|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
5-462 |
0e+00 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 858.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 5 KTNQSWGGRFSEPVDAFVARFTASVDFDKRLYRHDIMGSIAHATMLAKVGVLSDAERDAIVDGLQQIQAEIEAGSFDWRV 84
Cdd:PRK00855 2 MSNKLWGGRFSEGPDELVERFTASISFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILEEIEAGKFEFSP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 85 DLEDVHMNIEARLTDRIGVTGKKLHTGRSRNDQVATDIRLWLRDEIDTILAEITRLQEGLLGLAEAEADTIMPGFTHLQT 164
Cdd:PRK00855 82 ELEDIHMAIEARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 165 AQPVTFGHHLLAWFEMLGRDYERLVDCRKRVNRMPLGSAALAGTTYPIQREITCQLLGFDAVGGNSLDGVSDRDFAIEFC 244
Cdd:PRK00855 162 AQPVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAALAGTTFPIDRERTAELLGFDGVTENSLDAVSDRDFALEFL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 245 AAASLAMMHLSRFSEELVLWTSAQFQFIDLPDRFCTGSSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYNK 324
Cdd:PRK00855 242 SAASLLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLAYNR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 325 DNQEDKEPLFDAADTLRDSLRAFADMVPAIRPRREIMREAARRGFSTATDLADYLVRKGLPFRDCHEIVGHAVKYGVDSG 404
Cdd:PRK00855 322 DLQEDKEPLFDAVDTLKLSLEAMAGMLETLTVNKERMREAAGKGFSTATDLADYLVRKGVPFREAHEIVGKAVREAEERG 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 489204969 405 KDLAEMSLDELRRFSEQIDADVFDVLTLEGSVNARDHIGGTAPNQVRAAVARGRKLLA 462
Cdd:PRK00855 402 VDLADLSLEELQAFSPLITEDVYEVLTPEGSVAARNSIGGTAPEQVREQIARAKARLA 459
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
5-464 |
0e+00 |
|
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: 843.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 5 KTNQSWGGRFSEPVDAFVARFTASVDFDKRLYRHDIMGSIAHATMLAKVGVLSDAERDAIVDGLQQIQAEIEAGSFDWRV 84
Cdd:COG0165 1 MSMKLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAFEFDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 85 DLEDVHMNIEARLTDRIGVTGKKLHTGRSRNDQVATDIRLWLRDEIDTILAEITRLQEGLLGLAEAEADTIMPGFTHLQT 164
Cdd:COG0165 81 ELEDIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 165 AQPVTFGHHLLAWFEMLGRDYERLVDCRKRVNRMPLGSAALAGTTYPIQREITCQLLGFDAVGGNSLDGVSDRDFAIEFC 244
Cdd:COG0165 161 AQPVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 245 AAASLAMMHLSRFSEELVLWTSAQFQFIDLPDRFCTGSSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYNK 324
Cdd:COG0165 241 SAASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 325 DNQEDKEPLFDAADTLRDSLRAFADMVPAIRPRREIMREAARRGFSTATDLADYLVRKGLPFRDCHEIVGHAVKYGVDSG 404
Cdd:COG0165 321 DLQEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGFSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKG 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 405 KDLAEMSLDELRRFSEQIDADVFDVLTLEGSVNARDHIGGTAPNQVRAAVARGRKLLAQR 464
Cdd:COG0165 401 KDLEDLTLEELQAFSPLIEEDVYEALDPEGSVAARDSYGGTAPEAVREQIARARARLAAL 460
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
28-461 |
0e+00 |
|
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: 718.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 28 SVDFDKRLYRHDIMGSIAHATMLAKVGVLSDAERDAIVDGLQQIQAEIEAGSFDWRVDLEDVHMNIEARLTDRIGVTGKK 107
Cdd:cd01359 1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGDVGGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 108 LHTGRSRNDQVATDIRLWLRDEIDTILAEITRLQEGLLGLAEAEADTIMPGFTHLQTAQPVTFGHHLLAWFEMLGRDYER 187
Cdd:cd01359 81 LHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 188 LVDCRKRVNRMPLGSAALAGTTYPIQREITCQLLGFDAVGGNSLDGVSDRDFAIEFCAAASLAMMHLSRFSEELVLWTSA 267
Cdd:cd01359 161 LADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 268 QFQFIDLPDRFCTGSSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYNKDNQEDKEPLFDAADTLRDSLRAF 347
Cdd:cd01359 241 EFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 348 ADMVPAIRPRREIMREAARRGFSTATDLADYLVR-KGLPFRDCHEIVGHAVKYGVDSGKDLAEMSLDELRRFSEQIDADV 426
Cdd:cd01359 321 TGVISTLTVNPERMREAAEAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEEDV 400
|
410 420 430
....*....|....*....|....*....|....*
gi 489204969 427 FDVLTLEGSVNARDHIGGTAPNQVRAAVARGRKLL 461
Cdd:cd01359 401 REALDPENSVERRTSYGGTAPAEVREQIARARALL 435
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
10-455 |
0e+00 |
|
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: 660.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 10 WGGRFSEPVDAFVARFTASVDFDKRLYRHDIMGSIAHATMLAKVGVLSDAERDAIVDGLQQIQAEIEAGSFDWRVDLEDV 89
Cdd:TIGR00838 2 WGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPFILDPDDEDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 90 HMNIEARLTDRIGV-TGKKLHTGRSRNDQVATDIRLWLRDEIDTILAEITRLQEGLLGLAEAEADTIMPGFTHLQTAQPV 168
Cdd:TIGR00838 82 HMAIERELIDRVGEdLGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 169 TFGHHLLAWFEMLGRDYERLVDCRKRVNRMPLGSAALAGTTYPIQREITCQLLGFDAVGGNSLDGVSDRDFAIEFCAAAS 248
Cdd:TIGR00838 162 TLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFVAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 249 LAMMHLSRFSEELVLWTSAQFQFIDLPDRFCTGSSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYNKDNQE 328
Cdd:TIGR00838 242 LIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 329 DKEPLFDAADTLRDSLRAFADMVPAIRPRREIMREAARRGFSTATDLADYLVRKGLPFRDCHEIVGHAVKYGVDSGKDLA 408
Cdd:TIGR00838 322 DKEPLFDALKTVELSLEMATGMLDTITVNKERMEEAASAGFSNATELADYLVRKGVPFREAHHIVGELVATAIERGKGLE 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 489204969 409 EMSLDELRRFSEQIDADVFDVLTLEGSVNARDHIGGTAPNQVRAAVA 455
Cdd:TIGR00838 402 ELTLEELQKFSPEFDEDVYEALDPESSVEKRDAKGGTAPEEVLQAIA 448
