|
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 493180901 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQLQLEEALNNLLEEVRLDPAQILQSD 80
Cdd:PRK04833 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQQQLEEALNELLEEVRANPQQILASD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 81 AEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVAELLAANRQLQSALVETAQNNQDAVMPGYTHLQRA 160
Cdd:PRK04833 81 AEDIHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 161 QPVTFAHWCLAYVEMLARDESRLQDTLKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
Cdd:PRK04833 161 QPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 241 NASIGMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKD 320
Cdd:PRK04833 241 DASISMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPLAYNKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 321 MQEDKEGLFDALDTWLDCLHMGALVLDGIQVKRPRCQEAAQQGYANSTELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
Cdd:PRK04833 321 MQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 493180901 401 PLEDLPLADLQKFSAVIGEDVYPILALQSCLDKRAAKGGVSPKQVAQAIADAKNR 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: 830.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQLQLEEALNNLLEEVRLDPAQILQSD 80
Cdd:PRK12308 1 MALWGGRFSQAADTRFKQFNDSLRFDYRLAEQDIVGSIAWSKALLSVGVLSEEEQQKLELALNELKLEVMEDPEQILLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 81 AEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVAELLAANRQLQSALVETAQNNQDAVMPGYTHLQRA 160
Cdd:PRK12308 81 AEDIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 161 QPVTFAHWCLAYVEMLARDESRLQDTLKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
Cdd:PRK12308 161 QPVTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGSGALAGTAYPIDREALAHNLGFRRATRNSLDSVSDRDHVMELMS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 241 NASIGMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKD 320
Cdd:PRK12308 241 VASISMLHLSRLAEDLIFYNSGESGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 321 MQEDKEGLFDALDTWLDCLHMGALVLDGIQVKRPRCQEAAQQGYANSTELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
Cdd:PRK12308 321 MQEDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANATELADYLVAKGIPFREAHHIVGVAVVGAIAKGC 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 493180901 401 PLEDLPLADLQKFSAVIGEDVYPILALQSCLDKRAAKGGVSPKQVAQAIADAKNRL 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: 772.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 3 LWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQLQLEEALNNLLEEVRLDPaQILQSDAE 82
Cdd:TIGR00838 1 LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGP-FILDPDDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 83 DIHSWVEGKLIDKVG-QLGKKLHTGRSRNDQVATDLKLWCKDTVAELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQ 161
Cdd:TIGR00838 80 DIHMAIERELIDRVGeDLGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 162 PVTFAHWCLAYVEMLARDESRLQDTLKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSN 241
Cdd:TIGR00838 160 PITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 242 ASIGMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDM 321
Cdd:TIGR00838 240 AALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 322 QEDKEGLFDALDTWLDCLHMGALVLDGIQVKRPRCQEAAQQGYANSTELADYLVAKGVPFREAHHIVGEAVVEAIRQGKP 401
Cdd:TIGR00838 320 QEDKEPLFDALKTVELSLEMATGMLDTITVNKERMEEAASAGFSNATELADYLVRKGVPFREAHHIVGELVATAIERGKG 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 493180901 402 LEDLPLADLQKFSAVIGEDVYPILALQSCLDKRAAKGGVSPKQVAQAIADAKNRL 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: 736.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQLQLEEALNNLLEEVRLDPAQiLQSD 80
Cdd:COG0165 3 MKLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAFE-FDPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 81 AEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVAELLAANRQLQSALVETAQNNQDAVMPGYTHLQRA 160
Cdd:COG0165 82 LEDIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 161 QPVTFAHWCLAYVEMLARDESRLQDTLKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
Cdd:COG0165 162 QPVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 241 NASIGMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKD 320
Cdd:COG0165 242 AASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNKD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 321 MQEDKEGLFDALDTWLDCLHMGALVLDGIQVKRPRCQEAAQQGYANSTELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
Cdd:COG0165 322 LQEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGFSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKGK 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 493180901 401 PLEDLPLADLQKFSAVIGEDVYPILALQSCLDKRAAKGGVSPKQVAQAIADAKNRL 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: 696.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQLQLEEALNNLLEEVRLDPAQILQSD 80
Cdd:PRK00855 4 NKLWGGRFSEGPDELVERFTASISFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILEEIEAGKFEFSPEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 81 aEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVAELLAANRQLQSALVETAQNNQDAVMPGYTHLQRA 160
Cdd:PRK00855 84 -EDIHMAIEARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 161 QPVTFAHWCLAYVEMLARDESRLQDTLKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
Cdd:PRK00855 163 QPVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAALAGTTFPIDRERTAELLGFDGVTENSLDAVSDRDFALEFLS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 241 NASIGMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKD 320
Cdd:PRK00855 243 AASLLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLAYNRD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 321 MQEDKEGLFDALDTWLDCLHMGALVLDGIQVKRPRCQEAAQQGYANSTELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
