|
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: 1028.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTAEEQAQLEEALNVLLEDVRARPQQILESD 80
Cdd:PRK04833 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQQQLEEALNELLEEVRANPQQILASD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 81 AEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRA 160
Cdd:PRK04833 81 AEDIHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 161 QPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
Cdd:PRK04833 161 QPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 241 AAAIGMVHLSRFAEDLIFFNTGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKD 320
Cdd:PRK04833 241 DASISMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPLAYNKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 321 MQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
Cdd:PRK04833 321 MQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 16131798 401 PLEDLPLSELQKFSQVIDEDVYPILSLQSCLDKRAAKGGVSPQQVAQAIAFAQAR 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: 829.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTAEEQAQLEEALNVLLEDVRARPQQILESD 80
Cdd:PRK12308 1 MALWGGRFSQAADTRFKQFNDSLRFDYRLAEQDIVGSIAWSKALLSVGVLSEEEQQKLELALNELKLEVMEDPEQILLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 81 AEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRA 160
Cdd:PRK12308 81 AEDIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 161 QPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
Cdd:PRK12308 161 QPVTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGSGALAGTAYPIDREALAHNLGFRRATRNSLDSVSDRDHVMELMS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 241 AAAIGMVHLSRFAEDLIFFNTGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKD 320
Cdd:PRK12308 241 VASISMLHLSRLAEDLIFYNSGESGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 321 MQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
Cdd:PRK12308 321 MQEDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANATELADYLVAKGIPFREAHHIVGVAVVGAIAKGC 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131798 401 PLEDLPLSELQKFSQVIDEDVYPILSLQSCLDKRAAKGGVSPQQVAQAIAFAQARL 456
Cdd:PRK12308 401 ALEELSLEQLKEFSDVIEDDVYQILTIESCLEKRCALGGVSPEQVAYAVEQADKRL 456
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
3-457 |
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: 791.94 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 3 LWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTAEEQAQLEEALNVLLEDVRARPQqILESDAE 82
Cdd:TIGR00838 1 LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPF-ILDPDDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 83 DIHSWVEGKLIDKVG-QLGKKLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQ 161
Cdd:TIGR00838 80 DIHMAIERELIDRVGeDLGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 162 PVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSA 241
Cdd:TIGR00838 160 PITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 242 AAIGMVHLSRFAEDLIFFNTGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDM 321
Cdd:TIGR00838 240 AALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 322 QEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGKP 401
Cdd:TIGR00838 320 QEDKEPLFDALKTVELSLEMATGMLDTITVNKERMEEAASAGFSNATELADYLVRKGVPFREAHHIVGELVATAIERGKG 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 16131798 402 LEDLPLSELQKFSQVIDEDVYPILSLQSCLDKRAAKGGVSPQQVAQAIAFAQARLG 457
Cdd:TIGR00838 400 LEELTLEELQKFSPEFDEDVYEALDPESSVEKRDAKGGTAPEEVLQAIAEAKARLG 455
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
1-457 |
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: 740.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTAEEQAQLEEALNVLLEDVRARPQQILESD 80
Cdd:COG0165 3 MKLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAFEFDPEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 81 aEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRA 160
Cdd:COG0165 83 -EDIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 161 QPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
Cdd:COG0165 162 QPVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 241 AAAIGMVHLSRFAEDLIFFNTGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKD 320
Cdd:COG0165 242 AASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNKD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 321 MQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
Cdd:COG0165 322 LQEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGFSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKGK 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131798 401 PLEDLPLSELQKFSQVIDEDVYPILSLQSCLDKRAAKGGVSPQQVAQAIAFAQARLG 457
Cdd:COG0165 402 DLEDLTLEELQAFSPLIEEDVYEALDPEGSVAARDSYGGTAPEAVREQIARARARLA 458
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
1-457 |
0e+00 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 704.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTAEEQAQLEEALNVLLEDVRARPQQILESD 80
Cdd:PRK00855 4 NKLWGGRFSEGPDELVERFTASISFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILEEIEAGKFEFSPEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 81 aEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRA 160
Cdd:PRK00855 84 -EDIHMAIEARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 161 QPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
Cdd:PRK00855 163 QPVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAALAGTTFPIDRERTAELLGFDGVTENSLDAVSDRDFALEFLS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 241 AAAIGMVHLSRFAEDLIFFNTGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKD 320
Cdd:PRK00855 243 AASLLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLAYNRD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 321 MQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
Cdd:PRK00855 323 LQEDKEPLFDAVDTLKLSLEAMAGMLETLTVNKERMREAAGKGFSTATDLADYLVRKGVPFREAHEIVGKAVREAEERGV 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 16131798 401 PLEDLPLSELQKFSQVIDEDVYPILSLQSCLDKRAAKGGVSPQQVAQAIAFAQARLG 457
Cdd:PRK00855 403 DLADLSLEELQAFSPLITEDVYEVLTPEGSVAARNSIGGTAPEQVREQIARAKARLA 459
|
|
| 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: 660.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 22 SLRFDYRLAEQDIVGSVAWSKALVTVGVLTAEEQAQLEEALNVLLEDVRArPQQILESDAEDIHSWVEGKLIDKVGQLGK 101
Cdd:cd01359 1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEA-GAFELDPEDEDIHMAIERRLIERIGDVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 102 KLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDES 181
Cdd:cd01359 80 KLHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 182 RLQDALKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSAAAIGMVHLSRFAEDLIFFNT 261
Cdd:cd01359 160 RLADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 262 GEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQEDKEGLFDALDTWLDCLHM 341
Cdd:cd01359 240 QEFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 342 AALVLDGIQVKRPRCQEAAQQGYANATELADYLVA-KGVPFREAHHIVGEAVVEAIRQGKPLEDLPLSELQKFSQVIDED 420
Cdd:cd01359 320 LTGVISTLTVNPERMREAAEAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEED 399
|
410 420 430
....*....|....*....|....*....|....*.
