|
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: 1008.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 1 MALWGGRFSQQADQRFKQFNDSLRFDYRLAQQDIIGSVAWSKSLVTVGVLTESEQQSLEQALNALLKEVQDNPEIILQSD 80
Cdd:PRK04833 1 MALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQQQLEEALNELLEEVRANPQQILASD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 81 AEDIHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVALLLEAVTELQKALVITAENNQDAVMPGYTHLQRA 160
Cdd:PRK04833 81 AEDIHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 161 QPVTFAHWCLAYSEMLARDESRLKDTLKRLDVSPLGCGALAGTAYDIDREQLASWLGFASATRNSLDTVSDRDHVLELLS 240
Cdd:PRK04833 161 QPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 241 DASIGMVHLSRFAEDLIFFNSGEAGFVELSDKVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKD 320
Cdd:PRK04833 241 DASISMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPLAYNKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 321 MQEDKEGLFDALDTWLDCMHMAALVLDGIQIRRPRCEDAAKQGYANATELADYLVAKGVPFREAHHIVGEAVVTAIAQGK 400
Cdd:PRK04833 321 MQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 757599009 401 ALEEMALSDLQKFSDTIQLDVYEILSLQSCLDKRLAKGGVSQKQVASAIVEAKTR 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: 814.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 1 MALWGGRFSQQADQRFKQFNDSLRFDYRLAQQDIIGSVAWSKSLVTVGVLTESEQQSLEQALNALLKEVQDNPEIILQSD 80
Cdd:PRK12308 1 MALWGGRFSQAADTRFKQFNDSLRFDYRLAEQDIVGSIAWSKALLSVGVLSEEEQQKLELALNELKLEVMEDPEQILLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 81 AEDIHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVALLLEAVTELQKALVITAENNQDAVMPGYTHLQRA 160
Cdd:PRK12308 81 AEDIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 161 QPVTFAHWCLAYSEMLARDESRLKDTLKRLDVSPLGCGALAGTAYDIDREQLASWLGFASATRNSLDTVSDRDHVLELLS 240
Cdd:PRK12308 161 QPVTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGSGALAGTAYPIDREALAHNLGFRRATRNSLDSVSDRDHVMELMS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 241 DASIGMVHLSRFAEDLIFFNSGEAGFVELSDKVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKD 320
Cdd:PRK12308 241 VASISMLHLSRLAEDLIFYNSGESGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 321 MQEDKEGLFDALDTWLDCMHMAALVLDGIQIRRPRCEDAAKQGYANATELADYLVAKGVPFREAHHIVGEAVVTAIAQGK 400
Cdd:PRK12308 321 MQEDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANATELADYLVAKGIPFREAHHIVGVAVVGAIAKGC 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 757599009 401 ALEEMALSDLQKFSDTIQLDVYEILSLQSCLDKRLAKGGVSQKQVASAIVEAKTRL 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: 743.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 3 LWGGRFSQQADQRFKQFNDSLRFDYRLAQQDIIGSVAWSKSLVTVGVLTESEQQSLEQALNALLKEVQDNPeIILQSDAE 82
Cdd:TIGR00838 1 LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGP-FILDPDDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 83 DIHSWVEGKLIDKVG-DLGKKLHTGRSRNDQVATDLKLWCKDQVALLLEAVTELQKALVITAENNQDAVMPGYTHLQRAQ 161
Cdd:TIGR00838 80 DIHMAIERELIDRVGeDLGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 162 PVTFAHWCLAYSEMLARDESRLKDTLKRLDVSPLGCGALAGTAYDIDREQLASWLGFASATRNSLDTVSDRDHVLELLSD 241
Cdd:TIGR00838 160 PITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 242 ASIGMVHLSRFAEDLIFFNSGEAGFVELSDKVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDM 321
Cdd:TIGR00838 240 AALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 322 QEDKEGLFDALDTWLDCMHMAALVLDGIQIRRPRCEDAAKQGYANATELADYLVAKGVPFREAHHIVGEAVVTAIAQGKA 401
Cdd:TIGR00838 320 QEDKEPLFDALKTVELSLEMATGMLDTITVNKERMEEAASAGFSNATELADYLVRKGVPFREAHHIVGELVATAIERGKG 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 757599009 402 LEEMALSDLQKFSDTIQLDVYEILSLQSCLDKRLAKGGVSQKQVASAIVEAKTRLG 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: 723.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 1 MALWGGRFSQQADQRFKQFNDSLRFDYRLAQQDIIGSVAWSKSLVTVGVLTESEQQSLEQALNALLKEVQDNpEIILQSD 80
