|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
1-455 |
0e+00 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 1033.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQLQLEDALNNLLEEVRLNPQQILESD 80
Cdd:PRK04833 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQQQLEEALNELLEEVRANPQQILASD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 81 AEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVGELLAANRQLQSALVETAQNNQDAVMPGYTHLQRA 160
Cdd:PRK04833 81 AEDIHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 161 QPVTFAHWCLAYVEMLARDESRLQDTLKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
Cdd:PRK04833 161 QPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 241 NASIGMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKD 320
Cdd:PRK04833 241 DASISMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPLAYNKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 321 MQEDKEGLFDALDTWLDCLHMGALVLDGIQVKRPRCQEAAQQGYANSTELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
Cdd:PRK04833 321 MQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1221421241 401 PLEDLTLAELQKFSAVIGDDVYPILALQSCLDKRAAKGGVSPKQVAQAIADAKSR 455
Cdd:PRK04833 401 PLEDLPLAELQKFSSVIGDDVYPILSLQSCLDKRAAKGGVSPQQVAQAIAAAKAR 455
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
1-456 |
0e+00 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 831.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQLQLEDALNNLLEEVRLNPQQILESD 80
Cdd:PRK12308 1 MALWGGRFSQAADTRFKQFNDSLRFDYRLAEQDIVGSIAWSKALLSVGVLSEEEQQKLELALNELKLEVMEDPEQILLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 81 AEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVGELLAANRQLQSALVETAQNNQDAVMPGYTHLQRA 160
Cdd:PRK12308 81 AEDIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 161 QPVTFAHWCLAYVEMLARDESRLQDTLKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
Cdd:PRK12308 161 QPVTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGSGALAGTAYPIDREALAHNLGFRRATRNSLDSVSDRDHVMELMS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 241 NASIGMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKD 320
Cdd:PRK12308 241 VASISMLHLSRLAEDLIFYNSGESGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 321 MQEDKEGLFDALDTWLDCLHMGALVLDGIQVKRPRCQEAAQQGYANSTELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
Cdd:PRK12308 321 MQEDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANATELADYLVAKGIPFREAHHIVGVAVVGAIAKGC 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1221421241 401 PLEDLTLAELQKFSAVIGDDVYPILALQSCLDKRAAKGGVSPKQVAQAIADAKSRL 456
Cdd:PRK12308 401 ALEELSLEQLKEFSDVIEDDVYQILTIESCLEKRCALGGVSPEQVAYAVEQADKRL 456
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
3-456 |
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: 775.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 3 LWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQLQLEDALNNLLEEVRLNPQqILESDAE 82
Cdd:TIGR00838 1 LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPF-ILDPDDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 83 DIHSWVEGKLIDKVG-QLGKKLHTGRSRNDQVATDLKLWCKDTVGELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQ 161
Cdd:TIGR00838 80 DIHMAIERELIDRVGeDLGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 162 PVTFAHWCLAYVEMLARDESRLQDTLKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSN 241
Cdd:TIGR00838 160 PITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 242 ASIGMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDM 321
Cdd:TIGR00838 240 AALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 322 QEDKEGLFDALDTWLDCLHMGALVLDGIQVKRPRCQEAAQQGYANSTELADYLVAKGVPFREAHHIVGEAVVEAIRQGKP 401
Cdd:TIGR00838 320 QEDKEPLFDALKTVELSLEMATGMLDTITVNKERMEEAASAGFSNATELADYLVRKGVPFREAHHIVGELVATAIERGKG 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1221421241 402 LEDLTLAELQKFSAVIGDDVYPILALQSCLDKRAAKGGVSPKQVAQAIADAKSRL 456
Cdd:TIGR00838 400 LEELTLEELQKFSPEFDEDVYEALDPESSVEKRDAKGGTAPEEVLQAIAEAKARL 454
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
1-456 |
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: 735.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQLQLEDALNNLLEEVRLNPQQILESD 80
Cdd:COG0165 3 MKLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAFEFDPEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 81 aEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVGELLAANRQLQSALVETAQNNQDAVMPGYTHLQRA 160
Cdd:COG0165 83 -EDIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 161 QPVTFAHWCLAYVEMLARDESRLQDTLKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
Cdd:COG0165 162 QPVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 241 NASIGMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKD 320
Cdd:COG0165 242 AASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNKD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 321 MQEDKEGLFDALDTWLDCLHMGALVLDGIQVKRPRCQEAAQQGYANSTELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
Cdd:COG0165 322 LQEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGFSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKGK 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1221421241 401 PLEDLTLAELQKFSAVIGDDVYPILALQSCLDKRAAKGGVSPKQVAQAIADAKSRL 456
Cdd:COG0165 402 DLEDLTLEELQAFSPLIEEDVYEALDPEGSVAARDSYGGTAPEAVREQIARARARL 457