Cdd:PRK00855 323 LQEDKEPLFDAVDTLKLSLEAMAGMLETLTVNKERMREAAGKGFSTATDLADYLVRKGVPFREAHEIVGKAVREAEERGV 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 493180901 401 PLEDLPLADLQKFSAVIGEDVYPILALQSCLDKRAAKGGVSPKQVAQAIADAKNRL 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: 653.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 22 SLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQLQLEEALNNLLEEVRlDPAQILQSDAEDIHSWVEGKLIDKVGQLGK 101
Cdd:cd01359 1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIE-AGAFELDPEDEDIHMAIERRLIERIGDVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 102 KLHTGRSRNDQVATDLKLWCKDTVAELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDES 181
Cdd:cd01359 80 KLHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 182 RLQDTLKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSNASIGMVHLSRFAEDLIFFNS 261
Cdd:cd01359 160 RLADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 262 GEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQEDKEGLFDALDTWLDCLHM 341
Cdd:cd01359 240 QEFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 342 GALVLDGIQVKRPRCQEAAQQGYANSTELADYLVA-KGVPFREAHHIVGEAVVEAIRQGKPLEDLPLADLQKFSAVIGED 420
Cdd:cd01359 320 LTGVISTLTVNPERMREAAEAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEED 399
|
410 420 430
....*....|....*....|....*....|....*.
gi 493180901 421 VYPILALQSCLDKRAAKGGVSPKQVAQAIADAKNRL 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: 544.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 3 LWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQLQLEEALNNLLEEVRLDPAQIlQSDAE 82
Cdd:PLN02646 18 LWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAGKFEW-RPDRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 83 DIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVAELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQP 162
Cdd:PLN02646 97 DVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 163 VTFAHWCLAYVEMLARDESRLQDTLKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSNA 242
Cdd:PLN02646 177 VLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRDFVLEFLFAN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 243 SIGMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQ 322
Cdd:PLN02646 257 SITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTAYNRDLQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 323 EDKEGLFDALDTWLDCLHMGALVLDGIQVKRPRCQEAAQQGYANSTELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPL 402
Cdd:PLN02646 337 EDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLDATTLADYLVRKGVPFRETHHIVGAAVALAESKGCEL 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 493180901 403 EDLPLADLQKFSAVIGEDVYPILALQSCLDKRAAKGGVSPKQVAQAIADAKNRL 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 |
4.63e-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: 368.75 E-value: 4.63e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 31 EQDIVGSVAWSKALVTVGVLTADEQLQLEEALNNLLEEVRLDPAQILQSDaEDIHSWVEGKLIDKVGQL-GKKLHTGRSR 109
Cdd:cd01334 2 RADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVEQEGSG-THDVMAVEEVLAERAGELnGGYVHTGRSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 110 NDQVATDLKLWCKDTVAELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDTLKR 189
Cdd:cd01334 81 NDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 190 LDVSPLGCGALAGTAY--EIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSNASIGMVHLSRFAEDLIFFNSGEAGFV 267
Cdd:cd01334 161 LNVLPLGGGAVGTGANapPIDRERVAELLGFFGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 268 ELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQEDKEGLFDALDTWLDCLHMGALVLD 347
Cdd:cd01334 241 ELPDAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVLE 320
|
....
gi 493180901 348 GIQV 351
Cdd:cd01334 321 GLEV 324
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
6-301 |
9.38e-124 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 362.46 E-value: 9.38e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 6 GRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQLQLEEALNNLLEEVRLDPAQILQSDAEDIH 85
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDDQFPLKVWQEGSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 86 SWVEGKLIDKVGQL-------GKKLHTGRSRNDQVATDLKLWCKDTVAE-LLAANRQLQSALVETAQNNQDAVMPGYTHL 157
Cdd:pfam00206 81 TAVNMNLNEVIGELlgqlvhpNDHVHTGQSSNDQVPTALRLALKDALSEvLLPALRQLIDALKEKAKEFADIVKPGRTHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 158 QRAQPVTFAHWCLAYVEMLARDESRLQDTLKRLDVSPLGCGALAGTAYEIDRE---QLAGWLGF----ASATRNSLDSVS 230
Cdd:pfam00206 161 QDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEfaeLVAKELGFftglPVKAPNSFEATS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 493180901 231 DRDHVLELLSNASIGMVHLSRFAEDLIFFNSGEAGFVELSDRV-TSGSSLMPQKKNPDALELIRGKCGRVQG 301
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEgEPGSSIMPGKVNPDQLELLTGKAGRVMG 312
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
87-341 |
7.81e-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: 198.22 E-value: 7.81e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 87 WVEGKLIDKVGQLGKKLH------TGRSRNDQVATDLKLWCKDTVAELLAANRQLQSALVETAQNNQDAVMPGYTHLQRA 160
Cdd:cd01594 15 LVEEVLAGRAGELAGGLHgsalvhKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 161 QPVTFAHWCLAYVEMLARDESRLQDTlkrldvsplgcgalagtayeidreqlagwlgfasatrnsldsvsdrdHVLELLS 240
Cdd:cd01594 95 QPVTLGYELRAWAQVLGRDLERLEEA-----------------------------------------------AVAEALD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 241 NASIGMVHLSRFAEDLIFFNSGEAGFVELSDRV-TSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNK 319
Cdd:cd01594 128 ALALAAAHLSKIAEDLRLLLSGEFGELGEPFLPgQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDNE 207
|
250 260
....*....|....*....|..