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
4-463 |
0e+00 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 619.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 4 EKTNQSWGGRFSEPVDAFVARFTASVDFDKRLYRHDIMGSIAHATMLAKVGVLSDAERDAIVDGLQQIQAEIEAGSFDWR 83
Cdd:PLN02646 13 AKEKKLWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAGKFEWR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 84 VDLEDVHMNIEARLTDRIGVTGKKLHTGRSRNDQVATDIRLWLRDEIDTILAEITRLQEGLLGLAEAEADTIMPGFTHLQ 163
Cdd:PLN02646 93 PDREDVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQ 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 164 TAQPVTFGHHLLAWFEMLGRDYERLVDCRKRVNRMPLGSAALAGTTYPIQREITCQLLGFDAVGGNSLDGVSDRDFAIEF 243
Cdd:PLN02646 173 RAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRDFVLEF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 244 CAAASLAMMHLSRFSEELVLWTSAQFQFIDLPDRFCTGSSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYN 323
Cdd:PLN02646 253 LFANSITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTAYN 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 324 KDNQEDKEPLFDAADTLRDSLRAFADMVPAIRPRREIMREAARRGFSTATDLADYLVRKGLPFRDCHEIVGHAVKYGVDS 403
Cdd:PLN02646 333 RDLQEDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLDATTLADYLVRKGVPFRETHHIVGAAVALAESK 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 404 GKDLAEMSLDELRRFSEQIDADVFDVLTLEGSVNARDHIGGTAPNQVRAAVARGRKLLAQ 463
Cdd:PLN02646 413 GCELSDLTLEDLKSINPVFEEDVYEVLGVENSVEKFDSYGSTGSRSVLEQLEKWRTKLEI 472
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
10-455 |
0e+00 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 568.85 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 10 WGGRFSEPVDAFVARFTASVDFDKRLYRHDIMGSIAHATMLAKVGVLSDAERDAIVDGLQQIQAEIEAGSFD-WRVDLED 88
Cdd:PRK04833 4 WGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQQQLEEALNELLEEVRANPQQiLASDAED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 89 VHMNIEARLTDRIGVTGKKLHTGRSRNDQVATDIRLWLRDEIDTILAEITRLQEGLLGLAEAEADTIMPGFTHLQTAQPV 168
Cdd:PRK04833 84 IHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRAQPV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 169 TFGHHLLAWFEMLGRDYERLVDCRKRVNRMPLGSAALAGTTYPIQREITCQLLGFDAVGGNSLDGVSDRDFAIEFCAAAS 248
Cdd:PRK04833 164 TFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSDAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 249 LAMMHLSRFSEELVLWTSAQFQFIDLPDRFCTGSSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYNKDNQE 328
Cdd:PRK04833 244 ISMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPLAYNKDMQE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 329 DKEPLFDAADTLRDSLRAFADMVPAIRPRREIMREAARRGFSTATDLADYLVRKGLPFRDCHEIVGHAVKYGVDSGKDLA 408
Cdd:PRK04833 324 DKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPLE 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 489204969 409 EMSLDELRRFSEQIDADVFDVLTLEGSVNARDHIGGTAPNQVRAAVA 455
Cdd:PRK04833 404 DLPLAELQKFSSVIGDDVYPILSLQSCLDKRAAKGGVSPQQVAQAIA 450
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
10-464 |
5.16e-180 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 517.03 E-value: 5.16e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 10 WGGRFSEPVDAFVARFTASVDFDKRLYRHDIMGSIAHATMLAKVGVLSDAERDAIVDGLQQIQAEIEAGSFD-WRVDLED 88
Cdd:PRK12308 4 WGGRFSQAADTRFKQFNDSLRFDYRLAEQDIVGSIAWSKALLSVGVLSEEEQQKLELALNELKLEVMEDPEQiLLSDAED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 89 VHMNIEARLTDRIGVTGKKLHTGRSRNDQVATDIRLWLRDEIDTILAEITRLQEGLLGLAEAEADTIMPGFTHLQTAQPV 168
Cdd:PRK12308 84 IHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 169 TFGHHLLAWFEMLGRDYERLVDCRKRVNRMPLGSAALAGTTYPIQREITCQLLGFDAVGGNSLDGVSDRDFAIEFCAAAS 248
Cdd:PRK12308 164 TFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGSGALAGTAYPIDREALAHNLGFRRATRNSLDSVSDRDHVMELMSVAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 249 LAMMHLSRFSEELVLWTSAQFQFIDLPDRFCTGSSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYNKDNQE 328
Cdd:PRK12308 244 ISMLHLSRLAEDLIFYNSGESGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKDMQE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 329 DKEPLFDAADTLRDSLRAFADMVPAIRPRREIMREAARRGFSTATDLADYLVRKGLPFRDCHEIVGHAVKYGVDSGKDLA 408
Cdd:PRK12308 324 DKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANATELADYLVAKGIPFREAHHIVGVAVVGAIAKGCALE 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 489204969 409 EMSLDELRRFSEQIDADVFDVLTLEGSVNARDHIGGTAPNQVRAAVARGRKLLAQR 464
Cdd:PRK12308 404 ELSLEQLKEFSDVIEDDVYQILTIESCLEKRCALGGVSPEQVAYAVEQADKRLAAR 459
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
36-356 |
1.30e-143 |
|
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: 413.44 E-value: 1.30e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 36 YRHDIMGSIAHATMLAKVGVLSDAERDAIVDGLQQIQAEIEAGSFDWRVDLEDVHMNIEARLTDRIG-VTGKKLHTGRSR 114
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVEQEGSGTHDVMAVEEVLAERAGeLNGGYVHTGRSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 115 NDQVATDIRLWLRDEIDTILAEITRLQEGLLGLAEAEADTIMPGFTHLQTAQPVTFGHHLLAWFEMLGRDYERLVDCRKR 194
Cdd:cd01334 81 NDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 195 VNRMPLGSAALAGTTY--PIQREITCQLLGFDAVGGNSLDGVSDRDFAIEFCAAASLAMMHLSRFSEELVLWTSAQFQFI 272
Cdd:cd01334 161 LNVLPLGGGAVGTGANapPIDRERVAELLGFFGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 273 DLPDRFCTGSSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYNKDNQEDKEPLFDAADTLRDSLRAFADMVP 352
Cdd:cd01334 241 ELPDAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVLE 320
|
....