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
1-456 |
0e+00 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 698.06 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQLQLEDALNNLLEEVRLNPQQILESD 80
Cdd:PRK00855 4 NKLWGGRFSEGPDELVERFTASISFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILEEIEAGKFEFSPEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 81 aEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVGELLAANRQLQSALVETAQNNQDAVMPGYTHLQRA 160
Cdd:PRK00855 84 -EDIHMAIEARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 161 QPVTFAHWCLAYVEMLARDESRLQDTLKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
Cdd:PRK00855 163 QPVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAALAGTTFPIDRERTAELLGFDGVTENSLDAVSDRDFALEFLS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 241 NASIGMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKD 320
Cdd:PRK00855 243 AASLLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLAYNRD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 321 MQEDKEGLFDALDTWLDCLHMGALVLDGIQVKRPRCQEAAQQGYANSTELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
Cdd:PRK00855 323 LQEDKEPLFDAVDTLKLSLEAMAGMLETLTVNKERMREAAGKGFSTATDLADYLVRKGVPFREAHEIVGKAVREAEERGV 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1221421241 401 PLEDLTLAELQKFSAVIGDDVYPILALQSCLDKRAAKGGVSPKQVAQAIADAKSRL 456
Cdd:PRK00855 403 DLADLSLEELQAFSPLITEDVYEVLTPEGSVAARNSIGGTAPEQVREQIARAKARL 458
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
22-456 |
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: 651.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 22 SLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQLQLEDALNNLLEEVRlNPQQILESDAEDIHSWVEGKLIDKVGQLGK 101
Cdd:cd01359 1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIE-AGAFELDPEDEDIHMAIERRLIERIGDVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 102 KLHTGRSRNDQVATDLKLWCKDTVGELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDES 181
Cdd:cd01359 80 KLHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 182 RLQDTLKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSNASIGMVHLSRFAEDLIFFNS 261
Cdd:cd01359 160 RLADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 262 GEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQEDKEGLFDALDTWLDCLHM 341
Cdd:cd01359 240 QEFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 342 GALVLDGIQVKRPRCQEAAQQGYANSTELADYLVA-KGVPFREAHHIVGEAVVEAIRQGKPLEDLTLAELQKFSAVIGDD 420
Cdd:cd01359 320 LTGVISTLTVNPERMREAAEAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEED 399
|
410 420 430
....*....|....*....|....*....|....*.
gi 1221421241 421 VYPILALQSCLDKRAAKGGVSPKQVAQAIADAKSRL 456
Cdd:cd01359 400 VREALDPENSVERRTSYGGTAPAEVREQIARARALL 435
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
3-456 |
0e+00 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 544.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 3 LWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQLQLEDALNNLLEEVRLNPQQIlESDAE 82
Cdd:PLN02646 18 LWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAGKFEW-RPDRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 83 DIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVGELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQP 162
Cdd:PLN02646 97 DVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 163 VTFAHWCLAYVEMLARDESRLQDTLKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSNA 242
Cdd:PLN02646 177 VLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRDFVLEFLFAN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 243 SIGMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQ 322
Cdd:PLN02646 257 SITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTAYNRDLQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 323 EDKEGLFDALDTWLDCLHMGALVLDGIQVKRPRCQEAAQQGYANSTELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPL 402
Cdd:PLN02646 337 EDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLDATTLADYLVRKGVPFRETHHIVGAAVALAESKGCEL 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1221421241 403 EDLTLAELQKFSAVIGDDVYPILALQSCLDKRAAKGGVSPKQVAQAIADAKSRL 456
Cdd:PLN02646 417 SDLTLEDLKSINPVFEEDVYEVLGVENSVEKFDSYGSTGSRSVLEQLEKWRTKL 470
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
31-351 |
7.73e-126 |
|
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: 367.98 E-value: 7.73e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 31 EQDIVGSVAWSKALVTVGVLTADEQLQLEDALNNLLEEVrLNPQQILESDAEDIHSWVEGKLIDKVGQL-GKKLHTGRSR 109
Cdd:cd01334 2 RADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGI-AADQVEQEGSGTHDVMAVEEVLAERAGELnGGYVHTGRSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 110 NDQVATDLKLWCKDTVGELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDTLKR 189
Cdd:cd01334 81 NDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 190 LDVSPLGSGALAGTAY--EIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSNASIGMVHLSRFAEDLIFFNSGEAGFV 267
Cdd:cd01334 161 LNVLPLGGGAVGTGANapPIDRERVAELLGFFGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 268 ELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQEDKEGLFDALDTWLDCLHMGALVLD 347
Cdd:cd01334 241 ELPDAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVLE 320
|
....
