|
Name |
Accession |
Description |
Interval |
E-value |
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
13-468 |
0e+00 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 827.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 13 NKAQAWSARFSEPVSDLVKRYTASVDFDKRLARHDIRGSLAHADMLAAQGIISAQDLADIERGMQQILSEIDAGSFQWLL 92
Cdd:PRK00855 2 MSNKLWGGRFSEGPDELVERFTASISFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILEEIEAGKFEFSP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 93 DLEDVHLNIEKRLVELVGDAGKRLHTGRSRNDQVATDIRLWLRDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQV 172
Cdd:PRK00855 82 ELEDIHMAIEARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 173 AQPVTFGHHLLAYAEMFGRDAERLADCRKRVNRLPLGAAALAGTSYPIDRERVASTLGFDGVCRNSLDAVSDRDFAIEFC 252
Cdd:PRK00855 162 AQPVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAALAGTTFPIDRERTAELLGFDGVTENSLDAVSDRDFALEFL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 253 AAASLIMTHVSRLSEELVLWMSPRVGFIDLADRFCTGSSIMPQKKNPDVPELARGKTGRVNGHLVALLTLMKGQPLAYNK 332
Cdd:PRK00855 242 SAASLLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLAYNR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 333 DNQEDKEGLFDTADTLRDTLTIFADMAGGIKVKADNMRAAALQGFATATDLADYLVKRGLPFRDAHEVVAHAVRDCEQRG 412
Cdd:PRK00855 322 DLQEDKEPLFDAVDTLKLSLEAMAGMLETLTVNKERMREAAGKGFSTATDLADYLVRKGVPFREAHEIVGKAVREAEERG 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1478755605 413 CDLADLSLAELQAYHPSIEADIHQVLTLEGSVAARKHTGGTAPERVREEAQRVIQE 468
Cdd:PRK00855 402 VDLADLSLEELQAFSPLITEDVYEVLTPEGSVAARNSIGGTAPEQVREQIARAKAR 457
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
13-464 |
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: 807.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 13 NKAQAWSARFSEPVSDLVKRYTASVDFDKRLARHDIRGSLAHADMLAAQGIISAQDLADIERGMQQILSEIDAGSFQWLL 92
Cdd:COG0165 1 MSMKLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAFEFDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 93 DLEDVHLNIEKRLVELVGDAGKRLHTGRSRNDQVATDIRLWLRDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQV 172
Cdd:COG0165 81 ELEDIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 173 AQPVTFGHHLLAYAEMFGRDAERLADCRKRVNRLPLGAAALAGTSYPIDRERVASTLGFDGVCRNSLDAVSDRDFAIEFC 252
Cdd:COG0165 161 AQPVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 253 AAASLIMTHVSRLSEELVLWMSPRVGFIDLADRFCTGSSIMPQKKNPDVPELARGKTGRVNGHLVALLTLMKGQPLAYNK 332
Cdd:COG0165 241 SAASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNK 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 333 DNQEDKEGLFDTADTLRDTLTIFADMAGGIKVKADNMRAAALQGFATATDLADYLVKRGLPFRDAHEVVAHAVRDCEQRG 412
Cdd:COG0165 321 DLQEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGFSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKG 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1478755605 413 CDLADLSLAELQAYHPSIEADIHQVLTLEGSVAARKHTGGTAPERVREEAQR 464
Cdd:COG0165 401 KDLEDLTLEELQAFSPLIEEDVYEALDPEGSVAARDSYGGTAPEAVREQIAR 452
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
36-464 |
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: 685.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 36 SVDFDKRLARHDIRGSLAHADMLAAQGIISAQDLADIERGMQQILSEIDAGSFQWLLDLEDVHLNIEKRLVELVGDAGKR 115
Cdd:cd01359 1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGDVGGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 116 LHTGRSRNDQVATDIRLWLRDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPVTFGHHLLAYAEMFGRDAER 195
Cdd:cd01359 81 LHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLER 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 196 LADCRKRVNRLPLGAAALAGTSYPIDRERVASTLGFDGVCRNSLDAVSDRDFAIEFCAAASLIMTHVSRLSEELVLWMSP 275
Cdd:cd01359 161 LADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 276 RVGFIDLADRFCTGSSIMPQKKNPDVPELARGKTGRVNGHLVALLTLMKGQPLAYNKDNQEDKEGLFDTADTLRDTLTIF 355
Cdd:cd01359 241 EFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 356 ADMAGGIKVKADNMRAAALQGFATATDLADYLVK-RGLPFRDAHEVVAHAVRDCEQRGCDLADLSLAELQAYHPSIEADI 434
Cdd:cd01359 321 TGVISTLTVNPERMREAAEAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEEDV 400
|
410 420 430
....*....|....*....|....*....|
gi 1478755605 435 HQVLTLEGSVAARKHTGGTAPERVREEAQR 464
Cdd:cd01359 401 REALDPENSVERRTSYGGTAPAEVREQIAR 430
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
18-460 |
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: 622.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 18 WSARFSEPVSDLVKRYTASVDFDKRLARHDIRGSLAHADMLAAQGIISAQDLADIERGMQQILSEIDAGSFQWLLDLEDV 97
Cdd:TIGR00838 2 WGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPFILDPDDEDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 98 HLNIEKRLVELVG-DAGKRLHTGRSRNDQVATDIRLWLRDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPV 176
Cdd:TIGR00838 82 HMAIERELIDRVGeDLGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 177 TFGHHLLAYAEMFGRDAERLADCRKRVNRLPLGAAALAGTSYPIDRERVASTLGFDGVCRNSLDAVSDRDFAIEFCAAAS 256
Cdd:TIGR00838 162 TLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFVAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 257 LIMTHVSRLSEELVLWMSPRVGFIDLADRFCTGSSIMPQKKNPDVPELARGKTGRVNGHLVALLTLMKGQPLAYNKDNQE 336
Cdd:TIGR00838 242 LIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 337 DKEGLFDTADTLRDTLTIFADMAGGIKVKADNMRAAALQGFATATDLADYLVKRGLPFRDAHEVVAHAVRDCEQRGCDLA 416
Cdd:TIGR00838 322 DKEPLFDALKTVELSLEMATGMLDTITVNKERMEEAASAGFSNATELADYLVRKGVPFREAHHIVGELVATAIERGKGLE 401
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1478755605 417 DLSLAELQAYHPSIEADIHQVLTLEGSVAARKHTGGTAPERVRE 460