gi 489204969 353 AIRP 356
Cdd:cd01334 321 GLEV 324
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
12-306 |
5.65e-87 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 268.47 E-value: 5.65e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 12 GRFSEPVDAFVARFTASVDFDKRLYRHDIMGSIAHATMLAKVGVLSDAERDAIVDGLQQIQAEIEAGS-FDWRVDLEDVH 90
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDDqFPLKVWQEGSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 91 MNIEARLTDRIGV-------TGKKLHTGRSRNDQVATDIRLWLRDEIDT-ILAEITRLQEGLLGLAEAEADTIMPGFTHL 162
Cdd:pfam00206 81 TAVNMNLNEVIGEllgqlvhPNDHVHTGQSSNDQVPTALRLALKDALSEvLLPALRQLIDALKEKAKEFADIVKPGRTHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 163 QTAQPVTFGHHLLAWFEMLGRDYERLVDCRKRVNRMPLGSAALAGTTYPIQREITCQLL-------GFDAVGGNSLDGVS 235
Cdd:pfam00206 161 QDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEFAELVAkelgfftGLPVKAPNSFEATS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489204969 236 DRDFAIEFCAAASLAMMHLSRFSEELVLWTSAQFQFIDLPDRFCT-GSSIMPQKKNPDVPELVRGKSGRVFG 306
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEpGSSIMPGKVNPDQLELLTGKAGRVMG 312
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
45-463 |
2.54e-69 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 236.67 E-value: 2.54e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 45 AHATMLAKVGVLSdaeRDAIVDGLQQIQAEIEAG--SFDWRVDLEDVHMNIEARLTDRIGV-TGKKLHTGRSRNDQVATD 121
Cdd:PRK02186 447 AHLVMLGDTGIVA---PERARPLLDAHRRLRDAGfaPLLARPAPRGLYMLYEAYLIERLGEdVGGVLQTARSRNDINATT 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 122 IRLWLRDEIDTILAEITRLQEGLLGLAEAEADTIMPGFTHLQTAQPVTFGHHLLAWFEMLGRDYERLVDCRKRVNRMPLG 201
Cdd:PRK02186 524 TKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHALFALFEHIDVCPLG 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 202 SAALAGTTYPIQREITCQLLGFDAVGGNSLDGVSDRDFAIEFCAAASLAMMHLSRFSEELVLWTSAQFQFIDLPDRFCTG 281
Cdd:PRK02186 604 AGAGGGTTFPIDPEFVARLLGFEQPAPNSLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQLWTTREFALVSLPDALTGG 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 282 SSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYNKD-NQEDKEPLFDAADTLRDSLRAFADMVPAIRPRREI 360
Cdd:PRK02186 684 SSMLPQKKNPFLLEFVKGRAGVVAGALASASAALGKTPFSNSFEaGSPMNGPIAQACAAIEDAAAVLVLLIDGLEADQAR 763
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 361 MREAARRGFSTATDLADYLV-RKGLPFRDCHEIVGHAVKYGVDSGKDLAEmSLDELrrfseqiDADVFDVLTLEGsvnAR 439
Cdd:PRK02186 764 MRAHLEDGGVSATAVAESLVvRRSISFRSAHTQVGQAIRQSLDQGRSSAD-ALAAL-------DPQFVSRAPLEW---AR 832
|
410 420
....*....|....*....|....*.
gi 489204969 440 DHIGGTAPN--QVRAAVARGRKLLAQ 463
Cdd:PRK02186 833 SHRFGGGPGaaDLNAGLARACAALRD 858
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
91-348 |
1.94e-67 |
|
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: 215.55 E-value: 1.94e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 91 MNIEARLTDRIGVTGKKLH------TGRSRNDQVATDIRLWLRDEIDTILAEITRLQEGLLGLAEAEADTIMPGFTHLQT 164
Cdd:cd01594 14 ALVEEVLAGRAGELAGGLHgsalvhKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 165 AQPVTFGHHLLAWFEMLGRDYERLVDCrkrvnrmplgsaalagttypiqreitcqllgfdavggnsldgvsdrdFAIEFC 244
Cdd:cd01594 94 AQPVTLGYELRAWAQVLGRDLERLEEA-----------------------------------------------AVAEAL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 245 AAASLAMMHLSRFSEELVLWTSAQFQFIDLPD-RFCTGSSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYN 323
Cdd:cd01594 127 DALALAAAHLSKIAEDLRLLLSGEFGELGEPFlPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDN 206
|
250 260
....*....|....*....|....*
gi 489204969 324 KDNQEDKEPLFDAADTLRDSLRAFA 348
Cdd:cd01594 207 EDSPSMREILADSLLLLIDALRLLL 231
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
45-463 |
5.76e-56 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 193.66 E-value: 5.76e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 45 AHATMLAKVGVLSDAERDAIVDGLQQIqAEIEAGSFDWRVDLEDVHMNIEARLTDRIGV-TGKKLHTGRSRNDQVATDIR 123
Cdd:PRK06705 47 AHIVMLTEENLMKKEEAKFILHALKKV-EEIPEEQLLYTEQHEDLFFLVEHLISQEAKSdFVSNMHIGRSRNDMGVTMYR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 124 LWLRDEIDTILAEITRLQEGLLGLAEAEADTIMPGFTHLQTAQPVTFGHHLLAWFEMLGRDYERLVDCRKRVNRMPLGSA 203
Cdd:PRK06705 126 MSLRRYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKTYKLLNQSPMGAA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 204 ALAGTTYPIQREITCQLLGFDAVGGNSLDGVSDRDFAIEFCAAASLAMMHLSRFSEELVLWTSAQFQFIDLPDRFCTGSS 283
Cdd:PRK06705 206 ALSTTSFPIKRERVADLLGFTNVIENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLATKEYDGITVARPYVQISS 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 284 IMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYNKDNQEDKEP-LFDAadtLRDSLRAFADMVPAIRPRR---E 359
Cdd:PRK06705 286 IMPQKRNPVSIEHARAITSSALGEAFTVFQMIHNTPFGDIVDTEDDLQPyLYKG---IEKAIRVFCIMNAVIRTMKveeD 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 360 IMREAARRGFSTATDLADYLVRK-GLPFRDCHEIVGHAVKYGVDSGKDLAEMSLDELRRFSEQ------IDADVFDVLTL 432
Cdd:PRK06705 363 TLKRRSYKHAITITDFADVLTKNyGIPFRHAHHAASVIANMSLEQKKELHELCFKDVNIYLQEkfkiqlLEKEWEEIISP 442
|
410 420 430
....*....|....*....|....*....|.