Cdd:COG0165 3 MKLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAG-AFEFDPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 81 AEDIHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVALLLEAVTELQKALVITAENNQDAVMPGYTHLQRA 160
Cdd:COG0165 82 LEDIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 161 QPVTFAHWCLAYSEMLARDESRLKDTLKRLDVSPLGCGALAGTAYDIDREQLASWLGFASATRNSLDTVSDRDHVLELLS 240
Cdd:COG0165 162 QPVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFLS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 241 DASIGMVHLSRFAEDLIFFNSGEAGFVELSDKVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKD 320
Cdd:COG0165 242 AASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNKD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 321 MQEDKEGLFDALDTWLDCMHMAALVLDGIQIRRPRCEDAAKQGYANATELADYLVAKGVPFREAHHIVGEAVVTAIAQGK 400
Cdd:COG0165 322 LQEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGFSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKGK 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 757599009 401 ALEEMALSDLQKFSDTIQLDVYEILSLQSCLDKRLAKGGVSQKQVASAIVEAKTRLG 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: 688.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 1 MALWGGRFSQQADQRFKQFNDSLRFDYRLAQQDIIGSVAWSKSLVTVGVLTESEQQSLEQALNALLKEVQDNpEIILQSD 80
Cdd:PRK00855 4 NKLWGGRFSEGPDELVERFTASISFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILEEIEAG-KFEFSPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 81 AEDIHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVALLLEAVTELQKALVITAENNQDAVMPGYTHLQRA 160
Cdd:PRK00855 83 LEDIHMAIEARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 161 QPVTFAHWCLAYSEMLARDESRLKDTLKRLDVSPLGCGALAGTAYDIDREQLASWLGFASATRNSLDTVSDRDHVLELLS 240
Cdd:PRK00855 163 QPVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAALAGTTFPIDRERTAELLGFDGVTENSLDAVSDRDFALEFLS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 241 DASIGMVHLSRFAEDLIFFNSGEAGFVELSDKVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKD 320
Cdd:PRK00855 243 AASLLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLAYNRD 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 321 MQEDKEGLFDALDTWLDCMHMAALVLDGIQIRRPRCEDAAKQGYANATELADYLVAKGVPFREAHHIVGEAVVTAIAQGK 400
Cdd:PRK00855 323 LQEDKEPLFDAVDTLKLSLEAMAGMLETLTVNKERMREAAGKGFSTATDLADYLVRKGVPFREAHEIVGKAVREAEERGV 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 757599009 401 ALEEMALSDLQKFSDTIQLDVYEILSLQSCLDKRLAKGGVSQKQVASAIVEAKTRLG 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: 642.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 22 SLRFDYRLAQQDIIGSVAWSKSLVTVGVLTESEQQSLEQALNALLKEVqDNPEIILQSDAEDIHSWVEGKLIDKVGDLGK 101
Cdd:cd01359 1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEI-EAGAFELDPEDEDIHMAIERRLIERIGDVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 102 KLHTGRSRNDQVATDLKLWCKDQVALLLEAVTELQKALVITAENNQDAVMPGYTHLQRAQPVTFAHWCLAYSEMLARDES 181
Cdd:cd01359 80 KLHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 182 RLKDTLKRLDVSPLGCGALAGTAYDIDREQLASWLGFASATRNSLDTVSDRDHVLELLSDASIGMVHLSRFAEDLIFFNS 261
Cdd:cd01359 160 RLADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 262 GEAGFVELSDKVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQEDKEGLFDALDTWLDCMHM 341
Cdd:cd01359 240 QEFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 342 AALVLDGIQIRRPRCEDAAKQGYANATELADYLVA-KGVPFREAHHIVGEAVVTAIAQGKALEEMALSDLQKFSDTIQLD 420
Cdd:cd01359 320 LTGVISTLTVNPERMREAAEAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEED 399
|
410 420 430
....*....|....*....|....*....|....*.