gi 16131798 421 VYPILSLQSCLDKRAAKGGVSPQQVAQAIAFAQARL 456
Cdd:cd01359 400 VREALDPENSVERRTSYGGTAPAEVREQIARARALL 435
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
3-457 |
0e+00 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 544.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 3 LWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTAEEQAQLEEALNVLLEDVRARPQQIlESDAE 82
Cdd:PLN02646 18 LWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAGKFEW-RPDRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 83 DIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQP 162
Cdd:PLN02646 97 DVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 163 VTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSAA 242
Cdd:PLN02646 177 VLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRDFVLEFLFAN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 243 AIGMVHLSRFAEDLIFFNTGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQ 322
Cdd:PLN02646 257 SITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTAYNRDLQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 323 EDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPL 402
Cdd:PLN02646 337 EDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLDATTLADYLVRKGVPFRETHHIVGAAVALAESKGCEL 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 16131798 403 EDLPLSELQKFSQVIDEDVYPILSLQSCLDKRAAKGGVSPQQVAQAIAFAQARLG 457
Cdd:PLN02646 417 SDLTLEDLKSINPVFEEDVYEVLGVENSVEKFDSYGSTGSRSVLEQLEKWRTKLE 471
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
31-351 |
8.30e-129 |
|
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: 375.69 E-value: 8.30e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 31 EQDIVGSVAWSKALVTVGVLTAEEQAQLEEALNVLLEDVRARpQQILESDAEDIHSWVEGKLIDKVGQL-GKKLHTGRSR 109
Cdd:cd01334 2 RADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAAD-QVEQEGSGTHDVMAVEEVLAERAGELnGGYVHTGRSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 110 NDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDALKR 189
Cdd:cd01334 81 NDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 190 LDVSPLGCGALAGTAY--EIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSAAAIGMVHLSRFAEDLIFFNTGEAGFV 267
Cdd:cd01334 161 LNVLPLGGGAVGTGANapPIDRERVAELLGFFGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 268 ELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQEDKEGLFDALDTWLDCLHMAALVLD 347
Cdd:cd01334 241 ELPDAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVLE 320
|
....
gi 16131798 348 GIQV 351
Cdd:cd01334 321 GLEV 324
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
6-301 |
1.19e-127 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 372.47 E-value: 1.19e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 6 GRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTAEEQAQLEEALNVLLEDVRARPQQILESDAEDIH 85
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDDQFPLKVWQEGSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 86 SWVEGKLIDKVGQL-------GKKLHTGRSRNDQVATDLKLWCKDTVSE-LLTANRQLQSALVETAQNNQDAVMPGYTHL 157
Cdd:pfam00206 81 TAVNMNLNEVIGELlgqlvhpNDHVHTGQSSNDQVPTALRLALKDALSEvLLPALRQLIDALKEKAKEFADIVKPGRTHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 158 QRAQPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGCGALAGTAYEIDRE---QLAGWLGF----ASATRNSLDSVS 230
Cdd:pfam00206 161 QDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEfaeLVAKELGFftglPVKAPNSFEATS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 16131798 231 DRDHVLELLSAAAIGMVHLSRFAEDLIFFNTGEAGFVELSDRV-TSGSSLMPQKKNPDALELIRGKCGRVQG 301
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEgEPGSSIMPGKVNPDQLELLTGKAGRVMG 312
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
44-456 |
1.01e-65 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 226.65 E-value: 1.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 44 LVTVGVLTAEEQAQLEEALNVLLedvRARPQQILESDA-EDIHSWVEGKLIDKVGQ-LGKKLHTGRSRNDQVATDLKLWC 121
Cdd:PRK02186 452 LGDTGIVAPERARPLLDAHRRLR---DAGFAPLLARPApRGLYMLYEAYLIERLGEdVGGVLQTARSRNDINATTTKLHL 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 122 KDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGCGALA 201
Cdd:PRK02186 529 REATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHALFALFEHIDVCPLGAGAGG 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 202 GTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSAAAIGMVHLSRFAEDLIFFNTGEAGFVELSDRVTSGSSLMP 281
Cdd:PRK02186 609 GTTFPIDPEFVARLLGFEQPAPNSLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQLWTTREFALVSLPDALTGGSSMLP 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 282 QKKNPDALELIRGKCGRVQGALTGMMMTLKGLPlaYNKDMQEDKEG---LFDALDTWLDCLHMAALVLDGIQVKRPRCQE 358