gi 1221421241 348 GIQV 351
Cdd:cd01334 321 GLEV 324
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
6-301 |
2.07e-124 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 364.00 E-value: 2.07e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 6 GRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQLQLEDALNNLLEEVRLNPQQILESDAEDIH 85
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDDQFPLKVWQEGSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 86 SWVEGKLIDKVGQL-------GKKLHTGRSRNDQVATDLKLWCKDTVGE-LLAANRQLQSALVETAQNNQDAVMPGYTHL 157
Cdd:pfam00206 81 TAVNMNLNEVIGELlgqlvhpNDHVHTGQSSNDQVPTALRLALKDALSEvLLPALRQLIDALKEKAKEFADIVKPGRTHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 158 QRAQPVTFAHWCLAYVEMLARDESRLQDTLKRLDVSPLGSGALAGTAYEIDRE---QLAGWLGF----ASATRNSLDSVS 230
Cdd:pfam00206 161 QDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEfaeLVAKELGFftglPVKAPNSFEATS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1221421241 231 DRDHVLELLSNASIGMVHLSRFAEDLIFFNSGEAGFVELSDRV-TSGSSLMPQKKNPDALELIRGKCGRVQG 301
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEgEPGSSIMPGKVNPDQLELLTGKAGRVMG 312
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
44-456 |
2.52e-62 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 217.02 E-value: 2.52e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 44 LVTVGVLTADEQLQLEDALNNLLEEvrlNPQQILESDA-EDIHSWVEGKLIDKVGQ-LGKKLHTGRSRNDQVATDLKLWC 121
Cdd:PRK02186 452 LGDTGIVAPERARPLLDAHRRLRDA---GFAPLLARPApRGLYMLYEAYLIERLGEdVGGVLQTARSRNDINATTTKLHL 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 122 KDTVGELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDTLKRLDVSPLGSGALA 201
Cdd:PRK02186 529 REATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHALFALFEHIDVCPLGAGAGG 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 202 GTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSNASIGMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMP 281
Cdd:PRK02186 609 GTTFPIDPEFVARLLGFEQPAPNSLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQLWTTREFALVSLPDALTGGSSMLP 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 282 QKKNPDALELIRGKCGRVQGALTGMMMTLKGLPlaYNKDMQEDKEG---LFDALDTWLDCLHMGALVLDGIQVKRPRCQE 358
Cdd:PRK02186 689 QKKNPFLLEFVKGRAGVVAGALASASAALGKTP--FSNSFEAGSPMngpIAQACAAIEDAAAVLVLLIDGLEADQARMRA 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 359 AAQQGYANSTELADYLVA-KGVPFREAHHIVGEAVVEAIRQGKPLEDLTLAELQKFSAVIGDDvypilalqsCLDKRAAK 437
Cdd:PRK02186 767 HLEDGGVSATAVAESLVVrRSISFRSAHTQVGQAIRQSLDQGRSSADALAALDPQFVSRAPLE---------WARSHRFG 837
|
410
....*....|....*....
gi 1221421241 438 GGVSPKQVAQAIADAKSRL 456
Cdd:PRK02186 838 GGPGAADLNAGLARACAAL 856
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
87-341 |
1.04e-60 |
|
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: 197.83 E-value: 1.04e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 87 WVEGKLIDKVGQLGKKLH------TGRSRNDQVATDLKLWCKDTVGELLAANRQLQSALVETAQNNQDAVMPGYTHLQRA 160
Cdd:cd01594 15 LVEEVLAGRAGELAGGLHgsalvhKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 161 QPVTFAHWCLAYVEMLARDESRLQDTlkrldvsplgsgalagtayeidreqlagwlgfasatrnsldsvsdrdHVLELLS 240
Cdd:cd01594 95 QPVTLGYELRAWAQVLGRDLERLEEA-----------------------------------------------AVAEALD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 241 NASIGMVHLSRFAEDLIFFNSGEAGFVELSDRV-TSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNK 319
Cdd:cd01594 128 ALALAAAHLSKIAEDLRLLLSGEFGELGEPFLPgQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDNE 207
|
250 260
....*....|....*....|..
gi 1221421241 320 DMQEDKEGLFDALDTWLDCLHM 341
Cdd:cd01594 208 DSPSMREILADSLLLLIDALRL 229
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
49-453 |
1.43e-48 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 173.63 E-value: 1.43e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 49 VLTADEQLQLEDA--LNNLLEEVRLNPQQIL--ESDAEDIHSWVEGKLIDKVG-QLGKKLHTGRSRNDQVATDLKLWCKD 123
Cdd:PRK06705 51 MLTEENLMKKEEAkfILHALKKVEEIPEEQLlyTEQHEDLFFLVEHLISQEAKsDFVSNMHIGRSRNDMGVTMYRMSLRR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 124 TVGELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDTLKRLDVSPLGSGALAGT 203
Cdd:PRK06705 131 YVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKTYKLLNQSPMGAAALSTT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 204 AYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSNASIGMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQK 283
Cdd:PRK06705 211 SFPIKRERVADLLGFTNVIENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLATKEYDGITVARPYVQISSIMPQK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 284 KNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQEDKEG-LFDALDTWLDCLHMGALVLDGIQVKRPRCQEAAQQ 362
Cdd:PRK06705 291 RNPVSIEHARAITSSALGEAFTVFQMIHNTPFGDIVDTEDDLQPyLYKGIEKAIRVFCIMNAVIRTMKVEEDTLKRRSYK 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 363 GYANSTELADYLVAK-GVPFREAHHIVGEAVVEAIRQGKPLEDLTLAEL-----QKFSAVIGDDVYP-ILALQSCLDKRA 435
Cdd:PRK06705 371 HAITITDFADVLTKNyGIPFRHAHHAASVIANMSLEQKKELHELCFKDVniylqEKFKIQLLEKEWEeIISPEAFIQKRN 450
|
410
....*....|....*...