Cdd:TIGR00838 402 ELTLEELQKFSPEFDEDVYEALDPESSVEKRDAKGGTAPEEVLQ 445
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
5-461 |
0e+00 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 585.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 5 PSQQDQFANKAQAWSARFSEPVSDLVKRYTASVDFDKRLARHDIRGSLAHADMLAAQGIISAQDLADIERGMQQILSEID 84
Cdd:PLN02646 6 SASEEEAAKEKKLWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 85 AGSFQWLLDLEDVHLNIEKRLVELVGDAGKRLHTGRSRNDQVATDIRLWLRDEIDLLIDLLRQLRHALATVALDNAGTIM 164
Cdd:PLN02646 86 AGKFEWRPDREDVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 165 PGFTHLQVAQPVTFGHHLLAYAEMFGRDAERLADCRKRVNRLPLGAAALAGTSYPIDRERVASTLGFDGVCRNSLDAVSD 244
Cdd:PLN02646 166 PGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSD 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 245 RDFAIEFCAAASLIMTHVSRLSEELVLWMSPRVGFIDLADRFCTGSSIMPQKKNPDVPELARGKTGRVNGHLVALLTLMK 324
Cdd:PLN02646 246 RDFVLEFLFANSITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 325 GQPLAYNKDNQEDKEGLFDTADTLRDTLTIFADMAGGIKVKADNMRAAALQGFATATDLADYLVKRGLPFRDAHEVVAHA 404
Cdd:PLN02646 326 GLPTAYNRDLQEDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLDATTLADYLVRKGVPFRETHHIVGAA 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1478755605 405 VRDCEQRGCDLADLSLAELQAYHPSIEADIHQVLTLEGSVAARKHTGGTAPERVREE 461
Cdd:PLN02646 406 VALAESKGCELSDLTLEDLKSINPVFEEDVYEVLGVENSVEKFDSYGSTGSRSVLEQ 462
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
18-461 |
0e+00 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 554.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 18 WSARFSEPVSDLVKRYTASVDFDKRLARHDIRGSLAHADMLAAQGIISAQDLADIERGMQQILSEIDAGSFQWLL-DLED 96
Cdd:PRK04833 4 WGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQQQLEEALNELLEEVRANPQQILAsDAED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 97 VHLNIEKRLVELVGDAGKRLHTGRSRNDQVATDIRLWLRDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPV 176
Cdd:PRK04833 84 IHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRAQPV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 177 TFGHHLLAYAEMFGRDAERLADCRKRVNRLPLGAAALAGTSYPIDRERVASTLGFDGVCRNSLDAVSDRDFAIEFCAAAS 256
Cdd:PRK04833 164 TFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSDAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 257 LIMTHVSRLSEELVLWMSPRVGFIDLADRFCTGSSIMPQKKNPDVPELARGKTGRVNGHLVALLTLMKGQPLAYNKDNQE 336
Cdd:PRK04833 244 ISMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPLAYNKDMQE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 337 DKEGLFDTADTLRDTLTIFADMAGGIKVKADNMRAAALQGFATATDLADYLVKRGLPFRDAHEVVAHAVRDCEQRGCDLA 416
Cdd:PRK04833 324 DKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPLE 403
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1478755605 417 DLSLAELQAYHPSIEADIHQVLTLEGSVAARKHTGGTAPERVREE 461
Cdd:PRK04833 404 DLPLAELQKFSSVIGDDVYPILSLQSCLDKRAAKGGVSPQQVAQA 448
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
18-458 |
4.51e-169 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 489.68 E-value: 4.51e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 18 WSARFSEPVSDLVKRYTASVDFDKRLARHDIRGSLAHADMLAAQGIISAQDLADIERGMQQILSEIDAGSFQWLL-DLED 96
Cdd:PRK12308 4 WGGRFSQAADTRFKQFNDSLRFDYRLAEQDIVGSIAWSKALLSVGVLSEEEQQKLELALNELKLEVMEDPEQILLsDAED 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 97 VHLNIEKRLVELVGDAGKRLHTGRSRNDQVATDIRLWLRDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPV 176
Cdd:PRK12308 84 IHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 177 TFGHHLLAYAEMFGRDAERLADCRKRVNRLPLGAAALAGTSYPIDRERVASTLGFDGVCRNSLDAVSDRDFAIEFCAAAS 256
Cdd:PRK12308 164 TFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGSGALAGTAYPIDREALAHNLGFRRATRNSLDSVSDRDHVMELMSVAS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 257 LIMTHVSRLSEELVLWMSPRVGFIDLADRFCTGSSIMPQKKNPDVPELARGKTGRVNGHLVALLTLMKGQPLAYNKDNQE 336
Cdd:PRK12308 244 ISMLHLSRLAEDLIFYNSGESGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKDMQE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 337 DKEGLFDTADTLRDTLTIFADMAGGIKVKADNMRAAALQGFATATDLADYLVKRGLPFRDAHEVVAHAVRDCEQRGCDLA 416
Cdd:PRK12308 324 DKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANATELADYLVAKGIPFREAHHIVGVAVVGAIAKGCALE 403
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1478755605 417 DLSLAELQAYHPSIEADIHQVLTLEGSVAARKHTGGTAPERV 458
Cdd:PRK12308 404 ELSLEQLKEFSDVIEDDVYQILTIESCLEKRCALGGVSPEQV 445
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
45-364 |
8.99e-137 |
|
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: 396.49 E-value: 8.99e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 45 RHDIRGSLAHADMLAAQGIISAQDLADIERGMQQILSEIDAGSFQWLLDLEDVHLNIEKRLVELVGDA-GKRLHTGRSRN 123
Cdd:cd01334 2 RADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVEQEGSGTHDVMAVEEVLAERAGELnGGYVHTGRSSN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 124 DQVATDIRLWLRDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPVTFGHHLLAYAEMFGRDAERLADCRKRV 203
Cdd:cd01334 82 DIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 204 NRLPLGAAALAGTSY--PIDRERVASTLGFDGVCRNSLDAVSDRDFAIEFCAAASLIMTHVSRLSEELVLWMSPRVGFID 281
Cdd:cd01334 162 NVLPLGGGAVGTGANapPIDRERVAELLGFFGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEVE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 282 LADRFCTGSSIMPQKKNPDVPELARGKTGRVNGHLVALLTLMKGQPLAYNKDNQEDKEGLFDTADTLRDTLTIFADMAGG 361
Cdd:cd01334 242 LPDAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVLEG 321
|
...