gi 493180901 320 DMQEDKEGLFDALDTWLDCLHM 341
Cdd:cd01594 208 DSPSMREILADSLLLLIDALRL 229
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
44-456 |
5.44e-60 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 210.86 E-value: 5.44e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 44 LVTVGVLTADEQLQLEEALNNLLEEvrlDPAQILQSDA-EDIHSWVEGKLIDKVGQ-LGKKLHTGRSRNDQVATDLKLWC 121
Cdd:PRK02186 452 LGDTGIVAPERARPLLDAHRRLRDA---GFAPLLARPApRGLYMLYEAYLIERLGEdVGGVLQTARSRNDINATTTKLHL 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 122 KDTVAELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDTLKRLDVSPLGCGALA 201
Cdd:PRK02186 529 REATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHALFALFEHIDVCPLGAGAGG 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 202 GTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSNASIGMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMP 281
Cdd:PRK02186 609 GTTFPIDPEFVARLLGFEQPAPNSLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQLWTTREFALVSLPDALTGGSSMLP 688
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 282 QKKNPDALELIRGKCGRVQGALTGMMMTLKGLPlaYNKDMQEDKEG---LFDALDTWLDCLHMGALVLDGIQVKRPRCQE 358
Cdd:PRK02186 689 QKKNPFLLEFVKGRAGVVAGALASASAALGKTP--FSNSFEAGSPMngpIAQACAAIEDAAAVLVLLIDGLEADQARMRA 766
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 359 AAQQGYANSTELADYLVA-KGVPFREAHHIVGEAVVEAIRQGKPLEDlPLADL-QKFSAVIGEDvypilalqsCLDKRAA 436
Cdd:PRK02186 767 HLEDGGVSATAVAESLVVrRSISFRSAHTQVGQAIRQSLDQGRSSAD-ALAALdPQFVSRAPLE---------WARSHRF 836
|
410 420
....*....|....*....|
gi 493180901 437 KGGVSPKQVAQAIADAKNRL 456
Cdd:PRK02186 837 GGGPGAADLNAGLARACAAL 856
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
49-453 |
1.09e-49 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 176.71 E-value: 1.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 49 VLTADEQLQLEEA--LNNLLEEVRLDPAQIL--QSDAEDIHSWVEGKLIDKVG-QLGKKLHTGRSRNDQVATDLKLWCKD 123
Cdd:PRK06705 51 MLTEENLMKKEEAkfILHALKKVEEIPEEQLlyTEQHEDLFFLVEHLISQEAKsDFVSNMHIGRSRNDMGVTMYRMSLRR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 124 TVAELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDTLKRLDVSPLGCGALAGT 203
Cdd:PRK06705 131 YVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKTYKLLNQSPMGAAALSTT 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 204 AYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSNASIGMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQK 283
Cdd:PRK06705 211 SFPIKRERVADLLGFTNVIENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLATKEYDGITVARPYVQISSIMPQK 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 284 KNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQEDKEG-LFDALDTWLDCLHMGALVLDGIQVKRPRCQEAAQQ 362
Cdd:PRK06705 291 RNPVSIEHARAITSSALGEAFTVFQMIHNTPFGDIVDTEDDLQPyLYKGIEKAIRVFCIMNAVIRTMKVEEDTLKRRSYK 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 363 GYANSTELADYLVAK-GVPFREAHHIVGEAVVEAIRQGKPLEDLPLADL-----QKFSAVIGEDVYP-ILALQSCLDKRA 435
Cdd:PRK06705 371 HAITITDFADVLTKNyGIPFRHAHHAASVIANMSLEQKKELHELCFKDVniylqEKFKIQLLEKEWEeIISPEAFIQKRN 450
|
410
....*....|....*...