gi 1221421241 436 AKGGVSPKQVAQAIADAK 453
Cdd:PRK06705 451 VYGGPSKKEMERMINNRK 468
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
1-427 |
3.25e-37 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 141.18 E-value: 3.25e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 1 MALWGGRFTQAADQRFKQF--NDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQLQLEDALNNLLEE-VRLNPQQil 77
Cdd:PRK06389 1 MKIWSGGAGEELENDFYDNivKDDIDADKNLIKYEIINLLAYHVALAQRRLITEKAPKCVINALIDIYKNgIEIDLDL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 78 esdaEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVGELlaaNRQLQSALVETAQNNQDAVMPGYTHL 157
Cdd:PRK06389 79 ----EDVHTAIENFVIRRCGDMFKNFRLFLSRNEQVHADLNLFIIDKIIEI---EKILYEIIKVIPGFNLKGRLPGYTHF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 158 QRAQPVTFAHWcLAYVE-MLARDESRLQDTLKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVL 236
Cdd:PRK06389 152 RQAMPMTVNTY-INYIKsILYHHINNLDSFLMDLREMPYGYGSGYGSPSSVKFNQMSELLGMEKNIKNPVYSSSLYIKTI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 237 ELLSNASIG-MVHLSRFAEDLIffNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPL 315
Cdd:PRK06389 231 ENISYLISSlAVDLSRICQDII--IYYENGIITIPDEFTTGSSLMPNKRNPDYLELFQGIAAESISVLSFIAQSELNKTT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 316 AYNKDMQEDKEGLFDALDTWLDCLHMGALVLDGIQVKRPRCQEAAQQGYANSTELADYlvAKGVPFREAHHIVGEAV--- 392
Cdd:PRK06389 309 GYHRDFQIVKDSTISFINNFERILLGLPDLLYNIKFEITNEKNIKNSVYATYNAWLAF--KNGMDWKSAYAYIGNKIreg 386
|
410 420 430
....*....|....*....|....*....|....*..
gi 1221421241 393 --VEAIRQGKPLEDLTLAELQKFSAVIGDDVYPILAL 427
Cdd:PRK06389 387 evLDEYQPEDLTDYIDVNELKRINHNIKIIIEPREKL 423
|
|
| ASL_C2 |
pfam14698 |
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of ... |
364-431 |
4.04e-31 |
|
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: 114.05 E-value: 4.04e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1221421241 364 YANSTELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPLEDLTLAELQKFSAVIGDDVYPILALQSCL 431
Cdd:pfam14698 1 FSTATDLADYLVRKGVPFREAHEIVGRLVRLAEEKGKDLEDLTLEELQAISPLFEEDVYEALDPEASV 68
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
99-420 |
9.84e-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: 108.87 E-value: 9.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 99 LGKKLHTGRSRNDQVATDLKLWCKDTVGELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLAR 178
Cdd:cd01597 89 AGEYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 179 DESRLQDTLKRLDVSPLGsGAlAGT-------AYEIdREQLAGWLGFASATRNSLdsvSDRDHVLELLSNasIGMVH--L 249
Cdd:cd01597 169 HRERLDELRPRVLVVQFG-GA-AGTlaslgdqGLAV-QEALAAELGLGVPAIPWH---TARDRIAELASF--LALLTgtL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 250 SRFAEDLIFFNSGEAGFV-ELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTlkglplaynkdMQEDKEGl 328
Cdd:cd01597 241 GKIARDVYLLMQTEIGEVaEPFAKGRGGSSTMPHKRNPVGCELIVALARRVPGLAALLLDA-----------MVQEHER- 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 329 fdALDTW---------LDCLHMGAL-----VLDGIQVKRPRCQE--AAQQGYANStELADYLVAKGVPFREAHHIVGEAV 392
Cdd:cd01597 309 --DAGAWhaewialpeIFLLASGALeqaefLLSGLEVNEDRMRAnlDLTGGLILS-EAVMMALAPKLGRQEAHDLVYEAC 385
|
330 340
....*....|....*....|....*...