Cdd:PRK02186 689 QKKNPFLLEFVKGRAGVVAGALASASAALGKTP--FSNSFEAGSPMngpIAQACAAIEDAAAVLVLLIDGLEADQARMRA 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 359 AAQQGYANATELADYLVA-KGVPFREAHHIVGEAVVEAIRQGKPLEDlPLSEL-QKFSQVIDEDvypilslqsCLDKRAA 436
Cdd:PRK02186 767 HLEDGGVSATAVAESLVVrRSISFRSAHTQVGQAIRQSLDQGRSSAD-ALAALdPQFVSRAPLE---------WARSHRF 836
|
410 420
....*....|....*....|
gi 16131798 437 KGGVSPQQVAQAIAFAQARL 456
Cdd:PRK02186 837 GGGPGAADLNAGLARACAAL 856
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
87-343 |
1.95e-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: 1.95e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 87 WVEGKLIDKVGQLGKKLH------TGRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRA 160
Cdd:cd01594 15 LVEEVLAGRAGELAGGLHgsalvhKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 161 QPVTFAHWCLAYVEMLARDESRLQDAlkrldvsplgcgalagtayeidreqlagwlgfasatrnsldsvsdrdHVLELLS 240
Cdd:cd01594 95 QPVTLGYELRAWAQVLGRDLERLEEA-----------------------------------------------AVAEALD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 241 AAAIGMVHLSRFAEDLIFFNTGEAGFVELSDRV-TSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNK 319
Cdd:cd01594 128 ALALAAAHLSKIAEDLRLLLSGEFGELGEPFLPgQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDNE 207
|
250 260
....*....|....*....|....
gi 16131798 320 DMQEDKEGLFDALDTWLDCLHMAA 343
Cdd:cd01594 208 DSPSMREILADSLLLLIDALRLLL 231
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
49-449 |
6.10e-53 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 185.19 E-value: 6.10e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 49 VLTAEEQAQLEEALNVL--LEDVRARPQQIL--ESDAEDIHSWVEGKLIDKVG-QLGKKLHTGRSRNDQVATDLKLWCKD 123
Cdd:PRK06705 51 MLTEENLMKKEEAKFILhaLKKVEEIPEEQLlyTEQHEDLFFLVEHLISQEAKsDFVSNMHIGRSRNDMGVTMYRMSLRR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 124 TVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGCGALAGT 203
Cdd:PRK06705 131 YVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKTYKLLNQSPMGAAALSTT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 204 AYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSAAAIGMVHLSRFAEDLIFFNTGEAGFVELSDRVTSGSSLMPQK 283
Cdd:PRK06705 211 SFPIKRERVADLLGFTNVIENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLATKEYDGITVARPYVQISSIMPQK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 284 KNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQEDKEG-LFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQ 362
Cdd:PRK06705 291 RNPVSIEHARAITSSALGEAFTVFQMIHNTPFGDIVDTEDDLQPyLYKGIEKAIRVFCIMNAVIRTMKVEEDTLKRRSYK 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 363 GYANATELADYLVAK-GVPFREAHHIVGEAVVEAIRQGKPLEDLPLSELQKFSQ------VIDEDVYPILSLQSCLDKRA 435
Cdd:PRK06705 371 HAITITDFADVLTKNyGIPFRHAHHAASVIANMSLEQKKELHELCFKDVNIYLQekfkiqLLEKEWEEIISPEAFIQKRN 450
|
410
....*....|....
gi 16131798 436 AKGGVSPQQVAQAI 449
Cdd:PRK06705 451 VYGGPSKKEMERMI 464
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
1-427 |
7.55e-38 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 143.11 E-value: 7.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 1 MALWGGRFTQAADQRFKQF--NDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTAEEQAQLeeaLNVLLEDVRARPQqiLE 78
Cdd:PRK06389 1 MKIWSGGAGEELENDFYDNivKDDIDADKNLIKYEIINLLAYHVALAQRRLITEKAPKCV---INALIDIYKNGIE--ID 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 79 SDAEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVSELltaNRQLQSALVETAQNNQDAVMPGYTHLQ 158
Cdd:PRK06389 76 LDLEDVHTAIENFVIRRCGDMFKNFRLFLSRNEQVHADLNLFIIDKIIEI---EKILYEIIKVIPGFNLKGRLPGYTHFR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 159 RAQPVTFAHWcLAYVE-MLARDESRLQDALKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLE 237
Cdd:PRK06389 153 QAMPMTVNTY-INYIKsILYHHINNLDSFLMDLREMPYGYGSGYGSPSSVKFNQMSELLGMEKNIKNPVYSSSLYIKTIE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 238 LLSAAAIG-MVHLSRFAEDLIffNTGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLA 316
Cdd:PRK06389 232 NISYLISSlAVDLSRICQDII--IYYENGIITIPDEFTTGSSLMPNKRNPDYLELFQGIAAESISVLSFIAQSELNKTTG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 317 YNKDMQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPrcQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAV---- 392
Cdd:PRK06389 310 YHRDFQIVKDSTISFINNFERILLGLPDLLYNIKFEIT--NEKNIKNSVYATYNAWLAFKNGMDWKSAYAYIGNKIrege 387
|
410 420 430
....*....|....*....|....*....|....*.