gi 489204969 433 EGSVNARDHIGGTAPNQVRAAVARGRKLLAQ 463
Cdd:PRK06705 443 EAFIQKRNVYGGPSKKEMERMINNRKELFRK 473
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
16-402 |
2.76e-34 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 133.10 E-value: 2.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 16 EPVDAFVARftaSVDFDKRLYRHDIMGSIAHATMLAKVGVLSDAERDAIVDGLqqiqAEIEAGSFDWRVDLEDVHMNIEA 95
Cdd:PRK06389 15 DFYDNIVKD---DIDADKNLIKYEIINLLAYHVALAQRRLITEKAPKCVINAL----IDIYKNGIEIDLDLEDVHTAIEN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 96 RLTDRIGVTGKKLHTGRSRNDQVATDIRLWLRD---EIDTILAEITRLQEGllglaeAEADTIMPGFTHLQTAQPVTFGH 172
Cdd:PRK06389 88 FVIRRCGDMFKNFRLFLSRNEQVHADLNLFIIDkiiEIEKILYEIIKVIPG------FNLKGRLPGYTHFRQAMPMTVNT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 173 HLLAWFEMLGRDYERLVDCRKRVNRMPLGSAALAGTTYPIQREITCQLLGFDAVGGNSLDGVSDRDFAI-EFCAAASLAM 251
Cdd:PRK06389 162 YINYIKSILYHHINNLDSFLMDLREMPYGYGSGYGSPSSVKFNQMSELLGMEKNIKNPVYSSSLYIKTIeNISYLISSLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 252 MHLSRFSEELVLWTSAQFqfIDLPDRFCTGSSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYNKDNQEDKE 331
Cdd:PRK06389 242 VDLSRICQDIIIYYENGI--ITIPDEFTTGSSLMPNKRNPDYLELFQGIAAESISVLSFIAQSELNKTTGYHRDFQIVKD 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489204969 332 PLFDAADTLRDSLRAFADMVPAIrpRREIMREAARRGFSTATDLADYLVRKGLPFRDCHEIVGHAVKYGVD 402
Cdd:PRK06389 320 STISFINNFERILLGLPDLLYNI--KFEITNEKNIKNSVYATYNAWLAFKNGMDWKSAYAYIGNKIREGEV 388
|
|
| ASL_C2 |
pfam14698 |
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of ... |
369-436 |
1.80e-33 |
|
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of argininosuccinate lyase.
Pssm-ID: 464268 [Multi-domain] Cd Length: 68 Bit Score: 120.60 E-value: 1.80e-33
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489204969 369 FSTATDLADYLVRKGLPFRDCHEIVGHAVKYGVDSGKDLAEMSLDELRRFSEQIDADVFDVLTLEGSV 436
Cdd:pfam14698 1 FSTATDLADYLVRKGVPFREAHEIVGRLVRLAEEKGKDLEDLTLEELQAISPLFEEDVYEALDPEASV 68
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
51-423 |
1.30e-28 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 117.78 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 51 AKVGVLSDAERDAIVDGLQqiqaEIEAGSFD--WRVDL------EDVHMN----IEARLTDRIGvtGKK-----LH---- 109
Cdd:PRK13353 61 ADLGLLPRRIAEAIVQACD----EILAGKLHdqFIVDPiqggagTSTNMNanevIANRALELLG--GEKgdyhyVSpndh 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 110 --TGRSRNDQVATDIRLWLRDEIDTILAEITRLQEGLLGLAEAEADTIMPGFTHLQTAQPVTFGHHLLAWFEMLGRDYER 187
Cdd:PRK13353 135 vnMAQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKR 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 188 LVDCRKRVNRMPLGSAALaGT-----------TYPIQREITcqllGFDAVGGNSL-DGVSDRDFAIEFCAAASLAMMHLS 255
Cdd:PRK13353 215 IQQAREHLYEVNLGGTAV-GTglnadpeyierVVKHLAAIT----GLPLVGAEDLvDATQNTDAFVEVSGALKVCAVNLS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 256 RFSEELVLWTS---AQFQFIDLPDRFCtGSSIMPQKKNPDVPELVRGKSGRVFG--------ALTGLLTLMKGQPL-AYN 323
Cdd:PRK13353 290 KIANDLRLLSSgprTGLGEINLPAVQP-GSSIMPGKVNPVMPEVVNQIAFQVIGndvtitlaAEAGQLELNVMEPViAFN 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 324 kdnqedkepLFDAADTLRDSLRAFAD-MVPAIRPRREIMREAARRGFSTATDLADYLvrkGlpfrdcHEIVGHAVKYGVD 402
Cdd:PRK13353 369 ---------LLESISILTNACRAFTDnCVKGIEANEERCKEYVEKSVGIATALNPHI---G------YEAAARIAKEAIA 430
|
410 420
....*....|....*....|.