gi 1478755605 362 IKV 364
Cdd:cd01334 322 LEV 324
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
21-314 |
4.63e-78 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 245.74 E-value: 4.63e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 21 RFSEPVSDLVKRYTASVDFDKRLARHDIRGSLAHADMLAAQGIISAQDLADIERGMQQILSEIDAGS-FQWLLDLEDVHL 99
Cdd:pfam00206 2 RFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDDqFPLKVWQEGSGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 100 NIEKRLVELVG-------DAGKRLHTGRSRNDQVATDIRLWLRDEI-DLLIDLLRQLRHALATVALDNAGTIMPGFTHLQ 171
Cdd:pfam00206 82 AVNMNLNEVIGellgqlvHPNDHVHTGQSSNDQVPTALRLALKDALsEVLLPALRQLIDALKEKAKEFADIVKPGRTHLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 172 VAQPVTFGHHLLAYAEMFGRDAERLADCRKRVNRLPLGAAALAGTSYPIDRE---RVASTLGFDG----VCRNSLDAVSD 244
Cdd:pfam00206 162 DATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEfaeLVAKELGFFTglpvKAPNSFEATSD 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1478755605 245 RDFAIEFCAAASLIMTHVSRLSEELVLWMSPRVGFIDLADRFCT-GSSIMPQKKNPDVPELARGKTGRVNG 314
Cdd:pfam00206 242 RDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEpGSSIMPGKVNPDQLELLTGKAGRVMG 312
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
88-356 |
2.04e-61 |
|
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: 199.76 E-value: 2.04e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 88 FQWLLDLEDVHL--NIEKRLVELVGDAGKRLH------TGRSRNDQVATDIRLWLRDEIDLLIDLLRQLRHALATVALDN 159
Cdd:cd01594 1 VRADLLVELAAAlaLVEEVLAGRAGELAGGLHgsalvhKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 160 AGTIMPGFTHLQVAQPVTFGHHLLAYAEMFGRDAERLADCrkrvnrlplgaaalagtsypidrervastlgfdgvcrnsl 239
Cdd:cd01594 81 KGTVMPGRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEA---------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 240 davsdrdFAIEFCAAASLIMTHVSRLSEELVLWMSPRVGFIDLAD-RFCTGSSIMPQKKNPDVPELARGKTGRVNGHLVA 318
Cdd:cd01594 121 -------AVAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFlPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVA 193
|
250 260 270
....*....|....*....|....*....|....*...
gi 1478755605 319 LLTLMKGQPLAYNKDNQEDKEGLFDTADTLRDTLTIFA 356
Cdd:cd01594 194 VLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
53-425 |
8.77e-61 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 213.17 E-value: 8.77e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 53 AHADMLAAQGIISAQDLADIergMQQILSEIDAGsFQWLLDL---EDVHLNIEKRLVELVG-DAGKRLHTGRSRNDQVAT 128
Cdd:PRK02186 447 AHLVMLGDTGIVAPERARPL---LDAHRRLRDAG-FAPLLARpapRGLYMLYEAYLIERLGeDVGGVLQTARSRNDINAT 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 129 DIRLWLRDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPVTFGHHLLAYAEMFGRDAERLADCRKRVNRLPL 208
Cdd:PRK02186 523 TTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHALFALFEHIDVCPL 602
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 209 GAAALAGTSYPIDRERVASTLGFDGVCRNSLDAVSDRDFAIEFCAAASLIMTHVSRLSEELVLWMSPRVGFIDLADRFCT 288
Cdd:PRK02186 603 GAGAGGGTTFPIDPEFVARLLGFEQPAPNSLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQLWTTREFALVSLPDALTG 682
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 289 GSSIMPQKKNPDVPELARGKTGRVNGHLVALLTLMKGQPlaYNKDNQEDKEGLFDTADT---LRDTLTIFADMAGGIKVK 365
Cdd:PRK02186 683 GSSMLPQKKNPFLLEFVKGRAGVVAGALASASAALGKTP--FSNSFEAGSPMNGPIAQAcaaIEDAAAVLVLLIDGLEAD 760
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1478755605 366 ADNMRAAALQGFATATDLADYLV-KRGLPFRDAHEVVAHAVRDCEQRGCDLADlSLAELQA 425
Cdd:PRK02186 761 QARMRAHLEDGGVSATAVAESLVvRRSISFRSAHTQVGQAIRQSLDQGRSSAD-ALAALDP 820
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
53-467 |
5.98e-57 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 196.36 E-value: 5.98e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 53 AHADMLAAQGIISAQDLADIERGMQQIlSEIDAGSFQWLLDLEDVHLNIEKRLV-ELVGDAGKRLHTGRSRNDQVATDIR 131
Cdd:PRK06705 47 AHIVMLTEENLMKKEEAKFILHALKKV-EEIPEEQLLYTEQHEDLFFLVEHLISqEAKSDFVSNMHIGRSRNDMGVTMYR 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 132 LWLRDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPVTFGHHLLAYAEMFGRDAERLADCRKRVNRLPLGAA 211
Cdd:PRK06705 126 MSLRRYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKTYKLLNQSPMGAA 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 212 ALAGTSYPIDRERVASTLGFDGVCRNSLDAVSDRDFAIEFCAAASLIMTHVSRLSEELVLWMSPRVGFIDLADRFCTGSS 291
Cdd:PRK06705 206 ALSTTSFPIKRERVADLLGFTNVIENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLATKEYDGITVARPYVQISS 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 292 IMPQKKNPDVPELARGKTGRVNGHLVALLTLMKGQPLAYNKDNQEDKEGLFdtADTLRDTLTIFADMAGGI---KVKADN 368
Cdd:PRK06705 286 IMPQKRNPVSIEHARAITSSALGEAFTVFQMIHNTPFGDIVDTEDDLQPYL--YKGIEKAIRVFCIMNAVIrtmKVEEDT 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 369 MRAAALQGFATATDLADYLVKR-GLPFRDAHEVVAHAVRDCEQRGCDLADLSLAELQAYHPS------IEADIHQVLTLE 441
Cdd:PRK06705 364 LKRRSYKHAITITDFADVLTKNyGIPFRHAHHAASVIANMSLEQKKELHELCFKDVNIYLQEkfkiqlLEKEWEEIISPE 443
|
410 420
....*....|....*....|....*.