gi 16131798 393 -VEAIRQGKPLEDLPLSELQKFSQVIDEDVYPILSL 427
Cdd:PRK06389 388 vLDEYQPEDLTDYIDVNELKRINHNIKIIIEPREKL 423
|
|
| ASL_C2 |
pfam14698 |
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of ... |
364-431 |
1.40e-32 |
|
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: 117.90 E-value: 1.40e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 16131798 364 YANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPLEDLPLSELQKFSQVIDEDVYPILSLQSCL 431
Cdd:pfam14698 1 FSTATDLADYLVRKGVPFREAHEIVGRLVRLAEEKGKDLEDLTLEELQAISPLFEEDVYEALDPEASV 68
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
38-421 |
4.58e-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: 109.64 E-value: 4.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 38 VAWSKALVTVGVLTAEEQAQLEEALNVLLEDVRArpqqiLESDAEDI-HSwvegkLIDKVGQL--------GKKLHTGRS 108
Cdd:cd01597 29 AALARAQAELGVIPKEAAAEIAAAADVERLDLEA-----LAEATARTgHP-----AIPLVKQLtaacgdaaGEYVHWGAT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 109 RNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDALK 188
Cdd:cd01597 99 TQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 189 RLDVSPLG--CGALA---GTAYEIdREQLAGWLGFASATRNSLdsvSDRDHVLELlsAAAIGMVH--LSRFAEDLIFFNT 261
Cdd:cd01597 179 RVLVVQFGgaAGTLAslgDQGLAV-QEALAAELGLGVPAIPWH---TARDRIAEL--ASFLALLTgtLGKIARDVYLLMQ 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 262 GEAGFV-ELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTlkglplaynkdMQEDKEG-----------LF 329
Cdd:cd01597 253 TEIGEVaEPFAKGRGGSSTMPHKRNPVGCELIVALARRVPGLAALLLDA-----------MVQEHERdagawhaewiaLP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 330 DALDTWLDCLHMAALVLDGIQVKRPRCQE--AAQQGYANAtELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPLEDLPL 407
Cdd:cd01597 322 EIFLLASGALEQAEFLLSGLEVNEDRMRAnlDLTGGLILS-EAVMMALAPKLGRQEAHDLVYEACMRAVEEGRPLREVLL 400
|
410
....*....|....
gi 16131798 408 SELQKFSQVIDEDV 421
Cdd:cd01597 401 EDPEVAAYLSDEEL 414
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
38-310 |
2.50e-22 |
|
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: 97.96 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 38 VAWSKALVTVGVLTAEEQAQLEEALNVLLEDvrarPQQILESDAE---DIHSwVEGKLIDKVGQLGKK-LHTGRSRNDQV 113
Cdd:cd01595 19 AALAEAQAELGLIPKEAAEEIRAAADVFEID----AERIAEIEKEtghDVIA-FVYALAEKCGEDAGEyVHFGATSQDIN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 114 ATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDALKRLDVS 193
Cdd:cd01595 94 DTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 194 PLG--CGALAgTAYEID---REQLAGWLGFASATRNSLdsVSDRDHVLELLSAAAIGMVHLSRFAEDLIFFNTGEAGFVE 268
Cdd:cd01595 174 GISgaVGTHA-SLGPKGpevEERVAEKLGLKVPPITTQ--IEPRDRIAELLSALALIAGTLEKIATDIRLLQRTEIGEVE 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 16131798 269 L---SDRVtsGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTL 310
Cdd:cd01595 251 EpfeKGQV--GSSTMPHKRNPIDSENIEGLARLVRALAAPALENL 293
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
106-420 |
2.93e-22 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 98.90 E-value: 2.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 106 GRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQD 185
Cdd:PRK13353 138 AQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQ 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 186 ALKRLDVSPLGCGALaGTAYEIDRE---QLAGWLGFAS-----ATRNSLDSVSDRDHVLELLSAAAIGMVHLSRFAEDLI 257
Cdd:PRK13353 218 AREHLYEVNLGGTAV-GTGLNADPEyieRVVKHLAAITglplvGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 258 FFNTG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQEDKEGLFDALDTW 335
Cdd:PRK13353 297 LLSSGpRTGLGEINlPAVQPGSSIMPGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISIL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 336 LD-CLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLvakgvpfreAHHIVGEAVVEAIRQGKPLEDLPLSElqkfs 414
Cdd:PRK13353 377 TNaCRAFTDNCVKGIEANEERCKEYVEKSVGIATALNPHI---------GYEAAARIAKEAIATGRSVRELALEN----- 442
|
....*.
