|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
4-462 |
0e+00 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 860.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 4 DKTNQSWGGRFSEPVDAFVARFTASVDFDKRLYRHDIMGSIAHATMLAQVGVLTDAERDAIIDGLKTIQGEIEAGSFDWR 83
Cdd:PRK00855 1 MMSNKLWGGRFSEGPDELVERFTASISFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILEEIEAGKFEFS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 84 VDLEDVHMNIEARLTDRIGITGKKLHTGRSRNDQVATDIRLWLRDEIDLILAEITRLQQGLLEQAEREAETIMPGFTHLQ 163
Cdd:PRK00855 81 PELEDIHMAIEARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 164 TAQPVTFGHHLLAWFEMLSRDYERLVDCRKRTNRMPLGSAALAGTTYPIDRELTCKLLGFEAVAGNSLDGVSDRDFAIEF 243
Cdd:PRK00855 161 RAQPVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAALAGTTFPIDRERTAELLGFDGVTENSLDAVSDRDFALEF 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 244 CAAASLAMMHLSRFSEELVLWTSAQFQFIDLPDRFCTGSSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYN 323
Cdd:PRK00855 241 LSAASLLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLAYN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 324 KDNQEDKEPLFDAADTLRDSLRAFADMIPAIKPKHAIMREAALRGFSTATDLADYLVRRGLPFRDCHEIVGHAVKYGVDT 403
Cdd:PRK00855 321 RDLQEDKEPLFDAVDTLKLSLEAMAGMLETLTVNKERMREAAGKGFSTATDLADYLVRKGVPFREAHEIVGKAVREAEER 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1092625622 404 GKDLAEMSLDELRQFSDQIEQDVFAVLTLEGSVNARNHIGGTAPAQVRAAVARGKALLA 462
Cdd:PRK00855 401 GVDLADLSLEELQAFSPLITEDVYEVLTPEGSVAARNSIGGTAPEQVREQIARAKARLA 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: 841.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 5 KTNQSWGGRFSEPVDAFVARFTASVDFDKRLYRHDIMGSIAHATMLAQVGVLTDAERDAIIDGLKTIQGEIEAGSFDWRV 84
Cdd:COG0165 1 MSMKLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAFEFDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 85 DLEDVHMNIEARLTDRIGITGKKLHTGRSRNDQVATDIRLWLRDEIDLILAEITRLQQGLLEQAEREAETIMPGFTHLQT 164
Cdd:COG0165 81 ELEDIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 165 AQPVTFGHHLLAWFEMLSRDYERLVDCRKRTNRMPLGSAALAGTTYPIDRELTCKLLGFEAVAGNSLDGVSDRDFAIEFC 244
Cdd:COG0165 161 AQPVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 245 AAASLAMMHLSRFSEELVLWTSAQFQFIDLPDRFCTGSSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYNK 324
Cdd:COG0165 241 SAASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 325 DNQEDKEPLFDAADTLRDSLRAFADMIPAIKPKHAIMREAALRGFSTATDLADYLVRRGLPFRDCHEIVGHAVKYGVDTG 404
Cdd:COG0165 321 DLQEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGFSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKG 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 405 KDLAEMSLDELRQFSDQIEQDVFAVLTLEGSVNARNHIGGTAPAQVRAAVARGKALLASR 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: 711.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 28 SVDFDKRLYRHDIMGSIAHATMLAQVGVLTDAERDAIIDGLKTIQGEIEAGSFDWRVDLEDVHMNIEARLTDRIGITGKK 107
Cdd:cd01359 1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGDVGGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 108 LHTGRSRNDQVATDIRLWLRDEIDLILAEITRLQQGLLEQAEREAETIMPGFTHLQTAQPVTFGHHLLAWFEMLSRDYER 187
Cdd:cd01359 81 LHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 188 LVDCRKRTNRMPLGSAALAGTTYPIDRELTCKLLGFEAVAGNSLDGVSDRDFAIEFCAAASLAMMHLSRFSEELVLWTSA 267
Cdd:cd01359 161 LADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 268 QFQFIDLPDRFCTGSSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYNKDNQEDKEPLFDAADTLRDSLRAF 347
Cdd:cd01359 241 EFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 348 ADMIPAIKPKHAIMREAALRGFSTATDLADYLVR-RGLPFRDCHEIVGHAVKYGVDTGKDLAEMSLDELRQFSDQIEQDV 426
Cdd:cd01359 321 TGVISTLTVNPERMREAAEAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEEDV 400
|
410 420 430
....*....|....*....|....*....|....*
gi 1092625622 427 FAVLTLEGSVNARNHIGGTAPAQVRAAVARGKALL 461
Cdd:cd01359 401 REALDPENSVERRTSYGGTAPAEVREQIARARALL 435
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
10-462 |
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: 662.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 10 WGGRFSEPVDAFVARFTASVDFDKRLYRHDIMGSIAHATMLAQVGVLTDAERDAIIDGLKTIQGEIEAGSFDWRVDLEDV 89
Cdd:TIGR00838 2 WGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPFILDPDDEDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 90 HMNIEARLTDRIGI-TGKKLHTGRSRNDQVATDIRLWLRDEIDLILAEITRLQQGLLEQAEREAETIMPGFTHLQTAQPV 168
Cdd:TIGR00838 82 HMAIERELIDRVGEdLGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 169 TFGHHLLAWFEMLSRDYERLVDCRKRTNRMPLGSAALAGTTYPIDRELTCKLLGFEAVAGNSLDGVSDRDFAIEFCAAAS 248
Cdd:TIGR00838 162 TLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFVAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 249 LAMMHLSRFSEELVLWTSAQFQFIDLPDRFCTGSSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYNKDNQE 328
Cdd:TIGR00838 242 LIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 329 DKEPLFDAADTLRDSLRAFADMIPAIKPKHAIMREAALRGFSTATDLADYLVRRGLPFRDCHEIVGHAVKYGVDTGKDLA 408
Cdd:TIGR00838 322 DKEPLFDALKTVELSLEMATGMLDTITVNKERMEEAASAGFSNATELADYLVRKGVPFREAHHIVGELVATAIERGKGLE 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1092625622 409 EMSLDELRQFSDQIEQDVFAVLTLEGSVNARNHIGGTAPAQVRAAVARGKALLA 462
Cdd:TIGR00838 402 ELTLEELQKFSPEFDEDVYEALDPESSVEKRDAKGGTAPEEVLQAIAEAKARLG 455
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