gi 1478755605 442 GSVAARKHTGGTApervREEAQRVIQ 467
Cdd:PRK06705 444 AFIQKRNVYGGPS----KKEMERMIN 465
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
24-441 |
1.56e-34 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 133.87 E-value: 1.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 24 EPVSDLVKRytaSVDFDKRLARHDIRGSLAHADMLAAQGIISAQDLADIERGMQQILSeidaGSFQWLLDLEDVHLNIEK 103
Cdd:PRK06389 15 DFYDNIVKD---DIDADKNLIKYEIINLLAYHVALAQRRLITEKAPKCVINALIDIYK----NGIEIDLDLEDVHTAIEN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 104 RLVELVGDAGKRLHTGRSRNDQVATDIRLWLRDEIDLLIDLLRQLRHALATValdNAGTIMPGFTHLQVAQPVTFGHHLL 183
Cdd:PRK06389 88 FVIRRCGDMFKNFRLFLSRNEQVHADLNLFIIDKIIEIEKILYEIIKVIPGF---NLKGRLPGYTHFRQAMPMTVNTYIN 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 184 AYAEMFGRDAERLADCRKRVNRLPLGAAALAGTSYPIDRERVASTLGFDGVCRNSLDAVSDRDFAI-EFCAAASLIMTHV 262
Cdd:PRK06389 165 YIKSILYHHINNLDSFLMDLREMPYGYGSGYGSPSSVKFNQMSELLGMEKNIKNPVYSSSLYIKTIeNISYLISSLAVDL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 263 SRLSEELVLWMspRVGFIDLADRFCTGSSIMPQKKNPDVPELARGKTGRVNGHLVALLTLMKGQPLAYNKDNQEDKEGLF 342
Cdd:PRK06389 245 SRICQDIIIYY--ENGIITIPDEFTTGSSLMPNKRNPDYLELFQGIAAESISVLSFIAQSELNKTTGYHRDFQIVKDSTI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 343 DTADTLRDTLTIFADMAGGIKVKADNMRAAALQGFATATDLADYlvKRGLPFRDAHEVVAHAVRDCEqrgcdladlslaE 422
Cdd:PRK06389 323 SFINNFERILLGLPDLLYNIKFEITNEKNIKNSVYATYNAWLAF--KNGMDWKSAYAYIGNKIREGE------------V 388
|
410
....*....|....*....
gi 1478755605 423 LQAYHPSIEADIHQVLTLE 441
Cdd:PRK06389 389 LDEYQPEDLTDYIDVNELK 407
|
|
| ASL_C2 |
pfam14698 |
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of ... |
377-444 |
4.53e-34 |
|
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: 122.14 E-value: 4.53e-34
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1478755605 377 FATATDLADYLVKRGLPFRDAHEVVAHAVRDCEQRGCDLADLSLAELQAYHPSIEADIHQVLTLEGSV 444
Cdd:pfam14698 1 FSTATDLADYLVRKGVPFREAHEIVGRLVRLAEEKGKDLEDLTLEELQAISPLFEEDVYEALDPEASV 68
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
58-401 |
4.10e-30 |
|
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: 120.69 E-value: 4.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 58 LAAQGIISAQDLADIERGMQQILSEIDAgsfqwLLDLE-----DVhLNIEKRLVELVGD-AGKRLHTGRSRNDQVATDIR 131
Cdd:cd01595 25 QAELGLIPKEAAEEIRAAADVFEIDAER-----IAEIEketghDV-IAFVYALAEKCGEdAGEYVHFGATSQDINDTALA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 132 LWLRDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPVTFGHHLLAYAEMFGRDAERLADCRKRVNRL----P 207
Cdd:cd01595 99 LQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGgisgA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 208 LGAAALAGTSYPIDRERVASTLGFdgvcrnSLDAVS----DRDFAIEFCAAASLIMTHVSRLSEELVLWMSPRVGFIDL- 282
Cdd:cd01595 179 VGTHASLGPKGPEVEERVAEKLGL------KVPPITtqiePRDRIAELLSALALIAGTLEKIATDIRLLQRTEIGEVEEp 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 283 ADRFCTGSSIMPQKKNPDVPELARGKTGRVNGHLVALLTLMkgqplaynkdNQEDKEGLFDTAdTLRDT----------- 351
Cdd:cd01595 253 FEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENL----------VQWHERDLSDSS-VERNIlpdafllldaa 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1478755605 352 LTIFADMAGGIKVKADNMRA--AALQGFATATDLADYLVKRGLPFRDAHEVV 401
Cdd:cd01595 322 LSRLQGLLEGLVVNPERMRRnlDLTWGLILSEAVMMALAKKGLGRQEAYELV 373
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
58-460 |
1.12e-29 |
|
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: 120.19 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 58 LAAQGIISAQDLADIERgmqqiLSEIDAGSFQWLLDLEDV--HLNI--EKRLVELVGDAGKR-LHTGrsrndqvAT--DI 130
Cdd:COG0015 35 QAELGLIPAEAAAAIRA-----AADDFEIDAERIKEIEKEtrHDVKafVYALKEKVGAEAGEyIHFG-------ATsqDI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 131 -----RLWLRDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPVTFGHHLLAYAEMFGRDAERLADCRKRVNR 205
Cdd:COG0015 103 ndtalALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 206 LPLGAAalAGT--SYPID----RERVASTLGFdgvcrNSLDA---VSDRDFAIEFCAAASLIMTHVSRLSEELVLWMSPR 276
Cdd:COG0015 183 GKIGGA--VGTyaAHGEAwpevEERVAEKLGL-----KPNPVttqIEPRDRHAELFSALALIAGSLEKIARDIRLLQRTE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 277 VGFidLADRFC---TGSSIMPQKKNPDVPELARGKTGRVNGHLVALLTLMkgqplaynkdNQEDKEGLFDTAdTLRDT-- 351