gi 757599009 421 VYEILSLQSCLDKRLAKGGVSQKQVASAIVEAKTRL 456
Cdd:cd01359 400 VREALDPENSVERRTSYGGTAPAEVREQIARARALL 435
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
3-458 |
0e+00 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 545.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 3 LWGGRFSQQADQRFKQFNDSLRFDYRLAQQDIIGSVAWSKSLVTVGVLTESEQQSLEQALNALLKEVQDNpEIILQSDAE 82
Cdd:PLN02646 18 LWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAG-KFEWRPDRE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 83 DIHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVALLLEAVTELQKALVITAENNQDAVMPGYTHLQRAQP 162
Cdd:PLN02646 97 DVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 163 VTFAHWCLAYSEMLARDESRLKDTLKRLDVSPLGCGALAGTAYDIDREQLASWLGFASATRNSLDTVSDRDHVLELLSDA 242
Cdd:PLN02646 177 VLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRDFVLEFLFAN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 243 SIGMVHLSRFAEDLIFFNSGEAGFVELSDKVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQ 322
Cdd:PLN02646 257 SITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTAYNRDLQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 323 EDKEGLFDALDTWLDCMHMAALVLDGIQIRRPRCEDAAKQGYANATELADYLVAKGVPFREAHHIVGEAVVTAIAQGKAL 402
Cdd:PLN02646 337 EDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLDATTLADYLVRKGVPFRETHHIVGAAVALAESKGCEL 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 757599009 403 EEMALSDLQKFSDTIQLDVYEILSLQSCLDKRLAKGGVSQKQVASAIVEAKTRLGL 458
Cdd:PLN02646 417 SDLTLEDLKSINPVFEEDVYEVLGVENSVEKFDSYGSTGSRSVLEQLEKWRTKLEI 472
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
31-351 |
3.64e-124 |
|
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: 363.75 E-value: 3.64e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 31 QQDIIGSVAWSKSLVTVGVLTESEQQSLEQALNALLKEVQDNPEIILQSDaEDIHSWVEGKLIDKVGDL-GKKLHTGRSR 109
Cdd:cd01334 2 RADLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVEQEGSG-THDVMAVEEVLAERAGELnGGYVHTGRSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 110 NDQVATDLKLWCKDQVALLLEAVTELQKALVITAENNQDAVMPGYTHLQRAQPVTFAHWCLAYSEMLARDESRLKDTLKR 189
Cdd:cd01334 81 NDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 190 LDVSPLGCGALAGTAY--DIDREQLASWLGFASATRNSLDTVSDRDHVLELLSDASIGMVHLSRFAEDLIFFNSGEAGFV 267
Cdd:cd01334 161 LNVLPLGGGAVGTGANapPIDRERVAELLGFFGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 268 ELSDKVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQEDKEGLFDALDTWLDCMHMAALVLD 347
Cdd:cd01334 241 ELPDAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVLE 320
|
....