gi 493180901 436 AKGGVSPKQVAQAIADAK 453
Cdd:PRK06705 451 VYGGPSKKEMERMINNRK 468
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
1-427 |
9.33e-38 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 142.73 E-value: 9.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 1 MALWGGRFTQAADQRFKQF--NDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQLQLEEALNNLLEE-VRLDPaqil 77
Cdd:PRK06389 1 MKIWSGGAGEELENDFYDNivKDDIDADKNLIKYEIINLLAYHVALAQRRLITEKAPKCVINALIDIYKNgIEIDL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 78 qsDAEDIHSWVEGKLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVAELlaaNRQLQSALVETAQNNQDAVMPGYTHL 157
Cdd:PRK06389 77 --DLEDVHTAIENFVIRRCGDMFKNFRLFLSRNEQVHADLNLFIIDKIIEI---EKILYEIIKVIPGFNLKGRLPGYTHF 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 158 QRAQPVTFAHWcLAYVE-MLARDESRLQDTLKRLDVSPLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVL 236
Cdd:PRK06389 152 RQAMPMTVNTY-INYIKsILYHHINNLDSFLMDLREMPYGYGSGYGSPSSVKFNQMSELLGMEKNIKNPVYSSSLYIKTI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 237 ELLSNASIG-MVHLSRFAEDLIffNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPL 315
Cdd:PRK06389 231 ENISYLISSlAVDLSRICQDII--IYYENGIITIPDEFTTGSSLMPNKRNPDYLELFQGIAAESISVLSFIAQSELNKTT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 316 AYNKDMQEDKEGLFDALDTWLDCLHMGALVLDGIQVKRPRCQEAAQQGYANSTELADYlvAKGVPFREAHHIVGEAV--- 392
Cdd:PRK06389 309 GYHRDFQIVKDSTISFINNFERILLGLPDLLYNIKFEITNEKNIKNSVYATYNAWLAF--KNGMDWKSAYAYIGNKIreg 386
|
410 420 430
....*....|....*....|....*....|....*..
gi 493180901 393 --VEAIRQGKPLEDLPLADLQKFSAVIGEDVYPILAL 427
Cdd:PRK06389 387 evLDEYQPEDLTDYIDVNELKRINHNIKIIIEPREKL 423
|
|
| ASL_C2 |
pfam14698 |
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of ... |
364-431 |
9.10e-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: 113.28 E-value: 9.10e-31
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 493180901 364 YANSTELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPLEDLPLADLQKFSAVIGEDVYPILALQSCL 431
Cdd:pfam14698 1 FSTATDLADYLVRKGVPFREAHEIVGRLVRLAEEKGKDLEDLTLEELQAISPLFEEDVYEALDPEASV 68
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
38-409 |
1.54e-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: 111.18 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 38 VAWSKALVTVGVLTADEQLQLEEALNnlleEVRLDPAQILQSDAEDIHSwvegkLIDKVGQL--------GKKLHTGRSR 109
Cdd:cd01597 29 AALARAQAELGVIPKEAAAEIAAAAD----VERLDLEALAEATARTGHP-----AIPLVKQLtaacgdaaGEYVHWGATT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 110 NDQVATDLKLWCKDTVAELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDTLKR 189
Cdd:cd01597 100 QDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPR 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 190 LDVSPLG--CGALA---GTAYEIdREQLAGWLGFASATRNSLdsvSDRDHVLELLSNasIGMVH--LSRFAEDLIFFNSG 262
Cdd:cd01597 180 VLVVQFGgaAGTLAslgDQGLAV-QEALAAELGLGVPAIPWH---TARDRIAELASF--LALLTgtLGKIARDVYLLMQT 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 263 EAGFV-ELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTlkglplaynkdMQEDKEGlfdALDTW------ 335
Cdd:cd01597 254 EIGEVaEPFAKGRGGSSTMPHKRNPVGCELIVALARRVPGLAALLLDA-----------MVQEHER---DAGAWhaewia 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 336 ---LDCLHMGAL-----VLDGIQVKRPRCQE--AAQQGYANStELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPLEDL 405
Cdd:cd01597 320 lpeIFLLASGALeqaefLLSGLEVNEDRMRAnlDLTGGLILS-EAVMMALAPKLGRQEAHDLVYEACMRAVEEGRPLREV 398
|
....