gi 489204969 403 SGKDLAEMSLDELRRFSEQID 423
Cdd:PRK13353 431 TGRSVRELALENGLLSEEELD 451
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
73-393 |
1.03e-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: 105.28 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 73 AEIEAGSFDWRVDLEDVHmNIEAR-----------LTDRIGVTGKK-LHTGRSRNDQVATDIRLWLRDEIDTILAEITRL 140
Cdd:cd01595 37 EEIRAAADVFEIDAERIA-EIEKEtghdviafvyaLAEKCGEDAGEyVHFGATSQDINDTALALQLRDALDIILPDLDAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 141 QEGLLGLAEAEADTIMPGFTHLQTAQPVTFGHHLLAWFEMLGRDYERLVDCRKRVNRM----PLGSAALAGTTYPIQREI 216
Cdd:cd01595 116 IDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGgisgAVGTHASLGPKGPEVEER 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 217 TCQLLGFDAVGGNSLdgVSDRDFAIEFCAAasLAMMH--LSRFSEELVLWTSAQFQFIDLP-DRFCTGSSIMPQKKNPDV 293
Cdd:cd01595 196 VAEKLGLKVPPITTQ--IEPRDRIAELLSA--LALIAgtLEKIATDIRLLQRTEIGEVEEPfEKGQVGSSTMPHKRNPID 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 294 PELVRGKSGRVFGALTGLLTLMkgqplaynkdNQEDKEPLFDAA---DTLRDS-------LRAFADMVPAIRPRREIMRE 363
Cdd:cd01595 272 SENIEGLARLVRALAAPALENL----------VQWHERDLSDSSverNILPDAfllldaaLSRLQGLLEGLVVNPERMRR 341
|
330 340 350
....*....|....*....|....*....|....
gi 489204969 364 --AARRGF--STATDLAdyLVRKGLPFRDCHEIV 393
Cdd:cd01595 342 nlDLTWGLilSEAVMMA--LAKKGLGRQEAYELV 373
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
51-423 |
4.55e-24 |
|
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: 104.14 E-value: 4.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 51 AKVGVLSDAERDAIVDGLQqiqaEIEAGSFD--WRVDL------EDVHMN----IEARLTDRIGvtGKK-----LH---- 109
Cdd:cd01357 56 AELGLLDEEKAEAIVKACD----EIIAGKLHdqFVVDViqggagTSTNMNanevIANRALELLG--HEKgeyqyVHpndh 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 110 --TGRSRNDQVATDIRLWLRDEIDTILAEITRLQEGLLGLAEAEADTIMPGFTHLQTAQPVTFGHHLLAWFEMLGRDYER 187
Cdd:cd01357 130 vnMSQSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRAR 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 188 LVDCRKRVNRMPLGSAALaGT------TYPIQ-REITCQLLGFD-AVGGNSLDGVSDRDFAIEFCAAASLAMMHLSRFSE 259
Cdd:cd01357 210 IYKARERLREVNLGGTAI-GTginappGYIELvVEKLSEITGLPlKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIAN 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 260 ELVLWTS---AQFQFIDLPDRfCTGSSIMPQKKNPDVPELVRGKSGRVFG---ALT-----GLLTLMKGQPL-AYNkdnq 327
Cdd:cd01357 289 DLRLLSSgprAGLGEINLPAV-QPGSSIMPGKVNPVIPEVVNQVAFQVIGndlTITmaaeaGQLELNVFEPViAYN---- 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 328 edkepLFDAADTLRDSLRAFAD-MVPAIRPRREIMREAARRGFSTATDLADYLvrkGlpfrdcHEIVGHAVKYGVDSGKD 406
Cdd:cd01357 364 -----LLESIDILTNAVRTLRErCIDGITANEERCREYVENSIGIVTALNPYI---G------YEAAAEIAKEALETGRS 429
|
410
....*....|....*..
gi 489204969 407 LAEMSLDELRRFSEQID 423
Cdd:cd01357 430 VRELVLEEGLLTEEELD 446
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
105-456 |
2.95e-22 |
|
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: 98.86 E-value: 2.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 105 GKKLHTGRSRNDQVATDIRLWLRDEIDTILAEITRLQEGLLGLAEAEADTIMPGFTHLQTAQPVTFGHHLLAWFEMLGRD 184
Cdd:cd01597 90 GEYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRH 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 185 YERLVDCRKRVNRMPLGSAA--LA--GTTYPIQREITCQLLGFDAVGGNSLdgvSDRDFAIEFcaAASLAMMH--LSRFS 258
Cdd:cd01597 170 RERLDELRPRVLVVQFGGAAgtLAslGDQGLAVQEALAAELGLGVPAIPWH---TARDRIAEL--ASFLALLTgtLGKIA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 259 EELVLWTSAQFQFIDLPDRFCTG-SSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKgqplaynKDNQEDKEPLFDAA 337
Cdd:cd01597 245 RDVYLLMQTEIGEVAEPFAKGRGgSSTMPHKRNPVGCELIVALARRVPGLAALLLDAMV-------QEHERDAGAWHAEW 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 338 DTLRDSLRAFA-------DMVPAIRPRREIMRE--AARRGF----STATDLADYLVRKglpfrDCHEIVGHAVKYGVDSG 404
Cdd:cd01597 318 IALPEIFLLASgaleqaeFLLSGLEVNEDRMRAnlDLTGGLilseAVMMALAPKLGRQ-----EAHDLVYEACMRAVEEG 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 489204969 405 KDLAEMsLDELRRFSEQIDADVFDVLTlegsvNARDHIgGTAPNQVRAAVAR 456
Cdd:cd01597 393 RPLREV-LLEDPEVAAYLSDEELDALL-----DPANYL-GSAPALVDRVLAR 437
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
41-379 |
3.04e-20 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 92.81 E-value: 3.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 41 MGSIAHATMLA--KVGVLSDAERDAIVdglqqiQA--EIEAGSFD--WRVDL------EDVHMN----IEARLTDRIGvt 104