gi 1221421241 393 VEAIRQGKPLEDLtLAELQKFSAVIGDD 420
Cdd:cd01597 386 MRAVEEGRPLREV-LLEDPEVAAYLSDE 412
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
106-409 |
8.04e-22 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 97.75 E-value: 8.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 106 GRSRNDQVATDLKLWCKDTVGELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQD 185
Cdd:PRK13353 138 AQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQ 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 186 TLKRLDVSPLGSGALaGTAYEIDRE---QLAGWLGFAS-----ATRNSLDSVSDRDHVLELLSNASIGMVHLSRFAEDLI 257
Cdd:PRK13353 218 AREHLYEVNLGGTAV-GTGLNADPEyieRVVKHLAAITglplvGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 258 FFNSG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYN-------KDMQEDKEGL 328
Cdd:PRK13353 297 LLSSGpRTGLGEINlPAVQPGSSIMPGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNvmepviaFNLLESISIL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 329 FDALDTWLD-CLHmgalvldGIQVKRPRCQEAAQQGYANSTELADYLvakgvpfreAHHIVGEAVVEAIRQGKPLEDLTL 407
Cdd:PRK13353 377 TNACRAFTDnCVK-------GIEANEERCKEYVEKSVGIATALNPHI---------GYEAAARIAKEAIATGRSVRELAL 440
|
..
gi 1221421241 408 AE 409
Cdd:PRK13353 441 EN 442
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
38-310 |
8.84e-21 |
|
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: 93.72 E-value: 8.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 38 VAWSKALVTVGVLTADEQLQLEDALNNlleeVRLNPQQILESDAE---DIHSwVEGKLIDKVGQLGKK-LHTGRSRNDQV 113
Cdd:cd01595 19 AALAEAQAELGLIPKEAAEEIRAAADV----FEIDAERIAEIEKEtghDVIA-FVYALAEKCGEDAGEyVHFGATSQDIN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 114 ATDLKLWCKDTVGELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDTLKRLDVS 193
Cdd:cd01595 94 DTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 194 ----PLGSGALAGTAYEIDREQLAGWLGFASATRNSLdsVSDRDHVLELLSnaSIGMVH--LSRFAEDLIFFNSGEAGFV 267
Cdd:cd01595 174 gisgAVGTHASLGPKGPEVEERVAEKLGLKVPPITTQ--IEPRDRIAELLS--ALALIAgtLEKIATDIRLLQRTEIGEV 249
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1221421241 268 EL---SDRVtsGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTL 310
Cdd:cd01595 250 EEpfeKGQV--GSSTMPHKRNPIDSENIEGLARLVRALAAPALENL 293
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
106-409 |
1.86e-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: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 106 GRSRNDQVATDLKLWCKDTVGELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQD 185
Cdd:cd01357 133 SQSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 186 TLKRLDVSPLGSGALaGTAYEIDRE----------QLAGwLGFASATrNSLDSVSDRDHVLELLSNASIGMVHLSRFAED 255
Cdd:cd01357 213 ARERLREVNLGGTAI-GTGINAPPGyielvveklsEITG-LPLKRAE-NLIDATQNTDAFVEVSGALKRLAVKLSKIAND 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 256 LIFFNSG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKG--------LPL-AYNkdmqed 324
Cdd:cd01357 290 LRLLSSGpRAGLGEINlPAVQPGSSIMPGKVNPVIPEVVNQVAFQVIGNDLTITMAAEAgqlelnvfEPViAYN------ 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 325 kegLFDALDtwldclHMGALV-------LDGIQVKRPRCQEAAQQGYANSTELADYLvakgvpfreAHHIVGEAVVEAIR 397
Cdd:cd01357 364 ---LLESID------ILTNAVrtlrercIDGITANEERCREYVENSIGIVTALNPYI---------GYEAAAEIAKEALE 425
|
330
....*....|..
gi 1221421241 398 QGKPLEDLTLAE 409
Cdd:cd01357 426 TGRSVRELVLEE 437
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
38-432 |
4.69e-18 |
|
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439786 [Multi-domain] Cd Length: 436 Bit Score: 85.91 E-value: 4.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 38 VAWSKALVTVGVLTADEQlqleDALNNLLEEVRLNPQQILESDAE---DIHSwVEGKLIDKVGQLGKK-LHTGRSRNDQV 113
Cdd:COG0015 29 IALAEAQAELGLIPAEAA----AAIRAAADDFEIDAERIKEIEKEtrhDVKA-FVYALKEKVGAEAGEyIHFGATSQDIN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 114 ATDLKLWCKDTVGELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDTLKRLdvs 193
Cdd:COG0015 104 DTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERV--- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 194 PLG--SGAlAGT-------AYEIDREqLAGWLGFASATrnSLDSVSDRDHVLELLSN-ASIGMVhLSRFAEDLIFFNSGE 263
Cdd:COG0015 181 LVGkiGGA-VGTyaahgeaWPEVEER-VAEKLGLKPNP--VTTQIEPRDRHAELFSAlALIAGS-LEKIARDIRLLQRTE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 264 AGFVE---LSDRVtsGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLkglplaynkdMQEDKEGLFD---------- 330
Cdd:COG0015 256 VGEVEepfAKGQV--GSSAMPHKRNPIDSENIEGLARLARALAAALLEAL----------ASWHERDLSDssvernilpd 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 331 -------ALDTWLDclhmgalVLDGIQVKRPRCQE--AAQQGYANSTELADYLVAKGVPFREAHHIVGEAVVEAIRQGKP 401
Cdd:COG0015 324 afllldgALERLLK-------LLEGLVVNPERMRAnlDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAWEEGND 396
|
410 420 430
....*....|....*....|....*....|.