gi 16131798 415 QVIDED 420
Cdd:PRK13353 443 GLLSEE 448
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
106-409 |
1.31e-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: 90.66 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 106 GRSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQD 185
Cdd:cd01357 133 SQSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 186 ALKRLDVspLGCGALA-GTAYEIDRE----------QLAGwLGFASATrNSLDSVSDRDHVLELLSAAAIGMVHLSRFAE 254
Cdd:cd01357 213 ARERLRE--VNLGGTAiGTGINAPPGyielvveklsEITG-LPLKRAE-NLIDATQNTDAFVEVSGALKRLAVKLSKIAN 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 255 DLIFFNTG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKG--------LPL-AYNkdmqe 323
Cdd:cd01357 289 DLRLLSSGpRAGLGEINlPAVQPGSSIMPGKVNPVIPEVVNQVAFQVIGNDLTITMAAEAgqlelnvfEPViAYN----- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 324 dkegLFDALDTwldcLHMAALVL-----DGIQVKRPRCQEAAQQGYANATELADYLvakgvpfreAHHIVGEAVVEAIRQ 398
Cdd:cd01357 364 ----LLESIDI----LTNAVRTLrerciDGITANEERCREYVENSIGIVTALNPYI---------GYEAAAEIAKEALET 426
|
330
....*....|.
gi 16131798 399 GKPLEDLPLSE 409
Cdd:cd01357 427 GRSVRELVLEE 437
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
38-420 |
2.47e-19 |
|
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: 89.76 E-value: 2.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 38 VAWSKALVTVGVLTAEEQAQLEEALNVLLEDVRArpqqILESDAE---DIHSwVEGKLIDKVGQLGKK-LHTGRSRNDQV 113
Cdd:COG0015 29 IALAEAQAELGLIPAEAAAAIRAAADDFEIDAER----IKEIEKEtrhDVKA-FVYALKEKVGAEAGEyIHFGATSQDIN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 114 ATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDALKRLDVS 193
Cdd:COG0015 104 DTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 194 PLGcGAlAGT-------AYEIDREqLAGWLGFASATrnSLDSVSDRDHVLELLSA-AAIGMVhLSRFAED---LIFFNTG 262
Cdd:COG0015 184 KIG-GA-VGTyaahgeaWPEVEER-VAEKLGLKPNP--VTTQIEPRDRHAELFSAlALIAGS-LEKIARDirlLQRTEVG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 263 EA--GFVElsDRVtsGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLkglplaynkdMQEDKEGLFD---------- 330
Cdd:COG0015 258 EVeePFAK--GQV--GSSAMPHKRNPIDSENIEGLARLARALAAALLEAL----------ASWHERDLSDssvernilpd 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 331 -------ALDTWLDclhmaalVLDGIQVKRPRCQE--AAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGKP 401
Cdd:COG0015 324 afllldgALERLLK-------LLEGLVVNPERMRAnlDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAWEEGND 396
|
410
....*....|....*....
gi 16131798 402 LEDLpLSELQKFSQVIDED 420
Cdd:COG0015 397 LREL-LAADPEIPAELSKE 414
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
125-384 |
3.29e-16 |
|
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains aspartase (L-aspartate ammonia-lyase), fumarase class II enzymes, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.
Pssm-ID: 176468 [Multi-domain] Cd Length: 450 Bit Score: 80.55 E-value: 3.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 125 VSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGcgalaGTA 204
Cdd:cd01596 152 LERLLPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLG-----GTA 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 205 ----------Y-EIDREQLA---GwLGFASATrNSLDSVSDRDHVLELLSAAAIGMVHLSRFAEDLIFFNTG-EAGFVEL 269
Cdd:cd01596 227 vgtglnappgYaEKVAAELAeltG-LPFVTAP-NLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGpRAGLGEI 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 270 S-DRVTSGSSLMPQKKNP---DALELIrgkCGRVQGALTGMMMTLKG--------LPL-AYNkdmqedkegLFDALDTWL 336
Cdd:cd01596 305 NlPANQPGSSIMPGKVNPvipEAVNMV---AAQVIGNDTAITMAGSAgqlelnvfKPViAYN---------LLQSIRLLA 372
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 16131798 337 D-CLHMAALVLDGIQVKRPRCQEAAQQ------------GYANATELADYLVAKGVPFREA 384
Cdd:cd01596 373 NaCRSFRDKCVEGIEANEERCKEYVENslmlvtalnphiGYEKAAEIAKEALKEGRTLREA 433
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
52-294 |
7.04e-16 |
|
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP).