gi 757599009 348 GIQI 351
Cdd:cd01334 321 GLEV 324
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
6-301 |
1.30e-118 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 349.36 E-value: 1.30e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 6 GRFSQQADQRFKQFNDSLRFDYRLAQQDIIGSVAWSKSLVTVGVLTESEQQSLEQALNALLKEVQDNPEIILQSDAEDIH 85
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDDQFPLKVWQEGSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 86 SWVEGKLIDKVGDL-------GKKLHTGRSRNDQVATDLKLWCKDQV-ALLLEAVTELQKALVITAENNQDAVMPGYTHL 157
Cdd:pfam00206 81 TAVNMNLNEVIGELlgqlvhpNDHVHTGQSSNDQVPTALRLALKDALsEVLLPALRQLIDALKEKAKEFADIVKPGRTHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 158 QRAQPVTFAHWCLAYSEMLARDESRLKDTLKRLDVSPLGCGALAGTAYDIDRE---QLASWLGF----ASATRNSLDTVS 230
Cdd:pfam00206 161 QDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEfaeLVAKELGFftglPVKAPNSFEATS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757599009 231 DRDHVLELLSDASIGMVHLSRFAEDLIFFNSGEAGFVELSD-KVTSGSSLMPQKKNPDALELIRGKCGRVQG 301
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLaEGEPGSSIMPGKVNPDQLELLTGKAGRVMG 312
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
57-401 |
1.24e-64 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 223.57 E-value: 1.24e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 57 SLEQA---LNALLKEVQDNPEIILQSDA-EDIHSWVEGKLIDKVG-DLGKKLHTGRSRNDQVATDLKLWCKDQVALLLEA 131
Cdd:PRK02186 459 APERArplLDAHRRLRDAGFAPLLARPApRGLYMLYEAYLIERLGeDVGGVLQTARSRNDINATTTKLHLREATSRAFDA 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 132 VTELQKALVITAENNQDAVMPGYTHLQRAQPVTFAHWCLAYSEMLARDESRLKDTLKRLDVSPLGCGALAGTAYDIDREQ 211
Cdd:PRK02186 539 LWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHALFALFEHIDVCPLGAGAGGGTTFPIDPEF 618
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 212 LASWLGFASATRNSLDTVSDRDHVLELLSD-ASIGMVhLSRFAEDLIFFNSGEAGFVELSDKVTSGSSLMPQKKNPDALE 290
Cdd:PRK02186 619 VARLLGFEQPAPNSLDAVASRDGVLHFLSAmAAISTV-LSRLAQDLQLWTTREFALVSLPDALTGGSSMLPQKKNPFLLE 697
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 291 LIRGKCGRVQGALTGMMMTLKGLPlaYNKDMQEDKEG---LFDALDTWLDCMHMAALVLDGIQIRRPRCEDAAKQGYANA 367
Cdd:PRK02186 698 FVKGRAGVVAGALASASAALGKTP--FSNSFEAGSPMngpIAQACAAIEDAAAVLVLLIDGLEADQARMRAHLEDGGVSA 775
|
330 340 350
....*....|....*....|....*....|....*
gi 757599009 368 TELADYLVA-KGVPFREAHHIVGEAVVTAIAQGKA 401
Cdd:PRK02186 776 TAVAESLVVrRSISFRSAHTQVGQAIRQSLDQGRS 810
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
87-343 |
7.51e-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: 7.51e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 87 WVEGKLIDKVGDLGKKLH------TGRSRNDQVATDLKLWCKDQVALLLEAVTELQKALVITAENNQDAVMPGYTHLQRA 160
Cdd:cd01594 15 LVEEVLAGRAGELAGGLHgsalvhKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 161 QPVTFAHWCLAYSEMLARDESRLKDTlkrldvsplgcgalagtaydidreqlaswlgfasatrnsldtvsdrdHVLELLS 240
Cdd:cd01594 95 QPVTLGYELRAWAQVLGRDLERLEEA-----------------------------------------------AVAEALD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 241 DASIGMVHLSRFAEDLIFFNSGEAGFVELSD-KVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNK 319
Cdd:cd01594 128 ALALAAAHLSKIAEDLRLLLSGEFGELGEPFlPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDNE 207
|
250 260
....*....|....*....|....