gi 1221421241 402 LEDLtLAELQKFSAVIGDDvypilALQSCLD 432
Cdd:COG0015 397 LREL-LAADPEIPAELSKE-----ELEALFD 421
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
125-384 |
1.75e-15 |
|
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: 78.23 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 125 VGELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDTLKRLDVSPLGsgalaGTA 204
Cdd:cd01596 152 LERLLPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLG-----GTA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 205 ----------Y-EIDREQLA---GwLGFASATrNSLDSVSDRDHVLELLSNASIGMVHLSRFAEDLIFFNSG-EAGFVEL 269
Cdd:cd01596 227 vgtglnappgYaEKVAAELAeltG-LPFVTAP-NLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGpRAGLGEI 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 270 S-DRVTSGSSLMPQKKNP---DALELIrgkCGRVQGALTGMMMTLKG--------LPL-AYNkdMQEDKEGLFDALDTWL 336
Cdd:cd01596 305 NlPANQPGSSIMPGKVNPvipEAVNMV---AAQVIGNDTAITMAGSAgqlelnvfKPViAYN--LLQSIRLLANACRSFR 379
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1221421241 337 D-ClhmgalvLDGIQVKRPRCQEAAQQ------------GYANSTELADYLVAKGVPFREA 384
Cdd:cd01596 380 DkC-------VEGIEANEERCKEYVENslmlvtalnphiGYEKAAEIAKEALKEGRTLREA 433
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
59-294 |
1.05e-13 |
|
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: 72.20 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 59 EDALNNLLEEVRLNPQQILESDAE---DIHSWVEGkLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVGELLAANRQL 135
Cdd:cd01360 39 AEAAEEIRKKAKFDVERVKEIEAEtkhDVIAFVTA-IAEYCGEAGRYIHFGLTSSDVVDTALALQLREALDIILKDLKEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 136 QSALVETAQNNQDAVMPGYTHLQRAQPVTFAH-WCLAYVEMlARDESRLQDTLKRLDVSPLgSGALaGTAYEID---REQ 211
Cdd:cd01360 118 LEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLkFALWYAEF-KRHLERLKEARERILVGKI-SGAV-GTYANLGpevEER 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 212 LAGWLGFASATRNSldSVSDRDHVLELLSNASIGMVHLSRFAEDLIFFNSGEAGfvELSDRVTS---GSSLMPQKKNPDA 288
Cdd:cd01360 195 VAEKLGLKPEPIST--QVIQRDRHAEYLSTLALIASTLEKIATEIRHLQRTEVL--EVEEPFSKgqkGSSAMPHKRNPIL 270
|
....*.
gi 1221421241 289 LELIRG 294
Cdd:cd01360 271 SENICG 276
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
108-409 |
4.71e-13 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 70.92 E-value: 4.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 108 SRNDQVATDLKLWCKDTVGELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVT----FAhwclAYVEMLARDESRL 183
Cdd:PRK12273 142 STNDAYPTAIRIALLLSLRKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTlgqeFG----AYAVALAEDRKRL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 184 QDTLKRLDVSPLGSGAlAGT------AY-EIDREQLA---GwLGFASATrNSLDSVSDRDHVLELLSNASIGMVHLSRFA 253
Cdd:PRK12273 218 YRAAELLREVNLGATA-IGTglnappGYiELVVEKLAeitG-LPLVPAE-DLIEATQDTGAFVEVSGALKRLAVKLSKIC 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 254 EDLIFFNSG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGA-LTGMMMTLKG-------LPL-AYNkdmq 322
Cdd:PRK12273 295 NDLRLLSSGpRAGLNEINlPAVQAGSSIMPGKVNPVIPEVVNQVCFQVIGNdTTVTMAAEAGqlelnvmEPViAYN---- 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 323 edkegLFDALDTwldcLHMGALVL-----DGIQVKRPRCQEAAQQGYANSTELADYLvakgvpfreAHHIVGEAVVEAIR 397
Cdd:PRK12273 371 -----LFESISI----LTNACRTLrekciDGITANEERCREYVENSIGIVTALNPYI---------GYENAAEIAKEALE 432
|
330
....*....|..