Cdd:COG1027 46 LAMVKKAAALAnrELGLLDKEKADAIV------AAcdEIIAGKLHdqFVVDViqggagTSTNMNanevIANRALEILG-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 105 GKK-----LH------TGRSRNDQVATDIRLWLRDEIDTILAEITRLQEGLLGLAEAEADTIMPGFTHLQTAQPVTFGHH 173
Cdd:COG1027 118 GKKgdydyVHpndhvnMSQSTNDVYPTAIRLALLLLLRELLEALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQE 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 174 LLAWFEMLGRDYERLVDCRKRVNRMPLGSAAlAGT---TYPIQREITCQLL----GFD-AVGGNSLDGVSDRDFAIEFCA 245
Cdd:COG1027 198 FGAYAVALARDRWRLYEAAELLREVNLGGTA-IGTglnAPPGYIELVVEHLaeitGLPlVRAENLIEATQDTDAFVEVSG 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 246 AASLAMMHLSRFSEELVLWTS---AQFQFIDLPDRfCTGSSIMPQKKNPDVPELVRGKSGRVFGA-LTglLTLM--KGQ- 318
Cdd:COG1027 277 ALKRLAVKLSKICNDLRLLSSgprAGLGEINLPAV-QPGSSIMPGKVNPVIPEVVNQVAFQVIGNdLT--VTMAaeAGQl 353
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489204969 319 ------PL-AYNkdnqedkepLFDAADTLRDSLRAFADM-VPAIRPRREIMREAARRGFSTATDLADYL 379
Cdd:COG1027 354 elnvfePViAYN---------LLESIELLTNACRTLREKcIDGITANEERCREYVENSIGLVTALNPYI 413
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
44-453 |
3.30e-20 |
|
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439786 [Multi-domain] Cd Length: 436 Bit Score: 92.45 E-value: 3.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 44 IAHATMLAKVGVLSDAERDAIvdglqqiQAEIEAGSFDW-RVD-LE-----DVhMNIEARLTDRIGVTGKK-LHTGrsrn 115
Cdd:COG0015 29 IALAEAQAELGLIPAEAAAAI-------RAAADDFEIDAeRIKeIEketrhDV-KAFVYALKEKVGAEAGEyIHFG---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 116 dqvAT--DI-----RLWLRDEIDTILAEITRLQEGLLGLAEAEADTIMPGFTHLQTAQPVTFGHHLLAWFEMLGRDYERL 188
Cdd:COG0015 97 ---ATsqDIndtalALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 189 VDCRKRVnrmPLGsaALAGT--TY--------PIQREItCQLLGFDAvggNSLDG-VSDRDFAIEFCAAASLAMMHLSRF 257
Cdd:COG0015 174 EEARERV---LVG--KIGGAvgTYaahgeawpEVEERV-AEKLGLKP---NPVTTqIEPRDRHAELFSALALIAGSLEKI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 258 SEELVLWTSAQ----FQFIDlPDRfcTGSSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMkgqplaynkdNQEDKEPL 333
Cdd:COG0015 245 ARDIRLLQRTEvgevEEPFA-KGQ--VGSSAMPHKRNPIDSENIEGLARLARALAAALLEAL----------ASWHERDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 334 FDAA---DTLRDS-------LRAFADMVPAIRPRREIMRE--AARRGFSTATDLADYLVRKGLPFRDCHEIVGHAVKYGV 401
Cdd:COG0015 312 SDSSverNILPDAfllldgaLERLLKLLEGLVVNPERMRAnlDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAW 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 489204969 402 DSGKDLAEMsLDELRRFSEQIDADVFDVLTlegsvNARDHIgGTAPNQVRAA 453
Cdd:COG0015 392 EEGNDLREL-LAADPEIPAELSKEELEALF-----DPANYL-GAADEIVDRV 436
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
97-291 |
2.84e-19 |
|
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: 89.15 E-value: 2.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 97 LTDRIGVTGKKLHTGRSRNDQVATDIRLWLRDEIDTILAEITRLQEGLLGLAEAEADTIMPGFTHLQTAQPVTFGHHLLA 176
Cdd:cd01360 74 IAEYCGEAGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFAL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 177 WFEMLGRDYERLVDCRKRVNRM----PLGSAALAGttyPIQREITCQLLGFDAVGGNSldGVSDRDFAIEFCA-----AA 247
Cdd:cd01360 154 WYAEFKRHLERLKEARERILVGkisgAVGTYANLG---PEVEERVAEKLGLKPEPIST--QVIQRDRHAEYLStlaliAS 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489204969 248 SLAMM-----HLSRfSEelVLWTSAQFqfidlpDRFCTGSSIMPQKKNP 291
Cdd:cd01360 229 TLEKIateirHLQR-TE--VLEVEEPF------SKGQKGSSAMPHKRNP 268
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
41-379 |
7.20e-19 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 88.64 E-value: 7.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 41 MGSIAHATMLA--KVGVLSDAERDAIVdglqqiQA--EIEAGSFD--WRVDL------EDVHMNIEARLTDR-IGVTGKK 107
Cdd:PRK12273 51 LAMVKKAAALAnkELGLLDEEKADAIV------AAcdEILAGKLHdqFVVDViqggagTSTNMNANEVIANRaLELLGHE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 108 ------LH------TGRSRNDQVATDIRLWLRDEIDTILAEITRLQEGLLGLAEAEADTIMPGFTHLQTAQPVTFGHHLL 175
Cdd:PRK12273 125 kgeyqyVHpndhvnMSQSTNDAYPTAIRIALLLSLRKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 176 AWFEMLGRDYERLVDCRKRVNRMPLGSAAlAGT------TYPIQ-----REITcqllGFD-AVGGNSLDGVSDRDFAIEF 243
Cdd:PRK12273 205 AYAVALAEDRKRLYRAAELLREVNLGATA-IGTglnappGYIELvveklAEIT----GLPlVPAEDLIEATQDTGAFVEV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 244 CAAASLAMMHLSRFSEELVLWTS---AQFQFIDLPDRfCTGSSIMPQKKNPDVPELVRGKSGRVFGA-LTglLTLM--KG 317