3-450 |
0e+00 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 615.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 3 TDKTNQSWGGRFSEPVDAFVARFTASVDFDKRLYRHDIMGSIAHATMLAQVGVLTDAERDAIIDGLKTIQGEIEAGSFDW 82
Cdd:PLN02646 12 AAKEKKLWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAGKFEW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 83 RVDLEDVHMNIEARLTDRIGITGKKLHTGRSRNDQVATDIRLWLRDEIDLILAEITRLQQGLLEQAEREAETIMPGFTHL 162
Cdd:PLN02646 92 RPDREDVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 163 QTAQPVTFGHHLLAWFEMLSRDYERLVDCRKRTNRMPLGSAALAGTTYPIDRELTCKLLGFEAVAGNSLDGVSDRDFAIE 242
Cdd:PLN02646 172 QRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRDFVLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 243 FCAAASLAMMHLSRFSEELVLWTSAQFQFIDLPDRFCTGSSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAY 322
Cdd:PLN02646 252 FLFANSITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTAY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 323 NKDNQEDKEPLFDAADTLRDSLRAFADMIPAIKPKHAIMREAALRGFSTATDLADYLVRRGLPFRDCHEIVGHAVKYGVD 402
Cdd:PLN02646 332 NRDLQEDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLDATTLADYLVRKGVPFRETHHIVGAAVALAES 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1092625622 403 TGKDLAEMSLDELRQFSDQIEQDVFAVLTLEGSVNARNHIGGTAPAQV 450
Cdd:PLN02646 412 KGCELSDLTLEDLKSINPVFEEDVYEVLGVENSVEKFDSYGSTGSRSV 459
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
10-459 |
0e+00 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 574.24 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 10 WGGRFSEPVDAFVARFTASVDFDKRLYRHDIMGSIAHATMLAQVGVLTDAERDAIIDGLKTIQGEIEAGSFD-WRVDLED 88
Cdd:PRK04833 4 WGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQQQLEEALNELLEEVRANPQQiLASDAED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 89 VHMNIEARLTDRIGITGKKLHTGRSRNDQVATDIRLWLRDEIDLILAEITRLQQGLLEQAEREAETIMPGFTHLQTAQPV 168
Cdd:PRK04833 84 IHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRAQPV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 169 TFGHHLLAWFEMLSRDYERLVDCRKRTNRMPLGSAALAGTTYPIDRELTCKLLGFEAVAGNSLDGVSDRDFAIEFCAAAS 248
Cdd:PRK04833 164 TFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSDAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 249 LAMMHLSRFSEELVLWTSAQFQFIDLPDRFCTGSSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYNKDNQE 328
Cdd:PRK04833 244 ISMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPLAYNKDMQE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 329 DKEPLFDAADTLRDSLRAFADMIPAIKPKHAIMREAALRGFSTATDLADYLVRRGLPFRDCHEIVGHAVKYGVDTGKDLA 408
Cdd:PRK04833 324 DKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPLE 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1092625622 409 EMSLDELRQFSDQIEQDVFAVLTLEGSVNARNHIGGTAPAQVRAAVARGKA 459
Cdd:PRK04833 404 DLPLAELQKFSSVIGDDVYPILSLQSCLDKRAAKGGVSPQQVAQAIAAAKA 454
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
10-464 |
1.97e-179 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 515.49 E-value: 1.97e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 10 WGGRFSEPVDAFVARFTASVDFDKRLYRHDIMGSIAHATMLAQVGVLTDAERDAIIDGLKTIQGEIEAGSFD-WRVDLED 88
Cdd:PRK12308 4 WGGRFSQAADTRFKQFNDSLRFDYRLAEQDIVGSIAWSKALLSVGVLSEEEQQKLELALNELKLEVMEDPEQiLLSDAED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 89 VHMNIEARLTDRIGITGKKLHTGRSRNDQVATDIRLWLRDEIDLILAEITRLQQGLLEQAEREAETIMPGFTHLQTAQPV 168
Cdd:PRK12308 84 IHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 169 TFGHHLLAWFEMLSRDYERLVDCRKRTNRMPLGSAALAGTTYPIDRELTCKLLGFEAVAGNSLDGVSDRDFAIEFCAAAS 248
Cdd:PRK12308 164 TFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGSGALAGTAYPIDREALAHNLGFRRATRNSLDSVSDRDHVMELMSVAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 249 LAMMHLSRFSEELVLWTSAQFQFIDLPDRFCTGSSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYNKDNQE 328
Cdd:PRK12308 244 ISMLHLSRLAEDLIFYNSGESGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKDMQE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 329 DKEPLFDAADTLRDSLRAFADMIPAIKPKHAIMREAALRGFSTATDLADYLVRRGLPFRDCHEIVGHAVKYGVDTGKDLA 408
Cdd:PRK12308 324 DKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANATELADYLVAKGIPFREAHHIVGVAVVGAIAKGCALE 403
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1092625622 409 EMSLDELRQFSDQIEQDVFAVLTLEGSVNARNHIGGTAPAQVRAAVARGKALLASR 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 |
7.20e-144 |
|
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: 414.21 E-value: 7.20e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 36 YRHDIMGSIAHATMLAQVGVLTDAERDAIIDGLKTIQGEIEAGSFDWRVDLEDVHMNIEARLTDRIG-ITGKKLHTGRSR 114
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVEQEGSGTHDVMAVEEVLAERAGeLNGGYVHTGRSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 115 NDQVATDIRLWLRDEIDLILAEITRLQQGLLEQAEREAETIMPGFTHLQTAQPVTFGHHLLAWFEMLSRDYERLVDCRKR 194
Cdd:cd01334 81 NDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 195 TNRMPLGSAALAGTTY--PIDRELTCKLLGFEAVAGNSLDGVSDRDFAIEFCAAASLAMMHLSRFSEELVLWTSAQFQFI 272
Cdd:cd01334 161 LNVLPLGGGAVGTGANapPIDRERVAELLGFFGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 273 DLPDRFCTGSSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYNKDNQEDKEPLFDAADTLRDSLRAFADMIP 352
Cdd:cd01334 241 ELPDAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVLE 320
|
....