gi 493180901 406 PLAD 409
Cdd:cd01597 399 LLED 402
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
38-310 |
1.35e-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: 96.03 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 38 VAWSKALVTVGVLTADEQLQLEEALNNlleeVRLDPAQILQSDAE---DIHSwVEGKLIDKVGQLGKK-LHTGRSRNDQV 113
Cdd:cd01595 19 AALAEAQAELGLIPKEAAEEIRAAADV----FEIDAERIAEIEKEtghDVIA-FVYALAEKCGEDAGEyVHFGATSQDIN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 114 ATDLKLWCKDTVAELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDTLKRLDVS 193
Cdd:cd01595 94 DTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 194 PLG--CGALAgTAYEID---REQLAGWLGFASATRNSLdsVSDRDHVLELLSnaSIGMVH--LSRFAEDLIFFNSGEAGF 266
Cdd:cd01595 174 GISgaVGTHA-SLGPKGpevEERVAEKLGLKVPPITTQ--IEPRDRIAELLS--ALALIAgtLEKIATDIRLLQRTEIGE 248
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 493180901 267 VEL---SDRVtsGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTL 310
Cdd:cd01595 249 VEEpfeKGQV--GSSTMPHKRNPIDSENIEGLARLVRALAAPALENL 293
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
106-408 |
2.18e-21 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 96.21 E-value: 2.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 106 GRSRNDQVATDLKLWCKDTVAELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQD 185
Cdd:PRK13353 138 AQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQ 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 186 TLKRLDVSPLGCGALaGTAYEIDRE---QLAGWLGFAS-----ATRNSLDSVSDRDHVLELLSNASIGMVHLSRFAEDLI 257
Cdd:PRK13353 218 AREHLYEVNLGGTAV-GTGLNADPEyieRVVKHLAAITglplvGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLR 296
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 258 FFNSG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYN-------KDMQEDKEGL 328
Cdd:PRK13353 297 LLSSGpRTGLGEINlPAVQPGSSIMPGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNvmepviaFNLLESISIL 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 329 FDALDTWLD-CLHmgalvldGIQVKRPRCQEAAQQGYANSTELADYLvakgvpfreAHHIVGEAVVEAIRQGKPLEDLPL 407
Cdd:PRK13353 377 TNACRAFTDnCVK-------GIEANEERCKEYVEKSVGIATALNPHI---------GYEAAARIAKEAIATGRSVRELAL 440
|
.
gi 493180901 408 A 408
Cdd:PRK13353 441 E 441
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
106-405 |
2.03e-18 |
|
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: 87.19 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 106 GRSRNDQVATDLKLWCKDTVAELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQD 185
Cdd:cd01357 133 SQSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 186 TLKRLDVspLGCGALA-GTAYEIDRE----------QLAGwLGFASATrNSLDSVSDRDHVLELLSNASIGMVHLSRFAE 254
Cdd:cd01357 213 ARERLRE--VNLGGTAiGTGINAPPGyielvveklsEITG-LPLKRAE-NLIDATQNTDAFVEVSGALKRLAVKLSKIAN 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 255 DLIFFNSG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKG--------LPL-AYNkdmqe 323
Cdd:cd01357 289 DLRLLSSGpRAGLGEINlPAVQPGSSIMPGKVNPVIPEVVNQVAFQVIGNDLTITMAAEAgqlelnvfEPViAYN----- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 324 dkegLFDALDtwldclHMGALV-------LDGIQVKRPRCQEAAQQGYANSTELADYLvakgvpfreAHHIVGEAVVEAI 396
Cdd:cd01357 364 ----LLESID------ILTNAVrtlrercIDGITANEERCREYVENSIGIVTALNPYI---------GYEAAAEIAKEAL 424
|
....*....
gi 493180901 397 RQGKPLEDL 405
Cdd:cd01357 425 ETGRSVREL 433
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
38-432 |
3.11e-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: 86.68 E-value: 3.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 38 VAWSKALVTVGVLTADEQlqleEALNNLLEEVRLDPAQILQSDAE---DIHSwVEGKLIDKVGQLGKK-LHTGRSRNDQV 113
Cdd:COG0015 29 IALAEAQAELGLIPAEAA----AAIRAAADDFEIDAERIKEIEKEtrhDVKA-FVYALKEKVGAEAGEyIHFGATSQDIN 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 114 ATDLKLWCKDTVAELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDTLKRLDVS 193
Cdd:COG0015 104 DTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVG 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 194 PLGcGAlAGT-------AYEIDREqLAGWLGFASATrnSLDSVSDRDHVLELLSN-ASIGMVhLSRFAEDLIFFNSGEAG 265
Cdd:COG0015 184 KIG-GA-VGTyaahgeaWPEVEER-VAEKLGLKPNP--VTTQIEPRDRHAELFSAlALIAGS-LEKIARDIRLLQRTEVG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 266 FVE---LSDRVtsGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLkglplaynkdMQEDKEGLFD------------ 330
Cdd:COG0015 258 EVEepfAKGQV--GSSAMPHKRNPIDSENIEGLARLARALAAALLEAL----------ASWHERDLSDssvernilpdaf 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 331 -----ALDTWLDclhmgalVLDGIQVKRPRCQE--AAQQGYANSTELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPLE 403
Cdd:COG0015 326 llldgALERLLK-------LLEGLVVNPERMRAnlDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAWEEGNDLR 398
|
410 420
....*....|....*....|....*....