Pssm-ID: 176464 [Multi-domain] Cd Length: 387 Bit Score: 79.13 E-value: 7.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 52 AEEQAQL----EEALNVLLEDVRARPQQILESDAE---DIHSWVEGkLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDT 124
Cdd:cd01360 28 CEAWAKLgvipAEAAEEIRKKAKFDVERVKEIEAEtkhDVIAFVTA-IAEYCGEAGRYIHFGLTSSDVVDTALALQLREA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 125 VSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAH-WCLAYVEMlARDESRLQDALKRLDVSPLGcGALaGT 203
Cdd:cd01360 107 LDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLkFALWYAEF-KRHLERLKEARERILVGKIS-GAV-GT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 204 AYEID---REQLAGWLGFASATRNSldSVSDRDHVLELLSAAAIGMVHLSRFAEDLIFFNTGEAGfvELSDRVTS---GS 277
Cdd:cd01360 184 YANLGpevEERVAEKLGLKPEPIST--QVIQRDRHAEYLSTLALIASTLEKIATEIRHLQRTEVL--EVEEPFSKgqkGS 259
|
250
....*....|....*..
gi 16131798 278 SLMPQKKNPDALELIRG 294
Cdd:cd01360 260 SAMPHKRNPILSENICG 276
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
108-409 |
1.98e-13 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 72.08 E-value: 1.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 108 SRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVT----FAhwclAYVEMLARDESRL 183
Cdd:PRK12273 142 STNDAYPTAIRIALLLSLRKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTlgqeFG----AYAVALAEDRKRL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 184 QDALKRLDVSPLGcgalaGTA----------Y-EIDREQLA---GwLGFASATrNSLDSVSDRDHVLELLSAAAIGMVHL 249
Cdd:PRK12273 218 YRAAELLREVNLG-----ATAigtglnappgYiELVVEKLAeitG-LPLVPAE-DLIEATQDTGAFVEVSGALKRLAVKL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 250 SRFAEDLIFFNTG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGA-LTGMMMTLKG-------LPL-AYN 318
Cdd:PRK12273 291 SKICNDLRLLSSGpRAGLNEINlPAVQAGSSIMPGKVNPVIPEVVNQVCFQVIGNdTTVTMAAEAGqlelnvmEPViAYN 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 319 kdmqedkegLFDALDTwldcLHMAALVL-----DGIQVKRPRCQEAAQQGYANATELADYLvakgvpfreAHHIVGEAVV 393
Cdd:PRK12273 371 ---------LFESISI----LTNACRTLrekciDGITANEERCREYVENSIGIVTALNPYI---------GYENAAEIAK 428
|
330
....*....|....*.
gi 16131798 394 EAIRQGKPLEDLPLSE 409
Cdd:PRK12273 429 EALETGKSVRELVLER 444
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
39-404 |
1.30e-12 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 69.27 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 39 AWSKALVTVGVLTAEEQAQLEEALNVLLEDVRARPQQILESdaedihswveGKL-IDKVGQLGKK-----------LHTG 106
Cdd:PRK09053 36 ALARAEAACGVIPAAAVAPIEAACDAERLDLDALAQAAALA----------GNLaIPLVKQLTAQvaardaeaaryVHWG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 107 RSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDA 186
Cdd:PRK09053 106 ATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 187 LKRLDVspLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVS---DRDHVLELlsAAAIGMV--HLSRFAEDLIFFNT 261
Cdd:PRK09053 186 RPRALV--LQFGGAAGTLASLGEQALPVAQALAAELQLALPALPwhtQRDRIAEF--ASALGLLagTLGKIARDVSLLMQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 262 GEAGFV-ELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMmmtLKGLPlaynkdmQEDKEGL------FDALDT 334
Cdd:PRK09053 262 TEVGEVfEPAAAGKGGSSTMPHKRNPVGCAAVLTAATRAPGLVATL---FAAMP-------QEHERALggwhaeWDTLPE 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16131798 335 wLDCLHMAAL-----VLDGIQVKRPRCQE--AAQQG--YANATELAdylVAKGVPFREAHHIVGEAVVEAIRQGKPLED 404
Cdd:PRK09053 332 -LACLAAGALaqmaqIVEGLEVDAARMRAnlDLTHGliLAEAVMLA---LADRIGRLDAHHLVEQASKRAVAEGRHLRD 406
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
106-384 |
4.73e-12 |
|
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: 67.53 E-value: 4.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 106 GRSRND------QVATDLKLwckdtVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARD 179
Cdd:cd01362 133 SQSSNDtfptamHIAAALAL-----QERLLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHA 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 180 ESRLQDALKRLDVSPLGcGALAGT------------AYEIdrEQLAGwLGFASATrNSLDSVSDRDHVLELLSAAAIGMV 247
Cdd:cd01362 208 IARIEAALPRLYELALG-GTAVGTglnahpgfaekvAAEL--AELTG-LPFVTAP-NKFEALAAHDALVEASGALKTLAV 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 248 HLSRFAEDLIFFNTG-EAGFVELS-DRVTSGSSLMPQKKNP---DALELIrgkCGRVQGALTGmmMTLKG---------- 312