Cdd:COG0015 256 VGE--VEEPFAkgqVGSSAMPHKRNPIDSENIEGLARLARALAAALLEAL----------ASWHERDLSDSS-VERNIlp 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 352 ---------LTIFADMAGGIKVKADNMRA--AALQGFATATDLADYLVKRGLPFRDAHEVVAHAVRDCEQRGCDLADLsL 420
Cdd:COG0015 323 dafllldgaLERLLKLLEGLVVNPERMRAnlDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAWEEGNDLREL-L 401
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1478755605 421 AElqayhpsiEADIHQVLT---LEGSVAARKHTgGTAPERVRE 460
Cdd:COG0015 402 AA--------DPEIPAELSkeeLEALFDPANYL-GAADEIVDR 435
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
103-422 |
4.76e-26 |
|
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: 110.03 E-value: 4.76e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 103 KRLVELVGD-AGKRLHTGRSRNDQVATDIRLWLRDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPVTFGHH 181
Cdd:cd01597 79 KQLTAACGDaAGEYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 182 LLAYAEMFGRDAERLADCRKRVNRLPLGAAA--LA--GTSYPIDRERVASTLGFDgvcrnsLDAVS---DRDFAIEFCAA 254
Cdd:cd01597 159 VAVWLSELLRHRERLDELRPRVLVVQFGGAAgtLAslGDQGLAVQEALAAELGLG------VPAIPwhtARDRIAELASF 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 255 ASLIMTHVSRLSEELVLWMSPRVGfiDLADRFCTG---SSIMPQKKNPDVPELARGKTGRVNGHLVALLTLMKgqplayn 331
Cdd:cd01597 233 LALLTGTLGKIARDVYLLMQTEIG--EVAEPFAKGrggSSTMPHKRNPVGCELIVALARRVPGLAALLLDAMV------- 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 332 KDNQEDKEGLFDTADTLRDT-------LTIFADMAGGIKVKADNMRA--AALQGF----ATATDLADYLVKrglpfRDAH 398
Cdd:cd01597 304 QEHERDAGAWHAEWIALPEIfllasgaLEQAEFLLSGLEVNEDRMRAnlDLTGGLilseAVMMALAPKLGR-----QEAH 378
|
330 340
....*....|....*....|....
gi 1478755605 399 EVVAHAVRDCEQRGCDLADLSLAE 422
Cdd:cd01597 379 DLVYEACMRAVEEGRPLREVLLED 402
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
119-422 |
5.15e-23 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 101.21 E-value: 5.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 119 GRSRNDQVATDIRLWLRDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPVTFGHHLLAYAEMFGRDAERLAD 198
Cdd:PRK13353 138 AQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQ 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 199 CRKRVNRLPLGAAALaGTSYPIDRE---RVASTLGFD-GV----CRNSLDAVSDRDFAIEFCAAASLIMTHVSRLSEELV 270
Cdd:PRK13353 218 AREHLYEVNLGGTAV-GTGLNADPEyieRVVKHLAAItGLplvgAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 271 LWMS-PRVGF--IDLADRFCtGSSIMPQKKNPDVPELARGKTGRV--NGHLVAL------LTLMKGQPL-AYNkdnqedk 338
Cdd:PRK13353 297 LLSSgPRTGLgeINLPAVQP-GSSIMPGKVNPVMPEVVNQIAFQVigNDVTITLaaeagqLELNVMEPViAFN------- 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 339 egLFDTADTLRDTLTIFAD-MAGGIKVKADNMRAAALQGFATATDLADYLvkrglpfrdAHEVVAHAVRDCEQRGCDLAD 417
Cdd:PRK13353 369 --LLESISILTNACRAFTDnCVKGIEANEERCKEYVEKSVGIATALNPHI---------GYEAAARIAKEAIATGRSVRE 437
|
....*
gi 1478755605 418 LSLAE 422
Cdd:PRK13353 438 LALEN 442
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
52-306 |
7.70e-22 |
|
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: 96.85 E-value: 7.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 52 LAHADMLAAQGIISAQDLADIERGMQQILSEIDagsfqwlldledvhlNIEKR-----------LVELVGDAGKRLHTGR 120
Cdd:cd01360 25 AAVCEAWAKLGVIPAEAAEEIRKKAKFDVERVK---------------EIEAEtkhdviafvtaIAEYCGEAGRYIHFGL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 121 SRNDQVATDIRLWLRDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPVTFGHHLLAYAEMFGRDAERLADCR 200
Cdd:cd01360 90 TSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKEAR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 201 KRVNRL----PLGAAALAGtsyPIDRERVASTLGFdgvcrNSLDA---VSDRDFAIEFCAAASLIMTHVSRLSEELVLWM 273
Cdd:cd01360 170 ERILVGkisgAVGTYANLG---PEVEERVAEKLGL-----KPEPIstqVIQRDRHAEYLSTLALIASTLEKIATEIRHLQ 241
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1478755605 274 SPRVGfiDLADRFC---TGSSIMPQKKNPDVPE----LAR 306
Cdd:cd01360 242 RTEVL--EVEEPFSkgqKGSSAMPHKRNPILSEnicgLAR 279
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
119-387 |
2.05e-19 |
|
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: 90.27 E-value: 2.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 119 GRSRNDQVATDIRLWLRDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPVTFGHHLLAYAEMFGRDAERLAD 198