gi 1221421241 398 QGKPLEDLTLAE 409
Cdd:PRK12273 433 TGKSVRELVLER 444
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
100-432 |
2.03e-12 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 68.89 E-value: 2.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 100 GKKLHTGRSRNDQVATDLKLWCKDTVGELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARD 179
Cdd:PRK09053 99 ARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 180 ESRLQDTLKRLDVspLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVS---DRDHVLELlsNASIGMV--HLSRFAE 254
Cdd:PRK09053 179 RQRLAALRPRALV--LQFGGAAGTLASLGEQALPVAQALAAELQLALPALPwhtQRDRIAEF--ASALGLLagTLGKIAR 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 255 DLIFFNSGEAGFV-ELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMmmtLKGLPlaynkdmQEDKEGL----- 328
Cdd:PRK09053 255 DVSLLMQTEVGEVfEPAAAGKGGSSTMPHKRNPVGCAAVLTAATRAPGLVATL---FAAMP-------QEHERALggwha 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 329 -FDALDTwLDCLHMGAL-----VLDGIQVKRPRCQEAAQQ------GYANSTELADYLvakGVPfrEAHHIVGEAVVEAI 396
Cdd:PRK09053 325 eWDTLPE-LACLAAGALaqmaqIVEGLEVDAARMRANLDLthglilAEAVMLALADRI---GRL--DAHHLVEQASKRAV 398
|
330 340 350
....*....|....*....|....*....|....*.
gi 1221421241 397 RQGKPLEDLtLAELQKFSAVIGDDvypilALQSCLD 432
Cdd:PRK09053 399 AEGRHLRDV-LAEDPQVSAHLSPA-----ALDRLLD 428
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
106-384 |
3.44e-12 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 68.18 E-value: 3.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 106 GRSRNDQVATDLKLWCKDTVGE-LLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQ 184
Cdd:PLN00134 129 SQSSNDTFPTAMHIAAATEIHSrLIPALKELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 185 DTLKRLDVSPLGSGAL-------AGTAYEIDRE--QLAGwLGFASAtRNSLDSVSDRDHVLElLSNASIGM-VHLSRFAE 254
Cdd:PLN00134 209 CTLPRLYELAQGGTAVgtglntkKGFDEKIAAAvaEETG-LPFVTA-PNKFEALAAHDAFVE-LSGALNTVaVSLMKIAN 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 255 DLIFFNSG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGalTGMMMTLKGL----------PL-AYNkdM 321
Cdd:PLN00134 286 DIRLLGSGpRCGLGELNlPENEPGSSIMPGKVNPTQCEALTMVCAQVMG--NHVAITVGGSaghfelnvfkPLiAYN--L 361
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1221421241 322 QEDKEGLFDALDTW-LDClhmgalvLDGIQVKRPRCQEAAQQ------------GYANSTELADYLVAKGVPFREA 384
Cdd:PLN00134 362 LHSIRLLGDASASFrKNC-------VRGIEANRERISKLLHEslmlvtalnpkiGYDKAAAVAKKAHKEGTTLKEA 430
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
107-292 |
3.34e-11 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 65.02 E-value: 3.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 107 RSRNDQVATDLKLWCKDTVGELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDT 186
Cdd:PRK14515 145 QSTNDAFPTAIHIATLNALEGLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQS 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 187 LKRLDVSPLGSGALaGTAYEIDREQLAGWLGFASA--------TRNSLDSVSDRDHVLELLSNASIGMVHLSRFAEDLIF 258
Cdd:PRK14515 225 RQHLYEVNMGATAV-GTGLNADPEYIEAVVKHLAAiselplvgAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRL 303
|
170 180 190
....*....|....*....|....*....|....*..
gi 1221421241 259 FNSG-EAGFVE--LSDRvTSGSSLMPQKKNPDALELI 292
Cdd:PRK14515 304 MASGpRVGLAEimLPAR-QPGSSIMPGKVNPVMPEVI 339
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
106-286 |
9.16e-11 |
|
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: 63.67 E-value: 9.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 106 GRSRND------QVATDLKLwckdtVGELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARD 179
Cdd:cd01362 133 SQSSNDtfptamHIAAALAL-----QERLLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHA 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 180 ESRLQDTLKRLDVSPLGsGALAGT------------AYEIdrEQLAGwLGFASATrNSLDSVSDRDHVLELLSNASIGMV 247
Cdd:cd01362 208 IARIEAALPRLYELALG-GTAVGTglnahpgfaekvAAEL--AELTG-LPFVTAP-NKFEALAAHDALVEASGALKTLAV 282
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1221421241 248 HLSRFAEDLIFFNSG-EAGFVELS-DRVTSGSSLMPQKKNP 286
Cdd:cd01362 283 SLMKIANDIRWLGSGpRCGLGELSlPENEPGSSIMPGKVNP 323
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
106-384 |
1.19e-10 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 63.19 E-value: 1.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 106 GRSRND------QVATDLKLwckdtVGELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARD 179
Cdd:PRK00485 137 SQSSNDtfptamHIAAVLAI-----VERLLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHG 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 180 ESRLQDTLKRLDVSPLGsGALAGT------------AYEIdrEQLAGwLGFASAtRNSLDSVSDRDhvlellsnasiGMV 247
Cdd:PRK00485 212 IERIEAALPHLYELALG-GTAVGTglnahpgfaervAEEL--AELTG-LPFVTA-PNKFEALAAHD-----------ALV 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 248 HLS-----------RFAEDLIFFNSG-EAGFVELS--DRVtSGSSLMPQKKNP---DALELIrgkCGRVQG--------A 302
Cdd:PRK00485 276 EASgalktlavslmKIANDIRWLASGpRCGLGEISlpENE-PGSSIMPGKVNPtqcEALTMV---CAQVMGndaavtfaG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 303 LTG-----MMMTLkglpLAYNkdMQEDKEGLFDAldtwldCLHMGALVLDGIQVKRPRCQEAAQQ------------GYA 365
Cdd:PRK00485 352 SQGnfelnVFKPV----IAYN--FLQSIRLLADA------MRSFADHCVVGIEPNRERIKELLERslmlvtalnphiGYD 419
|
330
....*....|....*....