Cdd:cd01362 283 SLMKIANDIRWLGSGpRCGLGELSlPENEPGSSIMPGKVNPtqcEALTMV---AAQVMGNDAA--ITIAGssgnfelnvf 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 313 LPL-AYNkdMQEDKEGLFDAldtwldCLHMAALVLDGIQVKRPRCQEAAQQ------------GYANATELADYLVAKGV 379
Cdd:cd01362 358 KPViIYN--LLQSIRLLADA------CRSFADKCVAGIEPNRERIAELLERslmlvtalnphiGYDKAAKIAKKAHKEGL 429
|
....*
gi 16131798 380 PFREA 384
Cdd:cd01362 430 TLKEA 434
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
106-384 |
7.45e-12 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 67.02 E-value: 7.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 106 GRSRNDQVATDLKLWCKDTV-SELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQ 184
Cdd:PLN00134 129 SQSSNDTFPTAMHIAAATEIhSRLIPALKELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 185 DALKRLDVSPLGCGAL-------AGTAYEIDRE--QLAGwLGFASAtRNSLDSVSDRDHVLELLSAAAIGMVHLSRFAED 255
Cdd:PLN00134 209 CTLPRLYELAQGGTAVgtglntkKGFDEKIAAAvaEETG-LPFVTA-PNKFEALAAHDAFVELSGALNTVAVSLMKIAND 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 256 LIFFNTG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGalTGMMMTLKGL----------PL-AYNkdMQ 322
Cdd:PLN00134 287 IRLLGSGpRCGLGELNlPENEPGSSIMPGKVNPTQCEALTMVCAQVMG--NHVAITVGGSaghfelnvfkPLiAYN--LL 362
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16131798 323 EDKEGLFDALDTwldclhMAALVLDGIQVKRPRCQEAAQQ------------GYANATELADYLVAKGVPFREA 384
Cdd:PLN00134 363 HSIRLLGDASAS------FRKNCVRGIEANRERISKLLHEslmlvtalnpkiGYDKAAAVAKKAHKEGTTLKEA 430
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
107-292 |
1.69e-11 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 66.18 E-value: 1.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 107 RSRNDQVATDLKLWCKDTVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDA 186
Cdd:PRK14515 145 QSTNDAFPTAIHIATLNALEGLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQS 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 187 LKRLDVSPLGCGALaGTAYEIDREQLAGWLGFASA--------TRNSLDSVSDRDHVLELLSAAAIGMVHLSRFAEDLIF 258
Cdd:PRK14515 225 RQHLYEVNMGATAV-GTGLNADPEYIEAVVKHLAAiselplvgAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRL 303
|
170 180 190
....*....|....*....|....*....|....*..
gi 16131798 259 FNTG-EAGFVE--LSDRvTSGSSLMPQKKNPDALELI 292
Cdd:PRK14515 304 MASGpRVGLAEimLPAR-QPGSSIMPGKVNPVMPEVI 339
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
106-384 |
2.02e-11 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 65.50 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 106 GRSRND------QVATDLKLwckdtVSELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARD 179
Cdd:PRK00485 137 SQSSNDtfptamHIAAVLAI-----VERLLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHG 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 180 ESRLQDALKRLDVSPLGcGALAGT------------AYEIdrEQLAGwLGFASAtRNSLDSVSDRDHVLEL---LSAAAi 244
Cdd:PRK00485 212 IERIEAALPHLYELALG-GTAVGTglnahpgfaervAEEL--AELTG-LPFVTA-PNKFEALAAHDALVEAsgaLKTLA- 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 245 gmVHLSRFAEDLIFFNTG-EAGFVELS--DRVtSGSSLMPQKKNP---DALELIrgkCGRVQG--------ALTG----- 305
Cdd:PRK00485 286 --VSLMKIANDIRWLASGpRCGLGEISlpENE-PGSSIMPGKVNPtqcEALTMV---CAQVMGndaavtfaGSQGnfeln 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 306 MMMTLkglpLAYNkdMQEDKEGLFDAldtwldCLHMAALVLDGIQVKRPRCQEAAQQ------------GYANATELADY 373
Cdd:PRK00485 360 VFKPV----IAYN--FLQSIRLLADA------MRSFADHCVVGIEPNRERIKELLERslmlvtalnphiGYDKAAKIAKK 427
|
330
....*....|.
gi 16131798 374 LVAKGVPFREA 384
Cdd:PRK00485 428 AHKEGLTLKEA 438
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
106-290 |
7.85e-08 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 54.54 E-value: 7.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 106 GRSRNDQVATDLKLWCKDTV-SELLTANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQ 184
Cdd:PRK12425 135 SQSSNDCFPTAMHIAAAQAVhEQLLPAIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIR 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 185 DALKRldVSPLGCGALA---------GTAYEIDRE--QLAGwLGFASATrNSLDSVSDRDHVLELLSAAAIGMVHLSRFA 253
Cdd:PRK12425 215 AALPA--VCELAQGGTAvgtglnaphGFAEAIAAElaALSG-LPFVTAP-NKFAALAGHEPLVSLSGALKTLAVALMKIA 290
|
170 180 190
....*....|....*....|....*....|....*....