gi 757599009 320 DMQEDKEGLFDALDTWLDCMHMAA 343
Cdd:cd01594 208 DSPSMREILADSLLLLIDALRLLL 231
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
49-453 |
1.34e-53 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 187.11 E-value: 1.34e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 49 VLTESEQQSLEQA---LNALlKEVQDNPE--IILQSDAEDIHSWVEGKLIDKVG-DLGKKLHTGRSRNDQVATDLKLWCK 122
Cdd:PRK06705 51 MLTEENLMKKEEAkfiLHAL-KKVEEIPEeqLLYTEQHEDLFFLVEHLISQEAKsDFVSNMHIGRSRNDMGVTMYRMSLR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 123 DQVALLLEAVTELQKALVITAENNQDAVMPGYTHLQRAQPVTFAHWCLAYSEMLARDESRLKDTLKRLDVSPLGCGALAG 202
Cdd:PRK06705 130 RYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKTYKLLNQSPMGAAALST 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 203 TAYDIDREQLASWLGFASATRNSLDTVSDRDHVLELLSDASIGMVHLSRFAEDLIFFNSGEAGFVELSDKVTSGSSLMPQ 282
Cdd:PRK06705 210 TSFPIKRERVADLLGFTNVIENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLATKEYDGITVARPYVQISSIMPQ 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 283 KKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQEDKEG-LFDALDTWLDCMHMAALVLDGIQIRRPRCEDAAK 361
Cdd:PRK06705 290 KRNPVSIEHARAITSSALGEAFTVFQMIHNTPFGDIVDTEDDLQPyLYKGIEKAIRVFCIMNAVIRTMKVEEDTLKRRSY 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 362 QGYANATELADYLVAK-GVPFREAHHIVGEAVVTAIAQGKALEEMALSDL-----QKFS-DTIQLDVYEILSLQSCLDKR 434
Cdd:PRK06705 370 KHAITITDFADVLTKNyGIPFRHAHHAASVIANMSLEQKKELHELCFKDVniylqEKFKiQLLEKEWEEIISPEAFIQKR 449
|
410
....*....|....*....
gi 757599009 435 LAKGGVSQKQVASAIVEAK 453
Cdd:PRK06705 450 NVYGGPSKKEMERMINNRK 468
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
1-415 |
2.44e-41 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 152.36 E-value: 2.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 1 MALWGGrfSQQADQRFKQFNDSLRFDYR----LAQQDIIGSVAWSKSLVTVGVLTESEQQSLeqaLNALLKEVQDNPEII 76
Cdd:PRK06389 1 MKIWSG--GAGEELENDFYDNIVKDDIDadknLIKYEIINLLAYHVALAQRRLITEKAPKCV---INALIDIYKNGIEID 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 77 LqsDAEDIHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVallLEAVTELQKALVITAENNQDAVMPGYTH 156
Cdd:PRK06389 76 L--DLEDVHTAIENFVIRRCGDMFKNFRLFLSRNEQVHADLNLFIIDKI---IEIEKILYEIIKVIPGFNLKGRLPGYTH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 157 LQRAQPVTFAHWCLAYSEMLARDESRLKDTLKRLDVSPLGCGALAGTAYDIDREQLASWLGFASATRNSLDTVSDRDHVL 236
Cdd:PRK06389 151 FRQAMPMTVNTYINYIKSILYHHINNLDSFLMDLREMPYGYGSGYGSPSSVKFNQMSELLGMEKNIKNPVYSSSLYIKTI 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 237 ELLSDASIG-MVHLSRFAEDLIffNSGEAGFVELSDKVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPL 315
Cdd:PRK06389 231 ENISYLISSlAVDLSRICQDII--IYYENGIITIPDEFTTGSSLMPNKRNPDYLELFQGIAAESISVLSFIAQSELNKTT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 316 AYNKDMQEDKEGLFDALDTWLDCMHMAALVLDGIQIRRPRCEDAAKQGYANATELADYlvAKGVPFREAHHIVGEavvtA 395
Cdd:PRK06389 309 GYHRDFQIVKDSTISFINNFERILLGLPDLLYNIKFEITNEKNIKNSVYATYNAWLAF--KNGMDWKSAYAYIGN----K 382
|
410 420
....*....|....*....|
gi 757599009 396 IAQGKALEEMALSDLQKFSD 415