gi 493180901 404 DLPLADLQkFSAVIGEDvypilALQSCLD 432
Cdd:COG0015 399 ELLAADPE-IPAELSKE-----ELEALFD 421
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
127-384 |
2.37e-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: 77.85 E-value: 2.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 127 ELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDTLKRLDVSPLGcgalaGTA-- 204
Cdd:cd01596 154 RLLPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLG-----GTAvg 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 205 --------Y-EIDREQLA---GwLGFASATrNSLDSVSDRDHVLELLSNASIGMVHLSRFAEDLIFFNSG-EAGFVELS- 270
Cdd:cd01596 229 tglnappgYaEKVAAELAeltG-LPFVTAP-NLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGpRAGLGEINl 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 271 DRVTSGSSLMPQKKNP---DALELIrgkCGRVQGALTGMMMTLKG--------LPL-AYNkdMQEDKEGLFDALDTWLD- 337
Cdd:cd01596 307 PANQPGSSIMPGKVNPvipEAVNMV---AAQVIGNDTAITMAGSAgqlelnvfKPViAYN--LLQSIRLLANACRSFRDk 381
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 493180901 338 ClhmgalvLDGIQVKRPRCQEAAQQ------------GYANSTELADYLVAKGVPFREA 384
Cdd:cd01596 382 C-------VEGIEANEERCKEYVENslmlvtalnphiGYEKAAEIAKEALKEGRTLREA 433
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
59-294 |
8.62e-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: 69.50 E-value: 8.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 59 EEALNNLLEEVRLDPAQILQSDAE---DIHSWVEGkLIDKVGQLGKKLHTGRSRNDQVATDLKLWCKDTVAELLAANRQL 135
Cdd:cd01360 39 AEAAEEIRKKAKFDVERVKEIEAEtkhDVIAFVTA-IAEYCGEAGRYIHFGLTSSDVVDTALALQLREALDIILKDLKEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 136 QSALVETAQNNQDAVMPGYTHLQRAQPVTFAH-WCLAYVEMlARDESRLQDTLKRLDVSPLGcGALaGTAYEID---REQ 211
Cdd:cd01360 118 LEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLkFALWYAEF-KRHLERLKEARERILVGKIS-GAV-GTYANLGpevEER 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 212 LAGWLGFASATRNSldSVSDRDHVLELLSNASIGMVHLSRFAEDLIFFNSGEAGfvELSDRVTS---GSSLMPQKKNPDA 288
Cdd:cd01360 195 VAEKLGLKPEPIST--QVIQRDRHAEYLSTLALIASTLEKIATEIRHLQRTEVL--EVEEPFSKgqkGSSAMPHKRNPIL 270
|
....*.
gi 493180901 289 LELIRG 294
Cdd:cd01360 271 SENICG 276
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
100-411 |
1.21e-12 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 69.27 E-value: 1.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 100 GKKLHTGRSRNDQVATDLKLWCKDTVAELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARD 179
Cdd:PRK09053 99 ARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 180 ESRLQDTLKRLDVspLGCGALAGTAYEIDREQLAGWLGFASATRNSLDSVS---DRDHVLELlsNASIGMV--HLSRFAE 254
Cdd:PRK09053 179 RQRLAALRPRALV--LQFGGAAGTLASLGEQALPVAQALAAELQLALPALPwhtQRDRIAEF--ASALGLLagTLGKIAR 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 255 DLIFFNSGEAGFV-ELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMmmtLKGLPlaynkdmQEDKEGL----- 328
Cdd:PRK09053 255 DVSLLMQTEVGEVfEPAAAGKGGSSTMPHKRNPVGCAAVLTAATRAPGLVATL---FAAMP-------QEHERALggwha 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 329 -FDALDTwLDCLHMGAL-----VLDGIQVKRPRCQEAAQQ------GYANSTELADYLvakGVPfrEAHHIVGEAVVEAI 396
Cdd:PRK09053 325 eWDTLPE-LACLAAGALaqmaqIVEGLEVDAARMRANLDLthglilAEAVMLALADRI---GRL--DAHHLVEQASKRAV 398
|
330
....*....|....*
gi 493180901 397 RQGKPLEDLPLADLQ 411
Cdd:PRK09053 399 AEGRHLRDVLAEDPQ 413
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
108-405 |
2.55e-12 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 68.61 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 108 SRNDQVATDLKLWCKDTVAELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVT----FAhwclAYVEMLARDESRL 183
Cdd:PRK12273 142 STNDAYPTAIRIALLLSLRKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTlgqeFG----AYAVALAEDRKRL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 184 QDTLKRLDVSPLGcgalaGTA----------Y-EIDREQLA---GwLGFASATrNSLDSVSDRDHVLELLSNASIGMVHL 249
Cdd:PRK12273 218 YRAAELLREVNLG-----ATAigtglnappgYiELVVEKLAeitG-LPLVPAE-DLIEATQDTGAFVEVSGALKRLAVKL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 250 SRFAEDLIFFNSG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGA-LTGMMMTLKG-------LPL-AYN 318
Cdd:PRK12273 291 SKICNDLRLLSSGpRAGLNEINlPAVQAGSSIMPGKVNPVIPEVVNQVCFQVIGNdTTVTMAAEAGqlelnvmEPViAYN 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 319 kdmqedkegLFDALDTwldcLHMGALVL-----DGIQVKRPRCQEAAQQGYANSTELADYLvakgvpfreAHHIVGEAVV 393
Cdd:PRK12273 371 ---------LFESISI----LTNACRTLrekciDGITANEERCREYVENSIGIVTALNPYI---------GYENAAEIAK 428
|
330
....*....|..