gi 1092625622 353 AIKP 356
Cdd:cd01334 321 GLEV 324
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
12-306 |
1.72e-87 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 270.01 E-value: 1.72e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 12 GRFSEPVDAFVARFTASVDFDKRLYRHDIMGSIAHATMLAQVGVLTDAERDAIIDGLKTIQGEIEAGS-FDWRVDLEDVH 90
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDDqFPLKVWQEGSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 91 MNIEARLTDRIGI-------TGKKLHTGRSRNDQVATDIRLWLRDEI-DLILAEITRLQQGLLEQAEREAETIMPGFTHL 162
Cdd:pfam00206 81 TAVNMNLNEVIGEllgqlvhPNDHVHTGQSSNDQVPTALRLALKDALsEVLLPALRQLIDALKEKAKEFADIVKPGRTHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 163 QTAQPVTFGHHLLAWFEMLSRDYERLVDCRKRTNRMPLGSAALAGTTYPIDRE---LTCKLLGFEA----VAGNSLDGVS 235
Cdd:pfam00206 161 QDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEfaeLVAKELGFFTglpvKAPNSFEATS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092625622 236 DRDFAIEFCAAASLAMMHLSRFSEELVLWTSAQFQFIDLPDRFCT-GSSIMPQKKNPDVPELVRGKSGRVFG 306
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEpGSSIMPGKVNPDQLELLTGKAGRVMG 312
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
45-462 |
1.96e-70 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 239.75 E-value: 1.96e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 45 AHATMLAQVGVLTDAERDAIIDGLKTIQgeiEAG--SFDWRVDLEDVHMNIEARLTDRIGI-TGKKLHTGRSRNDQVATD 121
Cdd:PRK02186 447 AHLVMLGDTGIVAPERARPLLDAHRRLR---DAGfaPLLARPAPRGLYMLYEAYLIERLGEdVGGVLQTARSRNDINATT 523
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 122 IRLWLRDEIDLILAEITRLQQGLLEQAEREAETIMPGFTHLQTAQPVTFGHHLLAWFEMLSRDYERLVDCRKRTNRMPLG 201
Cdd:PRK02186 524 TKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHALFALFEHIDVCPLG 603
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 202 SAALAGTTYPIDRELTCKLLGFEAVAGNSLDGVSDRDFAIEFCAAASLAMMHLSRFSEELVLWTSAQFQFIDLPDRFCTG 281
Cdd:PRK02186 604 AGAGGGTTFPIDPEFVARLLGFEQPAPNSLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQLWTTREFALVSLPDALTGG 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 282 SSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYNKD-NQEDKEPLFDAADTLRDSLRAFADMIPAIKPKHAI 360
Cdd:PRK02186 684 SSMLPQKKNPFLLEFVKGRAGVVAGALASASAALGKTPFSNSFEaGSPMNGPIAQACAAIEDAAAVLVLLIDGLEADQAR 763
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 361 MREAALRGFSTATDLADYLV-RRGLPFRDCHEIVGHAVKYGVDTGKDLAEmSLDELrqfsdqiEQDVFAVLTLEGsvnAR 439
Cdd:PRK02186 764 MRAHLEDGGVSATAVAESLVvRRSISFRSAHTQVGQAIRQSLDQGRSSAD-ALAAL-------DPQFVSRAPLEW---AR 832
|
410 420
....*....|....*....|....*
gi 1092625622 440 NHIGGTAP--AQVRAAVARGKALLA 462
Cdd:PRK02186 833 SHRFGGGPgaADLNAGLARACAALR 857
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
91-348 |
2.51e-65 |
|
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: 209.77 E-value: 2.51e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 91 MNIEARLTDRIGITGKKLH------TGRSRNDQVATDIRLWLRDEIDLILAEITRLQQGLLEQAEREAETIMPGFTHLQT 164
Cdd:cd01594 14 ALVEEVLAGRAGELAGGLHgsalvhKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 165 AQPVTFGHHLLAWFEMLSRDYERLVDCrkrtnrmplgsaalagttypidreltckllgfeavagnsldgvsdrdFAIEFC 244
Cdd:cd01594 94 AQPVTLGYELRAWAQVLGRDLERLEEA-----------------------------------------------AVAEAL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 245 AAASLAMMHLSRFSEELVLWTSAQFQFIDLPD-RFCTGSSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYN 323
Cdd:cd01594 127 DALALAAAHLSKIAEDLRLLLSGEFGELGEPFlPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDN 206
|
250 260
....*....|....*....|....*
gi 1092625622 324 KDNQEDKEPLFDAADTLRDSLRAFA 348
Cdd:cd01594 207 EDSPSMREILADSLLLLIDALRLLL 231
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
45-461 |
3.51e-55 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 191.35 E-value: 3.51e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 45 AHATMLAQVGVLTDAERDAIIDGLKTIQGeIEAGSFDWRVDLEDVHMNIEARLTDRIGI-TGKKLHTGRSRNDQVATDIR 123
Cdd:PRK06705 47 AHIVMLTEENLMKKEEAKFILHALKKVEE-IPEEQLLYTEQHEDLFFLVEHLISQEAKSdFVSNMHIGRSRNDMGVTMYR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 124 LWLRDEIDLILAEITRLQQGLLEQAEREAETIMPGFTHLQTAQPVTFGHHLLAWFEMLSRDYERLVDCRKRTNRMPLGSA 203
Cdd:PRK06705 126 MSLRRYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKTYKLLNQSPMGAA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 204 ALAGTTYPIDRELTCKLLGFEAVAGNSLDGVSDRDFAIEFCAAASLAMMHLSRFSEELVLWTSAQFQFIDLPDRFCTGSS 283
Cdd:PRK06705 206 ALSTTSFPIKRERVADLLGFTNVIENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLATKEYDGITVARPYVQISS 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 284 IMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYNKDNQEDKEP-LFDAadtLRDSLRAFADM---IPAIKPKHA 359
Cdd:PRK06705 286 IMPQKRNPVSIEHARAITSSALGEAFTVFQMIHNTPFGDIVDTEDDLQPyLYKG---IEKAIRVFCIMnavIRTMKVEED 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 360 IMREAALRGFSTATDLADYLVRR-GLPFRDCHEIVGHAVKYGVDTGKDLAEMSLDELRQFSDQ------IEQDVFAVLTL 432
Cdd:PRK06705 363 TLKRRSYKHAITITDFADVLTKNyGIPFRHAHHAASVIANMSLEQKKELHELCFKDVNIYLQEkfkiqlLEKEWEEIISP 442
|
410 420
....*....|....*....|....*....