gi 1221421241 366 NSTELADYLVAKGVPFREA 384
Cdd:PRK00485 420 KAAKIAKKAHKEGLTLKEA 438
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
106-290 |
8.57e-08 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 54.16 E-value: 8.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 106 GRSRNDQVATDLKLWCKDTV-GELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQ 184
Cdd:PRK12425 135 SQSSNDCFPTAMHIAAAQAVhEQLLPAIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIR 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 185 DTLKRldVSPLGSGALA---------GTAYEIDRE--QLAGwLGFASATrNSLDSVSDRDHVLELLSNASIGMVHLSRFA 253
Cdd:PRK12425 215 AALPA--VCELAQGGTAvgtglnaphGFAEAIAAElaALSG-LPFVTAP-NKFAALAGHEPLVSLSGALKTLAVALMKIA 290
|
170 180 190
....*....|....*....|....*....|....*....
gi 1221421241 254 EDLIFFNSG-EAGFVELSDRVTS-GSSLMPQKKNPDALE 290
Cdd:PRK12425 291 NDLRLLGSGpRAGLAEVRLPANEpGSSIMPGKVNPTQCE 329
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
100-292 |
4.87e-07 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 51.59 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 100 GKKLHTGRSRNDQVATDLKLWCKdTVGELLAAnrqLQSALVET-----AQNNQDAVMpGYTHLQRAQPVTFAHWCLAYVE 174
Cdd:PRK05975 99 AAHVHFGATSQDVIDTSLMLRLK-AASEILAA---RLGALIARldaleATFGQNALM-GHTRMQAAIPITVADRLASWRA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 175 MLARDESRLQDTlkRLDVSPLGSGALAGTAYEID------REQLAGWLGFASATR--NSLDSVSDRDHVLELLSNAsigm 246
Cdd:PRK05975 174 PLLRHRDRLEAL--RADVFPLQFGGAAGTLEKLGgkaaavRARLAKRLGLEDAPQwhSQRDFIADFAHLLSLVTGS---- 247
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1221421241 247 vhLSRFAEDLiffnsgeAGFVELSDRVT----SGSSLMPQKKNPDALELI 292
Cdd:PRK05975 248 --LGKFGQDI-------ALMAQAGDEISlsggGGSSAMPHKQNPVAAETL 288
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
249-435 |
1.67e-06 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 48.87 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 249 LSRFAEDLIFFNSGEAGFVELSDRVTS-GSSLMPQKKNPDALELIrgkcgrvqgalTGMMMTLKGLPLAYNKDMQEDKEG 327
Cdd:PRK08937 30 LEKFANEIRLLQRSEIREVEEPFAKGQkGSSAMPHKRNPIGSERI-----------TGLARVLRSYLVTALENVPLWHER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 328 -----------LFDA-------LDTWLDClhmgalvLDGIQVKRPRCQE--AAQQGYANSTELADYLVAKGVPFREAHHI 387
Cdd:PRK08937 99 dlshssaeriaLPDAflaldyiLNRFVNI-------LENLVVFPENIERnlDKTLGFIATERVLLELVEKGMGREEAHEL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1221421241 388 VGEAVVEAIRQGKPLEDLtLAELQKFSAVIGDDvypilALQSCLDKRA 435
Cdd:PRK08937 172 IREKAMEAWKNQKDLREL-LEADERFTKQLTKE-----ELDELFDPEA 213
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
139-286 |
3.93e-03 |
|
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: 39.61 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 139 LVETAQNNQDAVMPGYTHLQRAQPVTFA-HWCLAYVEMLA--RDESRLQDTLKRLDVS-PLGSGALAGTAYEIDREQ--- 211
Cdd:cd03302 126 LAEFALEYKDLPTLGFTHYQPAQLTTVGkRACLWIQDLLMdlRNLERLRDDLRFRGVKgTTGTQASFLDLFEGDHDKvea 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1221421241 212 ----LAGWLGFASATrNSLDSVSDRDHVLELLSN-ASIGMVhLSRFAEDLIFFnsgeAGFVELSDRVTS---GSSLMPQK 283
Cdd:cd03302 206 ldelVTKKAGFKKVY-PVTGQTYSRKVDIDVLNAlSSLGAT-AHKIATDIRLL----ANLKEVEEPFEKgqiGSSAMPYK 279
|
...
gi 1221421241 284 KNP 286
Cdd:cd03302 280 RNP 282
|
|
| |