Cdd:PRK12273 280 SGALKRLAVKLSKICNDLRLLSSgprAGLNEINLPAV-QAGSSIMPGKVNPVIPEVVNQVCFQVIGNdTT--VTMAaeAG 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489204969 318 Q-------PL-AYNkdnqedkepLFDAADTLRDSLRAFADM-VPAIRPRREIMREAARRGFSTATDLADYL 379
Cdd:PRK12273 357 QlelnvmePViAYN---------LFESISILTNACRTLREKcIDGITANEERCREYVENSIGIVTALNPYI 418
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
113-379 |
3.06e-18 |
|
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: 86.71 E-value: 3.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 113 SRNDQVATDIRLWLRDEIDTILAEITRLQEGLLGLAEAEADTIMPGFTHLQTAQPVTFGHHLLAWFEMLGRDYERLVDCR 192
Cdd:cd01596 135 SNDDFPPAAHIAAALALLERLLPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAAL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 193 KRVNRMPLGSAALaGT---TYPIQREITC----QLLGFD-AVGGNSLDGVSDRDFAIEFCAAASLAMMHLSRFSEELVLW 264
Cdd:cd01596 215 ERLRELNLGGTAV-GTglnAPPGYAEKVAaelaELTGLPfVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLL 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 265 TS---AQFQFIDLPDRfCTGSSIMPQKKNPDVPELVRGKSGRVFG---ALT-----GLLTL--MKgqPL-AYNkdnqedk 330
Cdd:cd01596 294 SSgprAGLGEINLPAN-QPGSSIMPGKVNPVIPEAVNMVAAQVIGndtAITmagsaGQLELnvFK--PViAYN------- 363
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 489204969 331 epLFDAADTLRDSLRAFAD-MVPAIRPRREIMREAARRGFSTATDLADYL 379
Cdd:cd01596 364 --LLQSIRLLANACRSFRDkCVEGIEANEERCKEYVENSLMLVTALNPHI 411
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
112-306 |
2.71e-13 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 71.57 E-value: 2.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 112 RSRNDQVATDIRLWLRDEIDTILAEITRLQEGLLGLAEAEADTIMPGFTHLQTAQPVTFGHHLLAWFEMLGRDYERLVDC 191
Cdd:PRK14515 145 QSTNDAFPTAIHIATLNALEGLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQS 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 192 RKRVNRMPLGSAALAGTTYPIQREIT------CQLLGFDAVGGNSL-DGVSDRDFAIEFCAAASLAMMHLSRFSEELVLW 264
Cdd:PRK14515 225 RQHLYEVNMGATAVGTGLNADPEYIEavvkhlAAISELPLVGAEDLvDATQNTDAYTEVSAALKVCMMNMSKIANDLRLM 304
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489204969 265 TS---AQFQFIDLPDRfCTGSSIMPQKKNPDVPELVRGKSGRVFG 306
Cdd:PRK14515 305 ASgprVGLAEIMLPAR-QPGSSIMPGKVNPVMPEVINQIAFQVIG 348
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
95-204 |
5.69e-12 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 67.35 E-value: 5.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 95 ARLTDRIGVTGKKLHTGRSRNDQVATDIRLWLRDEIDTILAEITRLQEGLLGLAEAEADTIMPGFTHLQTAQPVTFGHHL 174
Cdd:PRK09053 89 AQVAARDAEAARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKF 168
|
90 100 110
....*....|....*....|....*....|
gi 489204969 175 LAWFEMLGRDYERLVDCRKRVNRMPLGSAA 204
Cdd:PRK09053 169 AGWLDALLRHRQRLAALRPRALVLQFGGAA 198
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
51-376 |
1.59e-11 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 65.88 E-value: 1.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 51 AKVGVLSDAERDAIVdglqqiQA--EIEAGSFDWRVDLeDV---------HMNI-E------ARLTDRIGVTGKKLH--- 109
Cdd:PRK00485 60 AELGLLDAEKADAIV------AAadEVIAGKHDDHFPL-DVwqtgsgtqsNMNVnEvianraSELLGGELGSKKPVHpnd 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 110 ---TGRSRNDQVATDIRLWLRDEI-DTILAEITRLQEGLLGLAEAEADTIMPGFTHLQTAQPVTFGHHLLAWFEMLGRDY 185
Cdd:PRK00485 133 hvnMSQSSNDTFPTAMHIAAVLAIvERLLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGI 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 186 ERLVDCRKRVNRMPLGSAAlAGT---TYP-----IQREITcQLLGFDAV-GGNSLDGVSDRDFAIEFCAA-ASLA--MMH 253
Cdd:PRK00485 213 ERIEAALPHLYELALGGTA-VGTglnAHPgfaerVAEELA-ELTGLPFVtAPNKFEALAAHDALVEASGAlKTLAvsLMK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 254 LS---RF---------SEelvlwtsaqfqfIDLPDRFcTGSSIMPQKKNPDVPELVRGKSGRVFG--------ALTGLLT 313
Cdd:PRK00485 291 IAndiRWlasgprcglGE------------ISLPENE-PGSSIMPGKVNPTQCEALTMVCAQVMGndaavtfaGSQGNFE 357
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489204969 314 L--MKgqPL-AYNkdnqedkepLFDAADTLRDSLRAFAD-MVPAIRPRREIMREAARRGFSTATDLA 376
Cdd:PRK00485 358 LnvFK--PViAYN---------FLQSIRLLADAMRSFADhCVVGIEPNRERIKELLERSLMLVTALN 413
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
111-375 |
4.00e-10 |
|
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: 61.75 E-value: 4.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 111 GRSRNDQVATDIRLWLRDEI-DTILAEITRLQEGLLGLAEAEADTIMPGFTHLQTAQPVTFGHHLLAWFEMLGRDYERLV 189