gi 1092625622 433 EGSVNARNHIGGTAPAQVRAAVARGKALL 461
Cdd:PRK06705 443 EAFIQKRNVYGGPSKKEMERMINNRKELF 471
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
16-402 |
1.19e-36 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 139.64 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 16 EPVDAFVARftaSVDFDKRLYRHDIMGSIAHATMLAQVGVLTDAERDAIIDGL-KTIQGEIEAgsfdwRVDLEDVHMNIE 94
Cdd:PRK06389 15 DFYDNIVKD---DIDADKNLIKYEIINLLAYHVALAQRRLITEKAPKCVINALiDIYKNGIEI-----DLDLEDVHTAIE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 95 ARLTDRIGITGKKLHTGRSRNDQVATDIRLWLRD---EIDLILAEITRLQQGLleqaerEAETIMPGFTHLQTAQPVTFG 171
Cdd:PRK06389 87 NFVIRRCGDMFKNFRLFLSRNEQVHADLNLFIIDkiiEIEKILYEIIKVIPGF------NLKGRLPGYTHFRQAMPMTVN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 172 HHLLAWFEMLSRDYERLVDCRKRTNRMPLGSAALAGTTYPIDRELTCKLLGFEAVAGNSLDGVSDRDFAI-EFCAAASLA 250
Cdd:PRK06389 161 TYINYIKSILYHHINNLDSFLMDLREMPYGYGSGYGSPSSVKFNQMSELLGMEKNIKNPVYSSSLYIKTIeNISYLISSL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 251 MMHLSRFSEELVLWTSAQFqfIDLPDRFCTGSSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKGQPLAYNKDNQEDK 330
Cdd:PRK06389 241 AVDLSRICQDIIIYYENGI--ITIPDEFTTGSSLMPNKRNPDYLELFQGIAAESISVLSFIAQSELNKTTGYHRDFQIVK 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092625622 331 EPLFDAADTLRDSLRAFADMIPAIKPKhaIMREAALRGFSTATDLADYLVRRGLPFRDCHEIVGHAVKYGVD 402
Cdd:PRK06389 319 DSTISFINNFERILLGLPDLLYNIKFE--ITNEKNIKNSVYATYNAWLAFKNGMDWKSAYAYIGNKIREGEV 388
|
|
| ASL_C2 |
pfam14698 |
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of ... |
369-436 |
5.46e-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: 119.06 E-value: 5.46e-33
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092625622 369 FSTATDLADYLVRRGLPFRDCHEIVGHAVKYGVDTGKDLAEMSLDELRQFSDQIEQDVFAVLTLEGSV 436
Cdd:pfam14698 1 FSTATDLADYLVRKGVPFREAHEIVGRLVRLAEEKGKDLEDLTLEELQAISPLFEEDVYEALDPEASV 68
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
111-414 |
3.70e-26 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 110.46 E-value: 3.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 111 GRSRNDQVATDIRLWLRDEIDLILAEITRLQQGLLEQAEREAETIMPGFTHLQTAQPVTFGHHLLAWFEMLSRDYERLVD 190
Cdd:PRK13353 138 AQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQ 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 191 CRKRTNRMPLGSAALaGTTYPIDRELTCKLLG-FEAVAG-------NSLDGVSDRDFAIEFCAAASLAMMHLSRFSEELV 262
Cdd:PRK13353 218 AREHLYEVNLGGTAV-GTGLNADPEYIERVVKhLAAITGlplvgaeDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 263 LWTS---AQFQFIDLPDRFCtGSSIMPQKKNPDVPELVRGKSGRVFG--------ALTGLLTLMKGQPL-AYNkdnqedk 330
Cdd:PRK13353 297 LLSSgprTGLGEINLPAVQP-GSSIMPGKVNPVMPEVVNQIAFQVIGndvtitlaAEAGQLELNVMEPViAFN------- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 331 epLFDAADTLRDSLRAFAD-MIPAIKPKHAIMREAALRGFSTATDLADYLvrrGlpfrdcHEIVGHAVKYGVDTGKDLAE 409
Cdd:PRK13353 369 --LLESISILTNACRAFTDnCVKGIEANEERCKEYVEKSVGIATALNPHI---G------YEAAARIAKEAIATGRSVRE 437
|
....*
gi 1092625622 410 MSLDE 414
Cdd:PRK13353 438 LALEN 442
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
74-315 |
1.40e-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: 104.89 E-value: 1.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 74 EIEAGSFDWRVDLEDVHmNIEAR-----------LTDRIGITGKK-LHTGRSRNDQVATDIRLWLRDEIDLILAEITRLQ 141
Cdd:cd01595 38 EIRAAADVFEIDAERIA-EIEKEtghdviafvyaLAEKCGEDAGEyVHFGATSQDINDTALALQLRDALDIILPDLDALI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 142 QGLLEQAEREAETIMPGFTHLQTAQPVTFGHHLLAWFEMLSRDYERLVDCRKRTNRM----PLGSAALAGTTYPIDRELT 217
Cdd:cd01595 117 DALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGgisgAVGTHASLGPKGPEVEERV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 218 CKLLGF--EAVAGNsldgVSDRDFAIEFCAAasLAMMH--LSRFSEELVLWTSAQFQFIDLP-DRFCTGSSIMPQKKNPD 292
Cdd:cd01595 197 AEKLGLkvPPITTQ----IEPRDRIAELLSA--LALIAgtLEKIATDIRLLQRTEIGEVEEPfEKGQVGSSTMPHKRNPI 270
|
250 260
....*....|....*....|...