gi 493180901 394 EAIRQGKPLEDL 405
Cdd:PRK12273 429 EALETGKSVREL 440
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
106-384 |
6.82e-12 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 67.02 E-value: 6.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 106 GRSRNDQVATDLKLWCKDTVAE-LLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQ 184
Cdd:PLN00134 129 SQSSNDTFPTAMHIAAATEIHSrLIPALKELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 185 DTLKRLDVSPLGCGAL-------AGTAYEIDRE--QLAGwLGFASAtRNSLDSVSDRDHVLElLSNASIGM-VHLSRFAE 254
Cdd:PLN00134 209 CTLPRLYELAQGGTAVgtglntkKGFDEKIAAAvaEETG-LPFVTA-PNKFEALAAHDAFVE-LSGALNTVaVSLMKIAN 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 255 DLIFFNSG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGalTGMMMTLKGL----------PL-AYNkdM 321
Cdd:PLN00134 286 DIRLLGSGpRCGLGELNlPENEPGSSIMPGKVNPTQCEALTMVCAQVMG--NHVAITVGGSaghfelnvfkPLiAYN--L 361
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 493180901 322 QEDKEGLFDALDTW-LDClhmgalvLDGIQVKRPRCQEAAQQ------------GYANSTELADYLVAKGVPFREA 384
Cdd:PLN00134 362 LHSIRLLGDASASFrKNC-------VRGIEANRERISKLLHEslmlvtalnpkiGYDKAAAVAKKAHKEGTTLKEA 430
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
107-292 |
5.02e-11 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 64.64 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 107 RSRNDQVATDLKLWCKDTVAELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDT 186
Cdd:PRK14515 145 QSTNDAFPTAIHIATLNALEGLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQS 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 187 LKRLDVSPLGCGALaGTAYEIDREQLAGWLGFASA--------TRNSLDSVSDRDHVLELLSNASIGMVHLSRFAEDLIF 258
Cdd:PRK14515 225 RQHLYEVNMGATAV-GTGLNADPEYIEAVVKHLAAiselplvgAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRL 303
|
170 180 190
....*....|....*....|....*....|....*..
gi 493180901 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 |
1.45e-10 |
|
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial fumarase, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.
