDTW 335
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 15600622 382 QRAMDMLrEHCITGITANVERCHELVEHsiglvtalnpyiGYENSTRIA 430
Cdd:PRK12308 336 NDCMEMA-ALCFDGIKVNGERTLEAAKQ------------GYANATELA 371
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
139-402 |
2.16e-07 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 53.70 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 139 VNMAQSTNDAYPTAIRLGLLLGHDTLLASLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDR 218
Cdd:PRK02186 510 LQTARSRNDINATTTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHA 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 219 LRRLAPELLTEVNLGGTAIGTGINADPGYqklaVERLAAISgqplKPAADLIEATSDMGAFVLFSGMLKRTAVKLSKICN 298
Cdd:PRK02186 590 LFALFEHIDVCPLGAGAGGGTTFPIDPEF----VARLLGFE----QPAPNSLDAVASRDGVLHFLSAMAAISTVLSRLAQ 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 299 DLRLLSSGPrtgINEINLPPR-QPGSSIMPGKVNPVIPEAVNQVAFEVIGNdLALTLAAEGGQLQLNVME---PLIAyKI 374
Cdd:PRK02186 662 DLQLWTTRE---FALVSLPDAlTGGSSMLPQKKNPFLLEFVKGRAGVVAGA-LASASAALGKTPFSNSFEagsPMNG-PI 736
|
250 260
....*....|....*....|....*...
gi 15600622 375 FDSIRLLQRAMDMLReHCITGITANVER 402
Cdd:PRK02186 737 AQACAAIEDAAAVLV-LLIDGLEADQAR 763
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
137-347 |
7.34e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 48.44 E-value: 7.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 137 NDVNMAQSTNDAYPTAIRLGL------LLGHDTLLAslDSLIQaFAAKGVEfagVLKMGRTQLQDAVPMTLGQEFHAFAT 210
Cdd:PRK06705 108 SNMHIGRSRNDMGVTMYRMSLrryvlrLMEHHLLLQ--ESILQ-LAADHKE---TIMPAYTHTQPAQPTTFGHYTLAIYD 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 211 TLGEDLDRLRRlAPELLTEVNLGGTAIGTgiNADPgyqkLAVERLAAISGqplkpAADLIEATSDM--GAFVLF--SGML 286
Cdd:PRK06705 182 TMQRDLERMKK-TYKLLNQSPMGAAALST--TSFP----IKRERVADLLG-----FTNVIENSYDAvaGADYLLevSSLL 249
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15600622 287 KRTAVKLSKICNDLRLLSSGPRTGINEINlpPRQPGSSIMPGKVNPVIPEAVNQVAFEVIG 347
Cdd:PRK06705 250 MVMMTNTSRWIHDFLLLATKEYDGITVAR--PYVQISSIMPQKRNPVSIEHARAITSSALG 308
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
164-220 |
1.01e-04 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 44.73 E-value: 1.01e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 15600622 164 LLASLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLDRLR 220
Cdd:PLN02848 146 VLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMANFAYRLSRQRKQLS 202
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
138-333 |
3.05e-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: 42.99 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 138 DVNmaqstNDAYPTAIRLGLllgHDTLLASLDSLIQAFAAKGVEFAGVLKMGRTQLQDAVPMTLGQEFHAFATTLGEDLD 217
Cdd:cd01598 103 DIN-----NLAYALMIKEAR---NEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYK 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15600622 218 RLRRLapELLTEVNlGgtAIGT---GINADPGYQKLAVERLAAIS-GQPLKPAADLIEATSDMGAfvlFSGMLKRTAVKL 293
Cdd:cd01598 175 QLKQI--EILGKFN-G--AVGNfnaHLVAYPDVDWRKFSEFFVTSlGLTWNPYTTQIEPHDYIAE---LFDALARINTIL 246
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 15600622 294 SKICND------LRLLSSGPRTGinEInlpprqpGSSIMPGKVNPV 333
Cdd:cd01598 247 IDLCRDiwgyisLGYFKQKVKKG--EV-------GSSTMPHKVNPI 283
|
|
| |