gi 1092625622 293 VPELVRGKSGRVFGALTGLLTLM 315
Cdd:cd01595 271 DSENIEGLARLVRALAAPALENL 293
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
51-414 |
5.14e-22 |
|
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: 97.98 E-value: 5.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 51 AQVGVLTDAERDAIIDGLKtiqgEIEAGSFD--WRVDL------EDVHMNIEARLTDR-IGITGKK------LH------ 109
Cdd:cd01357 56 AELGLLDEEKAEAIVKACD----EIIAGKLHdqFVVDViqggagTSTNMNANEVIANRaLELLGHEkgeyqyVHpndhvn 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 110 TGRSRNDQVATDIRLWLRDEIDLILAEITRLQQGLLEQAEREAETIMPGFTHLQTAQPVTFGHHLLAWFEMLSRDYERLV 189
Cdd:cd01357 132 MSQSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIY 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 190 DCRKRTNRMPLGSAALaGT---TYPIDRELTCKLL----GFE-AVAGNSLDGVSDRDFAIEFCAAASLAMMHLSRFSEEL 261
Cdd:cd01357 212 KARERLREVNLGGTAI-GTginAPPGYIELVVEKLseitGLPlKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDL 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 262 VLWTS---AQFQFIDLPDRfCTGSSIMPQKKNPDVPELVRGKSGRVFG---ALT-----GLLTLMKGQPL-AYNkdnqed 329
Cdd:cd01357 291 RLLSSgprAGLGEINLPAV-QPGSSIMPGKVNPVIPEVVNQVAFQVIGndlTITmaaeaGQLELNVFEPViAYN------ 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 330 kepLFDAADTLRDSLRAFAD-MIPAIKPKHAIMREAALRGFSTATDLADYLvrrGlpfrdcHEIVGHAVKYGVDTGKDLA 408
Cdd:cd01357 364 ---LLESIDILTNAVRTLRErCIDGITANEERCREYVENSIGIVTALNPYI---G------YEAAAEIAKEALETGRSVR 431
|
....*.
gi 1092625622 409 EMSLDE 414
Cdd:cd01357 432 ELVLEE 437
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
105-456 |
3.61e-21 |
|
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: 95.39 E-value: 3.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 105 GKKLHTGRSRNDQVATDIRLWLRDEIDLILAEITRLQQGLLEQAEREAETIMPGFTHLQTAQPVTFGHHLLAWFEMLSRD 184
Cdd:cd01597 90 GEYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRH 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 185 YERLVDCRKRTNRMPLGSAA--LA--GTTYPIDRELTCKLLGFEAVAGNSLdgvSDRDFAIEFcaAASLAMMH--LSRFS 258
Cdd:cd01597 170 RERLDELRPRVLVVQFGGAAgtLAslGDQGLAVQEALAAELGLGVPAIPWH---TARDRIAEL--ASFLALLTgtLGKIA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 259 EELVLWTSAQFQFIDLPDRFCTG-SSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMKgqplaynKDNQEDKEPLFDAA 337
Cdd:cd01597 245 RDVYLLMQTEIGEVAEPFAKGRGgSSTMPHKRNPVGCELIVALARRVPGLAALLLDAMV-------QEHERDAGAWHAEW 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 338 DTLRDSLRAFA-------DMIPAIKPKHAIMRE--AALRGF----STATDLADYLVRrglpfRDCHEIVGHAVKYGVDTG 404
Cdd:cd01597 318 IALPEIFLLASgaleqaeFLLSGLEVNEDRMRAnlDLTGGLilseAVMMALAPKLGR-----QEAHDLVYEACMRAVEEG 392
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1092625622 405 KDLAEmsldELRQfsdqiEQDVFAVLT---LEGSVNARNHIgGTAPAQVRAAVAR 456
Cdd:cd01597 393 RPLRE----VLLE-----DPEVAAYLSdeeLDALLDPANYL-GSAPALVDRVLAR 437
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
126-453 |
5.74e-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: 91.68 E-value: 5.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 126 LRDEIDLILAEITRLQQGLLEQAEREAETIMPGFTHLQTAQPVTFGHHLLAWFEMLSRDYERLVDCRKrtnRMPLGsaAL 205
Cdd:COG0015 111 LREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARE---RVLVG--KI 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 206 AGT--TY--------PIDRELTCKL-LGFEAVAGnsldGVSDRDFAIEFCAAASLAMMHLSRFSEELVLWTSAQ----FQ 270
Cdd:COG0015 186 GGAvgTYaahgeawpEVEERVAEKLgLKPNPVTT----QIEPRDRHAELFSALALIAGSLEKIARDIRLLQRTEvgevEE 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 271 FIDlPDRfcTGSSIMPQKKNPDVPELVRGKSGRVFGALTGLLTLMkgqplaynkdNQEDKEPLFDAA---DTLRDS---- 343
Cdd:COG0015 262 PFA-KGQ--VGSSAMPHKRNPIDSENIEGLARLARALAAALLEAL----------ASWHERDLSDSSverNILPDAflll 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 344 ---LRAFADMIPAIKPKHAIMRE--AALRGFSTATDLADYLVRRGLPFRDCHEIVGHAVKYGVDTGKDLAEMsLDELRQF 418
Cdd:COG0015 329 dgaLERLLKLLEGLVVNPERMRAnlDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAWEEGNDLREL-LAADPEI 407
|
330 340 350