Cdd:cd01357 133 SQSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 199 CRKRVNRLPLGAAALaGT------SYpidRERVASTL----GFDGV-CRNSLDAVSDRDFAIEFCAAASLIMTHVSRLSE 267
Cdd:cd01357 213 ARERLREVNLGGTAI-GTginappGY---IELVVEKLseitGLPLKrAENLIDATQNTDAFVEVSGALKRLAVKLSKIAN 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 268 ELVLWMS-PRVGF--IDLADRfCTGSSIMPQKKNPDVPELARGKTGRVNGHLVAL--------LTLMKGQPL-AYNkdnq 335
Cdd:cd01357 289 DLRLLSSgPRAGLgeINLPAV-QPGSSIMPGKVNPVIPEVVNQVAFQVIGNDLTItmaaeagqLELNVFEPViAYN---- 363
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1478755605 336 edkegLFDTADTLRDTLTIFADMA-GGIKVKADNMRAAALQGFATATDLADYL 387
Cdd:cd01357 364 -----LLESIDILTNAVRTLRERCiDGITANEERCREYVENSIGIVTALNPYI 411
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
121-422 |
3.25e-19 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 89.73 E-value: 3.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 121 SRNDQVATDIRLWLRDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPVTFGHHLLAYAEMFGRDAERLADCR 200
Cdd:COG1027 137 STNDVYPTAIRLALLLLLRELLEALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAA 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 201 KRVNRLPLGAAAlAGTS------YpidRERVASTL----GFDGV-CRNSLDAVSDRDFAIEFCAAASLIMTHVSRLSEEL 269
Cdd:COG1027 217 ELLREVNLGGTA-IGTGlnappgY---IELVVEHLaeitGLPLVrAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 270 VLwMS--PRVGF--IDL----AdrfctGSSIMPQKKNPDVPELargktgrVN-------GHLVAlLTLM--KGQ------ 326
Cdd:COG1027 293 RL-LSsgPRAGLgeINLpavqP-----GSSIMPGKVNPVIPEV-------VNqvafqviGNDLT-VTMAaeAGQlelnvf 358
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 327 -PL-AYNkdnqedkegLFDTADTLRDTLTIFADMA-GGIKVKADNMRAAALQGFATATDLADYLvkrGlpfrdaHEVVAH 403
Cdd:COG1027 359 ePViAYN---------LLESIELLTNACRTLREKCiDGITANEERCREYVENSIGLVTALNPYI---G------YEKAAE 420
|
330
....*....|....*....
gi 1478755605 404 AVRDCEQRGCDLADLSLAE 422
Cdd:COG1027 421 IAKEALATGKSVRELVLEK 439
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
121-387 |
3.28e-17 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 83.64 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 121 SRNDQVATDIRLWLRDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPVTFGHHLLAYAEMFGRDAERLADCR 200
Cdd:PRK12273 142 STNDAYPTAIRIALLLSLRKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAA 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 201 KRVNRLPLGAAAlAGT------SYpidRERVASTL----GFDGV-CRNSLDAVSDRDFAIEFCAAASLIMTHVSRLSEEL 269
Cdd:PRK12273 222 ELLREVNLGATA-IGTglnappGY---IELVVEKLaeitGLPLVpAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDL 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 270 VLwMS--PRVGF--IDLADRfCTGSSIMPQKKNPDVPELargktgrVN-------GHLVAlLTLM--KGQ-------PL- 328
Cdd:PRK12273 298 RL-LSsgPRAGLneINLPAV-QAGSSIMPGKVNPVIPEV-------VNqvcfqviGNDTT-VTMAaeAGQlelnvmePVi 367
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 329 AYNkdnqedkegLFDTADTLRDTLTIFADMA-GGIKVKADNMRAAALQGFATATDLADYL 387
Cdd:PRK12273 368 AYN---------LFESISILTNACRTLREKCiDGITANEERCREYVENSIGIVTALNPYI 418
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
121-397 |
5.06e-17 |
|
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: 82.86 E-value: 5.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 121 SRNDQVATDIRLWLRDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPVTFGHHLLAYAEMFGRDAERLADCR 200
Cdd:cd01596 135 SNDDFPPAAHIAAALALLERLLPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAAL 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 201 KRVNRLPLGAAALaGT---SYPIDRERVASTL----GFDGV-CRNSLDAVSDRDFAIEFCAAASLIMTHVSRLSEELvLW 272
Cdd:cd01596 215 ERLRELNLGGTAV-GTglnAPPGYAEKVAAELaeltGLPFVtAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDL-RL 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 273 MS--PRVGF--IDLADRfCTGSSIMPQKKNPDVPELARGKTGRVNGHLVAL----------LTLMKgqPL-AYNkdnqed 337
Cdd:cd01596 293 LSsgPRAGLgeINLPAN-QPGSSIMPGKVNPVIPEAVNMVAAQVIGNDTAItmagsagqleLNVFK--PViAYN------ 363
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1478755605 338 kegLFDTADTLRDTLTIFAD-MAGGIKVKADNMR---------AAALQ---GFATATDLADYLVKRGLPFRDA 397
Cdd:cd01596 364 ---LLQSIRLLANACRSFRDkCVEGIEANEERCKeyvenslmlVTALNphiGYEKAAEIAKEALKEGRTLREA 433
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