gi 16131798 254 EDLIFFNTG-EAGFVELSDRVTS-GSSLMPQKKNPDALE 290
Cdd:PRK12425 291 NDLRLLGSGpRAGLAEVRLPANEpGSSIMPGKVNPTQCE 329
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
30-292 |
5.56e-07 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 51.21 E-value: 5.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 30 AEQDIVGSVAWSKALVT----VGVLTAEEQAQLEEALNVLLEDVrARPQQILESDAEDIHSWVeGKLIDKVG-QLGKKLH 104
Cdd:PRK05975 26 AEADIAAMLAFEAALAEaeaeHGIIPAEAAERIAAACETFEPDL-AALRHATARDGVVVPALV-RQLRAAVGeEAAAHVH 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 105 TGRSRNDQVATDLKLWCKdTVSELLTAnrqLQSALVET-----AQNNQDAVMpGYTHLQRAQPVTFAHWCLAYVEMLARD 179
Cdd:PRK05975 104 FGATSQDVIDTSLMLRLK-AASEILAA---RLGALIARldaleATFGQNALM-GHTRMQAAIPITVADRLASWRAPLLRH 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 180 ESRLQDAlkRLDVSPLGCGALAGTAYEID------REQLAGWLGFASATR--NSLDSVSDRDHVLELLSAAaigmvhLSR 251
Cdd:PRK05975 179 RDRLEAL--RADVFPLQFGGAAGTLEKLGgkaaavRARLAKRLGLEDAPQwhSQRDFIADFAHLLSLVTGS------LGK 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 16131798 252 FAEDLiffntgeAGFVELSDRVT----SGSSLMPQKKNPDALELI 292
Cdd:PRK05975 251 FGQDI-------ALMAQAGDEISlsggGGSSAMPHKQNPVAAETL 288
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
249-435 |
1.38e-06 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 48.87 E-value: 1.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 249 LSRFAEDLIFFNTGEAGFVELSDRVTS-GSSLMPQKKNPDALELIrgkcgrvqgalTGMMMTLKGLPLAYNKDMQEDKEG 327
Cdd:PRK08937 30 LEKFANEIRLLQRSEIREVEEPFAKGQkGSSAMPHKRNPIGSERI-----------TGLARVLRSYLVTALENVPLWHER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 328 -----------LFDALDTWLDCLHMAALVLDGIQVKRPRCQ-EAAQQGYANATE-LADYLVAKGVPFREAHHIVGEAVVE 394
Cdd:PRK08937 99 dlshssaeriaLPDAFLALDYILNRFVNILENLVVFPENIErNLDKTLGFIATErVLLELVEKGMGREEAHELIREKAME 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 16131798 395 AIRQGKPLEDLpLSELQKFSQVIDEDvypilSLQSCLDKRA 435
Cdd:PRK08937 179 AWKNQKDLREL-LEADERFTKQLTKE-----ELDELFDPEA 213
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
139-286 |
8.16e-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: 38.45 E-value: 8.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 139 LVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDALKRLDV----SPLGCGALAGTAYEIDREQ--- 211
Cdd:cd03302 126 LAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFrgvkGTTGTQASFLDLFEGDHDKvea 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 212 ----LAGWLGFASATrNSLDSVSDRDHVLELLSA-AAIGMVhLSRFAEDLIFFntgeAGFVELSDRVTS---GSSLMPQK 283
Cdd:cd03302 206 ldelVTKKAGFKKVY-PVTGQTYSRKVDIDVLNAlSSLGAT-AHKIATDIRLL----ANLKEVEEPFEKgqiGSSAMPYK 279
|
...
gi 16131798 284 KNP 286
Cdd:cd03302 280 RNP 282
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
38-286 |
9.49e-03 |
|
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the product of the purB gene in Escherichia coli, and related proteins. It is a member of the Lyase class I family of the Lyase_I superfamily. Members of the Lyase class I family function as homotetramers to catalyze similar beta-elimination reactions in which a Calpha-N or Calpha-O bond is cleaved with the subsequent release of fumarate as one of the products. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two non-sequential steps in the de novo purine biosynthesis pathway: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylosuccinate (SAMP) into adenosine monophosphate (AMP).
Pssm-ID: 176470 [Multi-domain] Cd Length: 425 Bit Score: 38.37 E-value: 9.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 38 VAWSKALV------TVGVLTAEEQAQLEE-ALNVLLEDVrarpQQILESDAEDIHS------WVEGKlIDKVGQLGKKL- 103
Cdd:cd01598 19 VEWLIALSnleeipEVPPLTKEELKFLRAiIENFSEEDA----LRIKEIEATTNHDvkaveyFLKEK-FETLGLLKKIKe 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 104 --HTGRSRNDQVATDLKLWCKDTVSELLTAN-RQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEmlarde 180
Cdd:cd01598 94 fiHFACTSEDINNLAYALMIKEARNEVILPLlKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVY------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16131798 181 sRLQDALKRL-DVSPLGC--GAlAGT------AY-EIDreqlagWLGFASATRNSLD--------SVSDRDHVLELLSAa 242
Cdd:cd01598 168 -RLERQYKQLkQIEILGKfnGA-VGNfnahlvAYpDVD------WRKFSEFFVTSLGltwnpyttQIEPHDYIAELFDA- 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 16131798 243 aigMVHLSRFAEDL-----------IFFNTGEAGFVelsdrvtsGSSLMPQKKNP 286
Cdd:cd01598 239 ---LARINTILIDLcrdiwgyislgYFKQKVKKGEV--------GSSTMPHKVNP 282
|
|
| |