....*....|....*....|....*....|....*
gi 1092625622 419 SDQIEQDvfavlTLEGSVNARNHIgGTAPAQVRAA 453
Cdd:COG0015 408 PAELSKE-----ELEALFDPANYL-GAADEIVDRV 436
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
97-291 |
8.15e-20 |
|
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: 90.69 E-value: 8.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 97 LTDRIGITGKKLHTGRSRNDQVATDIRLWLRDEIDLILAEITRLQQGLLEQAEREAETIMPGFTHLQTAQPVTFGHHLLA 176
Cdd:cd01360 74 IAEYCGEAGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFAL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 177 WFEMLSRDYERLVDCRKRTNRM----PLGSAALAGttyPIDRELTCKLLGFEAVAGNSldGVSDRDFAIEFCA-----AA 247
Cdd:cd01360 154 WYAEFKRHLERLKEARERILVGkisgAVGTYANLG---PEVEERVAEKLGLKPEPIST--QVIQRDRHAEYLStlaliAS 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1092625622 248 SLAMM-----HLSRfSEelVLWTSAQFqfidlpDRFCTGSSIMPQKKNP 291
Cdd:cd01360 229 TLEKIateirHLQR-TE--VLEVEEPF------SKGQKGSSAMPHKRNP 268
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
113-414 |
7.35e-19 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 88.57 E-value: 7.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 113 SRNDQVATDIRLWLRDEIDLILAEITRLQQGLLEQAEREAETIMPGFTHLQTAQPVTFGHHLLAWFEMLSRDYERLVDCR 192
Cdd:COG1027 137 STNDVYPTAIRLALLLLLRELLEALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 193 KRTNRMPLGSAAlAGT---TYPIDRELTCKLL----GFE-AVAGNSLDGVSDRDFAIEFCAAASLAMMHLSRFSEELVLW 264
Cdd:COG1027 217 ELLREVNLGGTA-IGTglnAPPGYIELVVEHLaeitGLPlVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 265 TS---AQFQFIDLPDRfCTGSSIMPQKKNPDVPELVRGKSGRVFGA-LTglLTLM--KGQ-------PL-AYNkdnqedk 330
Cdd:COG1027 296 SSgprAGLGEINLPAV-QPGSSIMPGKVNPVIPEVVNQVAFQVIGNdLT--VTMAaeAGQlelnvfePViAYN------- 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 331 epLFDAADTLRDSLRAFADM-IPAIKPKHAIMREAALRGFSTATDLADYLvrrGlpfrdcHEIVGHAVKYGVDTGKDLAE 409
Cdd:COG1027 366 --LLESIELLTNACRTLREKcIDGITANEERCREYVENSIGLVTALNPYI---G------YEKAAEIAKEALATGKSVRE 434
|
....*
gi 1092625622 410 MSLDE 414
Cdd:COG1027 435 LVLEK 439
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
41-414 |
9.14e-18 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 85.56 E-value: 9.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 41 MGSIAHATMLA--QVGVLTDAERDAIIDGLKtiqgEIEAGSFD--WRVDL------EDVHMNIEARLTDR-IGITGKK-- 107
Cdd:PRK12273 51 LAMVKKAAALAnkELGLLDEEKADAIVAACD----EILAGKLHdqFVVDViqggagTSTNMNANEVIANRaLELLGHEkg 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 108 ----LH------TGRSRNDQVATDIRLWLRDEIDLILAEITRLQQGLLEQAEREAETIMPGFTHLQTAQPVTFGHHLLAW 177
Cdd:PRK12273 127 eyqyVHpndhvnMSQSTNDAYPTAIRIALLLSLRKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAY 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 178 FEMLSRDYERLVDCRKRTNRMPLGSAAlAGT---TYPIDRELTCKLL----GFE-AVAGNSLDGVSDRDFAIEFCAAASL 249
Cdd:PRK12273 207 AVALAEDRKRLYRAAELLREVNLGATA-IGTglnAPPGYIELVVEKLaeitGLPlVPAEDLIEATQDTGAFVEVSGALKR 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 250 AMMHLSRFSEELVLWTS---AQFQFIDLPDRfCTGSSIMPQKKNPDVPELVRGKSGRVFGA-LTglLTLM--KGQ----- 318
Cdd:PRK12273 286 LAVKLSKICNDLRLLSSgprAGLNEINLPAV-QAGSSIMPGKVNPVIPEVVNQVCFQVIGNdTT--VTMAaeAGQlelnv 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 319 --PL-AYNkdnqedkepLFDAADTLRDSLRAFADM-IPAIKPKHAIMREAALRGFSTATDLADYLvrrGlpfrdcHEIVG 394
Cdd:PRK12273 363 mePViAYN---------LFESISILTNACRTLREKcIDGITANEERCREYVENSIGIVTALNPYI---G------YENAA 424
|
410 420
....*....|....*....|
gi 1092625622 395 HAVKYGVDTGKDLAEMSLDE 414
Cdd:PRK12273 425 EIAKEALETGKSVRELVLER 444
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
134-409 |
4.19e-16 |
|
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: 80.16 E-value: 4.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 134 LAEITRLQQGLLEQAEREAETIMPGFTHLQTAQPVTFGHHLLAWFEMLSRDYERLVDCRKRTNRMPLGSAALaGT---TY 210
Cdd:cd01596 156 LPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAV-GTglnAP 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 211 PIDRELTCKLL----GFE-AVAGNSLDGVSDRDFAIEFCAAASLAMMHLSRFSEELVLWTS---AQFQFIDLPDRfCTGS 282