47-425 |
8.80e-17 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 82.37 E-value: 8.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 47 DIRGSLAHAdmLAAQGIISAQDLADIERGMQQILSEIDAGSfqwlldlEDVHL--NIEKRLVELVG--------DAGKRL 116
Cdd:PRK09053 32 DFEAALARA--EAACGVIPAAAVAPIEAACDAERLDLDALA-------QAAALagNLAIPLVKQLTaqvaardaEAARYV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 117 HTGRSRNDQVATDIRLWLRDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPVTFGHHLLAYAEMFGRDAERL 196
Cdd:PRK09053 103 HWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 197 ADCRKRVNRLPLGAAA--LA--GTSYPIDRERVASTLGFDgvcrnsLDAVS---DRDFAIEFCAAASLIMTHVSRLSEEL 269
Cdd:PRK09053 183 AALRPRALVLQFGGAAgtLAslGEQALPVAQALAAELQLA------LPALPwhtQRDRIAEFASALGLLAGTLGKIARDV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 270 VLWMSPRVG-FIDLADRFCTGSSIMPQKKNPDVPELARGKTGRVNGhLVAllTLMKGQPlaynkDNQEDKEGLFDTA-DT 347
Cdd:PRK09053 257 SLLMQTEVGeVFEPAAAGKGGSSTMPHKRNPVGCAAVLTAATRAPG-LVA--TLFAAMP-----QEHERALGGWHAEwDT 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 348 LRD-------TLTIFADMAGGIKVKADNMRA------AALQGFATATDLADYLVKrglpfRDAHEVVAHAVRDCEQRGCD 414
Cdd:PRK09053 329 LPElaclaagALAQMAQIVEGLEVDAARMRAnldlthGLILAEAVMLALADRIGR-----LDAHHLVEQASKRAVAEGRH 403
|
410 420
....*....|....*....|..
gi 1478755605 415 L-----------ADLSLAELQA 425
Cdd:PRK09053 404 LrdvlaedpqvsAHLSPAALDR 425
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
65-304 |
2.69e-14 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 74.65 E-value: 2.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 65 SAQDLADIERGMQQILSEIDAGSFQWL-LDLEDVhlnIEKRLVELVG---------DAGKRLHTGRSRNDQVATDIRLWL 134
Cdd:PRK14515 83 AAQEILDGKWHDHFIVDPIQGGAGTSMnMNANEV---IANRALELLGmekgdyhyiSPNSHVNMAQSTNDAFPTAIHIAT 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 135 RDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPVTFGHHLLAYAEMFGRDAERLADCRKRVNRLPLGAAALa 214
Cdd:PRK14515 160 LNALEGLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAV- 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 215 GTSYPIDRERV-------ASTLGFDGVCRNSL-DAVSDRDFAIEFCAAASLIMTHVSRLSEELVLWMS-PRVGF--IDLA 283
Cdd:PRK14515 239 GTGLNADPEYIeavvkhlAAISELPLVGAEDLvDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASgPRVGLaeIMLP 318
|
250 260
....*....|....*....|.
gi 1478755605 284 DRfCTGSSIMPQKKNPDVPEL 304
Cdd:PRK14515 319 AR-QPGSSIMPGKVNPVMPEV 338
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
119-397 |
1.63e-12 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 69.35 E-value: 1.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 119 GRSRNDQVATDIRLWLRDEI-DLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPVTFGHHLLAYAEMFGRDAERLA 197
Cdd:PRK00485 137 SQSSNDTFPTAMHIAAVLAIvERLLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIE 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 198 DCRKRVNRLPLGAAAlAGT---SYPIDRERVASTL----GFDGV-CRNSLDAVSDRDFAIEF-----CAAASLImthvsR 264
Cdd:PRK00485 217 AALPHLYELALGGTA-VGTglnAHPGFAERVAEELaeltGLPFVtAPNKFEALAAHDALVEAsgalkTLAVSLM-----K 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 265 LSEELvLWMS--PRVGF--IDLADRFcTGSSIMPQKKNPDVPELARGKTGRVNGHLVAL----------LTLMKgqPL-A 329
Cdd:PRK00485 291 IANDI-RWLAsgPRCGLgeISLPENE-PGSSIMPGKVNPTQCEALTMVCAQVMGNDAAVtfagsqgnfeLNVFK--PViA 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 330 YNkdnqedkegLFDTADTLRDTLTIFAD-MAGGIKVKADNMRAAALQ------------GFATATDLADYLVKRGLPFRD 396
Cdd:PRK00485 367 YN---------FLQSIRLLADAMRSFADhCVVGIEPNRERIKELLERslmlvtalnphiGYDKAAKIAKKAHKEGLTLKE 437
|
.
gi 1478755605 397 A 397
Cdd:PRK00485 438 A 438
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
119-303 |
4.06e-10 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 61.63 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 119 GRSRNDQVATDIRLWLRDEI-DLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPVTFGHHLLAYAEMFGRDAERLA 197
Cdd:PLN00134 129 SQSSNDTFPTAMHIAAATEIhSRLIPALKELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 198 DCRKRVNRLPLGAAALaGTSYPIDR---ERVASTLGFDG-----VCRNSLDAVSDRDFAIEFCAAASLIMTHVSRLSEEL 269
Cdd:PLN00134 209 CTLPRLYELAQGGTAV-GTGLNTKKgfdEKIAAAVAEETglpfvTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDI 287
|
170 180 190
....*....|....*....|....*....|....*..