Cdd:cd01362 133 SQSSNDTFPTAMHIAAALALqERLLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 190 DCRKRVNRMPLGSAALaGT---TYP-----IQREITcQLLGFDAVGG-NSLDGVSDRDFAIEF-----CAAASLamMHLS 255
Cdd:cd01362 213 AALPRLYELALGGTAV-GTglnAHPgfaekVAAELA-ELTGLPFVTApNKFEALAAHDALVEAsgalkTLAVSL--MKIA 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 256 RfseELVLWTS---AQFQFIDLPDRFcTGSSIMPQKKNPDVPELVRGKSGRVFG--------ALTGLLTL--MKgqPL-A 321
Cdd:cd01362 289 N---DIRWLGSgprCGLGELSLPENE-PGSSIMPGKVNPTQCEALTMVAAQVMGndaaitiaGSSGNFELnvFK--PViI 362
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 489204969 322 YNkdnqedkepLFDAADTLRDSLRAFAD-MVPAIRPRREIMREAARRGFSTATDL 375
Cdd:cd01362 363 YN---------LLQSIRLLADACRSFADkCVAGIEPNRERIAELLERSLMLVTAL 408
|
|
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
134-376 |
2.28e-08 |
|
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: 56.19 E-value: 2.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 134 LAEITRLQEGLLGLAEAEADTIMPGFTHLQTAQPVTFGHHLLAWFEMLGRDYERLVDCRKRVNRMPLGsaalaGTtypiq 213
Cdd:COG0114 161 LPALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALG-----GT----- 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 214 reitcqllgfdAVG-G-NSldgvsDRDFAIEFCA--------------------AASLAMMHLS---------------- 255
Cdd:COG0114 231 -----------AVGtGlNA-----HPGFAERVAAelaeltglpfvsapnkfealAAHDALVELSgalktlavslmkiand 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 256 -R---------FSEelvlwtsaqfqfIDLPDRFcTGSSIMPQKKNPDVPELVRGKSGRVFG---ALT-----GLLTL--M 315
Cdd:COG0114 295 iRwlasgprcgLGE------------IRLPANE-PGSSIMPGKVNPTQCEALTMVCAQVMGndaAITfagssGNFELnvM 361
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489204969 316 KgqPL-AYNkdnqedkepLFDAADTLRDSLRAFAD-MVPAIRPRREIMREAARRGFSTATDLA 376
Cdd:COG0114 362 K--PViAYN---------LLQSIRLLADACRSFADkCVAGIEANEERIEELLERSLMLVTALN 413
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
126-291 |
2.19e-05 |
|
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.
Pssm-ID: 176471 [Multi-domain] Cd Length: 436 Bit Score: 46.54 E-value: 2.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 126 LRDEIDTILAEITRLQEGLLGLAEAEADTIMPGFTHLQTAQPVTFGHHLLAWFEMLGRDYERLVDCRkrvNRMPLGSAal 205
Cdd:cd03302 108 IRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLR---DDLRFRGV-- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 206 AGTTYPIQR----------------EITCQLLGFDAVgGNSLDGVSDRDFAIEFCAAASLAMMHLSRFSEELVLWtsAQF 269
Cdd:cd03302 183 KGTTGTQASfldlfegdhdkvealdELVTKKAGFKKV-YPVTGQTYSRKVDIDVLNALSSLGATAHKIATDIRLL--ANL 259
|
170 180
....*....|....*....|...
gi 489204969 270 QFIDLP-DRFCTGSSIMPQKKNP 291
Cdd:cd03302 260 KEVEEPfEKGQIGSSAMPYKRNP 282
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
131-375 |
1.77e-04 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 43.76 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 131 DTILAEITRLQEGLLGLAEAEADTIMPGFTHLQTAQPVTFGHHLLAWFEMLGRDYERLVDCRKRVNRMPLGSAALA-GTT 209
Cdd:PRK12425 156 EQLLPAIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGtGLN 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 210 YP--IQREITCQLLGFDAV----GGNSLDGVSDRDFAIEFCAAASLAMMHLSRFSEELVLWTS---AQFQFIDLPDRFcT 280
Cdd:PRK12425 236 APhgFAEAIAAELAALSGLpfvtAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSgprAGLAEVRLPANE-P 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 281 GSSIMPQKKNPDVPELVRGKSGRV--------FGALTGLLTLMKGQP-LAYNkdnqedkepLFDAADTLRDSLRAFAD-M 350
Cdd:PRK12425 315 GSSIMPGKVNPTQCEALSMLACQVmgndatigFAASQGHLQLNVFKPvIIHN---------LLQSIRLLADGCRNFQQhC 385
|
250 260
....*....|....*....|....*
gi 489204969 351 VPAIRPRREIMREAARRGFSTATDL 375
Cdd:PRK12425 386 VAGLEPDAEQMAAHLERGLMLVTAL 410
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
281-443 |
1.90e-04 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 42.71 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 281 GSSIMPQKKNPDVPELVrgksgrvfgalTGLLTLMKGQPLAYNKDNQEDKEP-----------LFDAADTLRDSLRAFAD 349
Cdd:PRK08937 58 GSSAMPHKRNPIGSERI-----------TGLARVLRSYLVTALENVPLWHERdlshssaeriaLPDAFLALDYILNRFVN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489204969 350 MVPAIRPRREIMREAARR--GFSTATDLADYLVRKGLPFRDCHEIVG-HAVKyGVDSGKDLAEMSLDElRRFSEQIDADV 426
Cdd:PRK08937 127 ILENLVVFPENIERNLDKtlGFIATERVLLELVEKGMGREEAHELIReKAME-AWKNQKDLRELLEAD-ERFTKQLTKEE 204
|
170
....*....|....*..
gi 489204969 427 FDVLtlegsVNARDHIG 443
Cdd:PRK08937 205 LDEL-----FDPEAFVG 216
|
|
| |