Cdd:cd01596 235 PGYAEKVAAELaeltGLPfVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSgprAGLGEINLPAN-QPGS 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 283 SIMPQKKNPDVPELVRGKSGRVFG---ALT-----GLLTL--MKgqPL-AYNkdnqedkepLFDAADTLRDSLRAFAD-M 350
Cdd:cd01596 314 SIMPGKVNPVIPEAVNMVAAQVIGndtAITmagsaGQLELnvFK--PViAYN---------LLQSIRLLANACRSFRDkC 382
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1092625622 351 IPAIKPKHAIMREAALRGFSTATDLADYLvrrGlpfrdcHEIVGHAVKYGVDTGKDLAE 409
Cdd:cd01596 383 VEGIEANEERCKEYVENSLMLVTALNPHI---G------YEKAAEIAKEALKEGRTLRE 432
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
112-412 |
2.95e-14 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 74.65 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 112 RSRNDQVATDIRLWLRDEIDLILAEITRLQQGLLEQAEREAETIMPGFTHLQTAQPVTFGHHLLAWFEMLSRDYERLVDC 191
Cdd:PRK14515 145 QSTNDAFPTAIHIATLNALEGLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQS 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 192 RKRTNRMPLGSAALaGTTYPIDRELT-------CKLLGFEAVAGNSL-DGVSDRDFAIEFCAAASLAMMHLSRFSEELVL 263
Cdd:PRK14515 225 RQHLYEVNMGATAV-GTGLNADPEYIeavvkhlAAISELPLVGAEDLvDATQNTDAYTEVSAALKVCMMNMSKIANDLRL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 264 WTS---AQFQFIDLPDRfCTGSSIMPQKKNPDVPELVRGKSGRVFG--------ALTGLLTLMKGQP-LAYNkdnqedke 331
Cdd:PRK14515 304 MASgprVGLAEIMLPAR-QPGSSIMPGKVNPVMPEVINQIAFQVIGndhticlaSEAGQLELNVMEPvLVFN-------- 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 332 pLFDAADTLRDSLRAFAD-MIPAIKPKHAIMREAALRGFSTATDLADYLvrrglpfrdCHEIVGHAVKYGVDTGKDLAEM 410
Cdd:PRK14515 375 -LLQSISIMNNGFRAFTDnCLKGIEANEDRLKEYVEKSVGIITAVNPHI---------GYEAAARVAKEAIATGQSVREL 444
|
..
gi 1092625622 411 SL 412
Cdd:PRK14515 445 CV 446
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
95-420 |
3.71e-12 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 68.12 E-value: 3.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 95 ARLTDRIGITGKKLHTGRSRNDQVATDIRLWLRDEIDLILAEITRLQQGLLEQAEREAETIMPGFTHLQTAQPVTFGHHL 174
Cdd:PRK09053 89 AQVAARDAEAARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKF 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 175 LAWFEMLSRDYERLVDCRKRTNRMPLGSAA-----LAGTTYPIDRELTCKL-LGFEAVAGNsldgvSDRDFAIEFCAAAS 248
Cdd:PRK09053 169 AGWLDALLRHRQRLAALRPRALVLQFGGAAgtlasLGEQALPVAQALAAELqLALPALPWH-----TQRDRIAEFASALG 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 249 LAMMHLSRFSEELVLwtSAQFQFIDL-----PDRfcTGSSIMPQKKNPDVPELVRGKSGRVFGALTgllTLMKGQPlayn 323
Cdd:PRK09053 244 LLAGTLGKIARDVSL--LMQTEVGEVfepaaAGK--GGSSTMPHKRNPVGCAAVLTAATRAPGLVA---TLFAAMP---- 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 324 kdnQEDKEPL--FDAA-DTLRD-------SLRAFADMIPAIKPKHAIMRE------AALRGFSTATDLADYLVRrglpfR 387
Cdd:PRK09053 313 ---QEHERALggWHAEwDTLPElaclaagALAQMAQIVEGLEVDAARMRAnldlthGLILAEAVMLALADRIGR-----L 384
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1092625622 388 DCHEIVGHAVKYGVDTGKDL-----------AEMSLDELRQFSD 420
Cdd:PRK09053 385 DAHHLVEQASKRAVAEGRHLrdvlaedpqvsAHLSPAALDRLLD 428
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
51-376 |
8.76e-09 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 57.41 E-value: 8.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 51 AQVGVLTDAERDAIIDGLKtiqgEIEAGSFDWRVDLeDV---------HMNI-E------ARLTDRIGITGKKLH----- 109
Cdd:PRK00485 60 AELGLLDAEKADAIVAAAD----EVIAGKHDDHFPL-DVwqtgsgtqsNMNVnEvianraSELLGGELGSKKPVHpndhv 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 110 -TGRSRNDQVATDIRLWLRDEI--DLILAeITRLQQGLLEQAEREAETIMPGFTHLQTAQPVTFGHHLLAWFEMLSRDYE 186
Cdd:PRK00485 135 nMSQSSNDTFPTAMHIAAVLAIveRLLPA-LEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 187 RLVDCRKRTNRMPLGSAAlAGT---TYP-----IDRELTcKLLGFEAV-AGNSLDGVSDRDFAIEFCAA-ASLA--MMHL 254
Cdd:PRK00485 214 RIEAALPHLYELALGGTA-VGTglnAHPgfaerVAEELA-ELTGLPFVtAPNKFEALAAHDALVEASGAlKTLAvsLMKI 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 255 S---RF---------SEelvlwtsaqfqfIDLPDRFcTGSSIMPQKKNPDVPELVRGKSGRVFG--------ALTGLLTL 314