Pssm-ID: 176465 [Multi-domain] Cd Length: 455 Bit Score: 62.90 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 106 GRSRND------QVATDLKLwckdtVAELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARD 179
Cdd:cd01362 133 SQSSNDtfptamHIAAALAL-----QERLLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHA 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 180 ESRLQDTLKRLDVSPLGcGALAGT------------AYEIdrEQLAGwLGFASATrNSLDSVSDRDHVLELLSNASIGMV 247
Cdd:cd01362 208 IARIEAALPRLYELALG-GTAVGTglnahpgfaekvAAEL--AELTG-LPFVTAP-NKFEALAAHDALVEASGALKTLAV 282
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 493180901 248 HLSRFAEDLIFFNSG-EAGFVELS-DRVTSGSSLMPQKKNP 286
Cdd:cd01362 283 SLMKIANDIRWLGSGpRCGLGELSlPENEPGSSIMPGKVNP 323
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
106-384 |
2.06e-10 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 62.42 E-value: 2.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 106 GRSRND------QVATDLKLwckdtVAELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARD 179
Cdd:PRK00485 137 SQSSNDtfptamHIAAVLAI-----VERLLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHG 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 180 ESRLQDTLKRLDVSPLGcGALAGT------------AYEIdrEQLAGwLGFASAtRNSLDSVSDRDhvlellsnasiGMV 247
Cdd:PRK00485 212 IERIEAALPHLYELALG-GTAVGTglnahpgfaervAEEL--AELTG-LPFVTA-PNKFEALAAHD-----------ALV 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 248 HLS-----------RFAEDLIFFNSG-EAGFVELS--DRVtSGSSLMPQKKNP---DALELIrgkCGRVQG--------A 302
Cdd:PRK00485 276 EASgalktlavslmKIANDIRWLASGpRCGLGEISlpENE-PGSSIMPGKVNPtqcEALTMV---CAQVMGndaavtfaG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 303 LTG-----MMMTLkglpLAYNkdMQEDKEGLFDAldtwldCLHMGALVLDGIQVKRPRCQEAAQQ------------GYA 365
Cdd:PRK00485 352 SQGnfelnVFKPV----IAYN--FLQSIRLLADA------MRSFADHCVVGIEPNRERIKELLERslmlvtalnphiGYD 419
|
330
....*....|....*....
gi 493180901 366 NSTELADYLVAKGVPFREA 384
Cdd:PRK00485 420 KAAKIAKKAHKEGLTLKEA 438
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
106-290 |
2.10e-07 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 53.00 E-value: 2.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 106 GRSRNDQVATDLKLWCKDTV-AELLAANRQLQSALVETAQNNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQ 184
Cdd:PRK12425 135 SQSSNDCFPTAMHIAAAQAVhEQLLPAIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIR 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 185 DTLKRldVSPLGCGALA---------GTAYEIDRE--QLAGwLGFASATrNSLDSVSDRDHVLELLSNASIGMVHLSRFA 253
Cdd:PRK12425 215 AALPA--VCELAQGGTAvgtglnaphGFAEAIAAElaALSG-LPFVTAP-NKFAALAGHEPLVSLSGALKTLAVALMKIA 290
|
170 180 190
....*....|....*....|....*....|....*....
gi 493180901 254 EDLIFFNSG-EAGFVELSDRVTS-GSSLMPQKKNPDALE 290
Cdd:PRK12425 291 NDLRLLGSGpRAGLAEVRLPANEpGSSIMPGKVNPTQCE 329
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
100-292 |
2.61e-07 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 52.36 E-value: 2.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 100 GKKLHTGRSRNDQVATDLKLWCKdTVAELLAAnrqLQSALVET-----AQNNQDAVMpGYTHLQRAQPVTFAHWCLAYVE 174
Cdd:PRK05975 99 AAHVHFGATSQDVIDTSLMLRLK-AASEILAA---RLGALIARldaleATFGQNALM-GHTRMQAAIPITVADRLASWRA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 175 MLARDESRLQDTlkRLDVSPLGCGALAGTAYEID------REQLAGWLGFASATR--NSLDSVSDRDHVLELLSNAsigm 246
Cdd:PRK05975 174 PLLRHRDRLEAL--RADVFPLQFGGAAGTLEKLGgkaaavRARLAKRLGLEDAPQwhSQRDFIADFAHLLSLVTGS---- 247
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 493180901 247 vhLSRFAEDLiffnsgeAGFVELSDRVT----SGSSLMPQKKNPDALELI 292
Cdd:PRK05975 248 --LGKFGQDI-------ALMAQAGDEISlsggGGSSAMPHKQNPVAAETL 288
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
249-435 |
3.71e-07 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 50.80 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 249 LSRFAEDLIFFNSGEAGFVELSDRVTS-GSSLMPQKKNPDALELIrgkcgrvqgalTGMMMTLKGLPLAYNKDMQEDKEG 327
Cdd:PRK08937 30 LEKFANEIRLLQRSEIREVEEPFAKGQkGSSAMPHKRNPIGSERI-----------TGLARVLRSYLVTALENVPLWHER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 493180901 328 -----------LFDA-------LDTWLDClhmgalvLDGIQVKRPRCQE--AAQQGYANSTELADYLVAKGVPFREAHHI 387
Cdd:PRK08937 99 dlshssaeriaLPDAflaldyiLNRFVNI-------LENLVVFPENIERnlDKTLGFIATERVLLELVEKGMGREEAHEL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 493180901 388 VGEAVVEAIRQGKPLEDLPLADlQKFSAVIGEDvypilALQSCLDKRA 435
Cdd:PRK08937 172 IREKAMEAWKNQKDLRELLEAD-ERFTKQLTKE-----ELDELFDPEA 213
|
|
| |