gi 1478755605 270 VLWMS-PRVGF--IDLADRfCTGSSIMPQKKNPDVPE 303
Cdd:PLN00134 288 RLLGSgPRCGLgeLNLPEN-EPGSSIMPGKVNPTQCE 323
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
119-397 |
6.38e-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: 60.98 E-value: 6.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 119 GRSRNDQVATDIRLWLRDEI-DLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPVTFGHHLLAYAEMFGRDAERLA 197
Cdd:cd01362 133 SQSSNDTFPTAMHIAAALALqERLLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIE 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 198 DCRKRVNRLPLGAAALaGT---SYPIDRERVASTL----GFDGV-CRNSLDAVSDRDFAIEF-----CAAASLImthvsR 264
Cdd:cd01362 213 AALPRLYELALGGTAV-GTglnAHPGFAEKVAAELaeltGLPFVtAPNKFEALAAHDALVEAsgalkTLAVSLM-----K 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 265 LSEELvLWMS--PRVGF--IDLADRFcTGSSIMPQKKNPDVPELARGKTGRVNGHLVAL----------LTLMKgqPL-A 329
Cdd:cd01362 287 IANDI-RWLGsgPRCGLgeLSLPENE-PGSSIMPGKVNPTQCEALTMVAAQVMGNDAAItiagssgnfeLNVFK--PViI 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 330 YNkdnqedkegLFDTADTLRDTLTIFAD-MAGGIKVKADNMRAA---------ALQ---GFATATDLADYLVKRGLPFRD 396
Cdd:cd01362 363 YN---------LLQSIRLLADACRSFADkCVAGIEPNRERIAELlerslmlvtALNphiGYDKAAKIAKKAHKEGLTLKE 433
|
.
gi 1478755605 397 A 397
Cdd:cd01362 434 A 434
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
44-306 |
5.00e-07 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 51.59 E-value: 5.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 44 ARHDIRGSL----AHADMLAAQGIISAQDLADIERGMQQIlsEIDAGSFQWLLDLEDVHL-NIEKRLVELVG-DAGKRLH 117
Cdd:PRK05975 26 AEADIAAMLafeaALAEAEAEHGIIPAEAAERIAAACETF--EPDLAALRHATARDGVVVpALVRQLRAAVGeEAAAHVH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 118 TGRSRNDQVATDIRLWLRDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPVTFGHHLLAYAEMFGRDAERLA 197
Cdd:PRK05975 104 FGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRHRDRLE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 198 DCRKRVNRLPLGAAAlaGT------SYPIDRERVASTLGF-DGVCrnsldAVSDRDFAIEFCAAASLIMTHVSRLSEELV 270
Cdd:PRK05975 184 ALRADVFPLQFGGAA--GTleklggKAAAVRARLAKRLGLeDAPQ-----WHSQRDFIADFAHLLSLVTGSLGKFGQDIA 256
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1478755605 271 LwMSPRVGFIDLADRfcTGSSIMPQKKNPDVPE----LAR 306
Cdd:PRK05975 257 L-MAQAGDEISLSGG--GGSSAMPHKQNPVAAEtlvtLAR 293
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
107-299 |
3.81e-06 |
|
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.
Pssm-ID: 176471 [Multi-domain] Cd Length: 436 Bit Score: 49.24 E-value: 3.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 107 ELVGDAGKRLHTG-RSRNDQVATDIrLWLRDEIDLLIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPVTFGHHLLAY 185
Cdd:cd03302 81 LLCPAAAGIIHLGaTSCFVTDNTDL-IQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLW 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 186 AEMFGRDAERLADCRkrvNRLPL-GAAALAGTS------YPIDR-------ERVASTLGFDGVcRNSLDAVSDRDFAIEF 251
Cdd:cd03302 160 IQDLLMDLRNLERLR---DDLRFrGVKGTTGTQasfldlFEGDHdkvealdELVTKKAGFKKV-YPVTGQTYSRKVDIDV 235
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1478755605 252 CAAASLIMTHVSRLSEELVLwmspRVGFIDLADRFCT---GSSIMPQKKNP 299
Cdd:cd03302 236 LNALSSLGATAHKIATDIRL----LANLKEVEEPFEKgqiGSSAMPYKRNP 282
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
254-422 |
3.55e-05 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 45.02 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 254 AASLIMTHVSRLSEELVLWMSPRVGFIDLA-DRFCTGSSIMPQKKNPDVPElargktgrvngHLVALLTLMKGQPLAYNK 332
Cdd:PRK08937 22 VLALIATSLEKFANEIRLLQRSEIREVEEPfAKGQKGSSAMPHKRNPIGSE-----------RITGLARVLRSYLVTALE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 333 DNQEDKEG-----------LFDTADTLRDTLTIFADMAGGIKVKADNMRA--AALQGFATATDLADYLVKRGLPFRDAHE 399
Cdd:PRK08937 91 NVPLWHERdlshssaeriaLPDAFLALDYILNRFVNILENLVVFPENIERnlDKTLGFIATERVLLELVEKGMGREEAHE 170
|
170 180
....*....|....*....|...
gi 1478755605 400 VVAHAVRDCEQRGCDLADLSLAE 422
Cdd:PRK08937 171 LIREKAMEAWKNQKDLRELLEAD 193
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
141-299 |
3.92e-04 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 42.60 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 141 LIDLLRQLRHALATVALDNAGTIMPGFTHLQVAQPVTFGHHLLAYAEMFGRDAERLADCRKRVNRLPLGAAAL------- 213
Cdd:PRK12425 158 LLPAIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVgtglnap 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1478755605 214 AGTSYPIDRERVA-STLGFDGVcRNSLDAVSDRDFAIEFCAAASLIMTHVSRLSEELVLWMS-PRVGFIDL---ADRfcT 288
Cdd:PRK12425 238 HGFAEAIAAELAAlSGLPFVTA-PNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSgPRAGLAEVrlpANE--P 314
|
170
....*....|.
gi 1478755605 289 GSSIMPQKKNP 299
Cdd:PRK12425 315 GSSIMPGKVNP 325
|
|
| |