Cdd:PRK00485 292 AndiRWlasgprcglGE------------ISLPENE-PGSSIMPGKVNPTQCEALTMVCAQVMGndaavtfaGSQGNFEL 358
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1092625622 315 --MKgqPL-AYNkdnqedkepLFDAADTLRDSLRAFAD-MIPAIKPKHAIMREAALRGFSTATDLA 376
Cdd:PRK00485 359 nvFK--PViAYN---------FLQSIRLLADAMRSFADhCVVGIEPNRERIKELLERSLMLVTALN 413
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
126-291 |
8.18e-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: 54.25 E-value: 8.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 126 LRDEIDLILAEITRLQQGLLEQAEREAETIMPGFTHLQTAQPVTFGHHLLAWFEMLSRDYERLVDCRkrtNRMPLGSAal 205
Cdd:cd03302 108 IRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLR---DDLRFRGV-- 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 206 AGTT---------YPIDR-------ELTCKLLGFEAVAgNSLDGVSDRDFAIEFCAAASLAMMHLSRFSEELVLWtsAQF 269
Cdd:cd03302 183 KGTTgtqasfldlFEGDHdkvealdELVTKKAGFKKVY-PVTGQTYSRKVDIDVLNALSSLGATAHKIATDIRLL--ANL 259
|
170 180
....*....|....*....|...
gi 1092625622 270 QFIDLP-DRFCTGSSIMPQKKNP 291
Cdd:cd03302 260 KEVEEPfEKGQIGSSAMPYKRNP 282
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
111-375 |
4.86e-07 |
|
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: 51.73 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 111 GRSRNDQVATDIRLWLRDEI-DLILAEITRLQQGLLEQAEREAETIMPGFTHLQTAQPVTFGHHLLAWFEMLSRDYERLV 189
Cdd:cd01362 133 SQSSNDTFPTAMHIAAALALqERLLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 190 DCRKRTNRMPLGSAALaGT---TYPIDRELTCKLL----GFEAV-AGNSLDGVSDRDFAIEF-----CAAASLamMHLSR 256
Cdd:cd01362 213 AALPRLYELALGGTAV-GTglnAHPGFAEKVAAELaeltGLPFVtAPNKFEALAAHDALVEAsgalkTLAVSL--MKIAN 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 257 fseELVLWTS---AQFQFIDLPDRFcTGSSIMPQKKNPDVPELVRGKSGRVFG--------ALTGLLTL--MKgqPL-AY 322
Cdd:cd01362 290 ---DIRWLGSgprCGLGELSLPENE-PGSSIMPGKVNPTQCEALTMVAAQVMGndaaitiaGSSGNFELnvFK--PViIY 363
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1092625622 323 NkdnqedkepLFDAADTLRDSLRAFAD-MIPAIKPKHAIMREAALRGFSTATDL 375
Cdd:cd01362 364 N---------LLQSIRLLADACRSFADkCVAGIEPNRERIAELLERSLMLVTAL 408
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
133-375 |
2.75e-06 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 49.54 E-value: 2.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 133 ILAEITRLQQGLLEQAEREAETIMPGFTHLQTAQPVTFGHHLLAWFEMLsrdyerlvDCRKRTNRMPL---------GSA 203
Cdd:PRK12425 158 LLPAIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQL--------DYAERAIRAALpavcelaqgGTA 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 204 ALAGTTYP------IDRELTCkLLGFEAV-AGNSLDGVSDRDFAIEFCAAASLAMMHLSRFSEELVLWTS---AQFQFID 273
Cdd:PRK12425 230 VGTGLNAPhgfaeaIAAELAA-LSGLPFVtAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSgprAGLAEVR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 274 LPDRFcTGSSIMPQKKNPDVPELVRGKSGRV--------FGALTGLLTLMKGQP-LAYNkdnqedkepLFDAADTLRDSL 344
Cdd:PRK12425 309 LPANE-PGSSIMPGKVNPTQCEALSMLACQVmgndatigFAASQGHLQLNVFKPvIIHN---------LLQSIRLLADGC 378
|
250 260 270
....*....|....*....|....*....|..
gi 1092625622 345 RAFAD-MIPAIKPKHAIMREAALRGFSTATDL 375
Cdd:PRK12425 379 RNFQQhCVAGLEPDAEQMAAHLERGLMLVTAL 410
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
281-443 |
3.25e-03 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 38.86 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 281 GSSIMPQKKNPDVPELVrgksgrvfgalTGLLTLMKGQPLAYNKDNQEDKEP-----------LFDA----------ADT 339
Cdd:PRK08937 58 GSSAMPHKRNPIGSERI-----------TGLARVLRSYLVTALENVPLWHERdlshssaeriaLPDAflaldyilnrFVN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092625622 340 LRDSLRAFADMIpaikpKHAIMREaalRGFSTATDLADYLVRRGLPFRDCHEIVG-HAVKyGVDTGKDLAEMSLDELRqF 418
Cdd:PRK08937 127 ILENLVVFPENI-----ERNLDKT---LGFIATERVLLELVEKGMGREEAHELIReKAME-AWKNQKDLRELLEADER-F 196
|
170 180
....*....|....*....|....*
gi 1092625622 419 SDQIEQDvfavlTLEGSVNARNHIG 443
Cdd:PRK08937 197 TKQLTKE-----ELDELFDPEAFVG 216
|
|
| |