Cdd:PRK06389 383 IREGEVLDEYQPEDLTDYID 402
|
|
| ASL_C2 |
pfam14698 |
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of ... |
364-431 |
1.38e-29 |
|
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: 109.82 E-value: 1.38e-29
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 757599009 364 YANATELADYLVAKGVPFREAHHIVGEAVVTAIAQGKALEEMALSDLQKFSDTIQLDVYEILSLQSCL 431
Cdd:pfam14698 1 FSTATDLADYLVRKGVPFREAHEIVGRLVRLAEEKGKDLEDLTLEELQAISPLFEEDVYEALDPEASV 68
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
97-409 |
2.04e-23 |
|
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: 101.94 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 97 GDLGKKLHTGRSRNDQVATDLKLWCKDQVALLLEAVTELQKALVITAENNQDAVMPGYTHLQRAQPVTFAHWCLAYSEML 176
Cdd:cd01597 87 DAAGEYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSEL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 177 ARDESRLKDTLKRLDVSPLGcGAlAGTaydidreqLASWLGFASATRNSLD-----TV------SDRDHVLELLSdaSIG 245
Cdd:cd01597 167 LRHRERLDELRPRVLVVQFG-GA-AGT--------LASLGDQGLAVQEALAaelglGVpaipwhTARDRIAELAS--FLA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 246 MVH--LSRFAEDLIFFNSGEAGFV-ELSDKVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTlkglplaynkdMQ 322
Cdd:cd01597 235 LLTgtLGKIARDVYLLMQTEIGEVaEPFAKGRGGSSTMPHKRNPVGCELIVALARRVPGLAALLLDA-----------MV 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 323 EDKEGlfdALDTW---------LDCMHMAAL-----VLDGIQIRRPRC-EDAAKQGYANATELADYLVAKGVPFREAHHI 387
Cdd:cd01597 304 QEHER---DAGAWhaewialpeIFLLASGALeqaefLLSGLEVNEDRMrANLDLTGGLILSEAVMMALAPKLGRQEAHDL 380
|
330 340
....*....|....*....|..
gi 757599009 388 VGEAVVTAIAQGKALEEMALSD 409
Cdd:cd01597 381 VYEACMRAVEEGRPLREVLLED 402
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
106-408 |
9.23e-22 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 97.36 E-value: 9.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 106 GRSRNDQVATDLKLWCKDQVALLLEAVTELQKALVITAENNQDAVMPGYTHLQRAQPVTFAHWCLAYSEMLARDESRLKD 185
Cdd:PRK13353 138 AQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQ 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 186 TLKRLDVSPLGCGALaGTAYDIDRE-------QLA--SWLGFASATrNSLDTVSDRDHVLELLSDASIGMVHLSRFAEDL 256
Cdd:PRK13353 218 AREHLYEVNLGGTAV-GTGLNADPEyiervvkHLAaiTGLPLVGAE-DLVDATQNTDAFVEVSGALKVCAVNLSKIANDL 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 257 IFFNSG-EAGFVELS-DKVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKGLPLAYNKDMQEDKEGLFDALDT 334
Cdd:PRK13353 296 RLLSSGpRTGLGEINlPAVQPGSSIMPGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISI 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 757599009 335 WLD-CMHMAALVLDGIQIRRPRCEDAAKQGYANATELADYLvakgvpfreAHHIVGEAVVTAIAQGKALEEMALS 408
Cdd:PRK13353 376 LTNaCRAFTDNCVKGIEANEERCKEYVEKSVGIATALNPHI---------GYEAAARIAKEAIATGRSVRELALE 441
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
38-310 |
8.07e-20 |
|
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: 90.64 E-value: 8.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 38 VAWSKSLVTVGVLTESEQQsleqALNALLKEVQDNPEIILQSDAE---DIHSwVEGKLIDKVGDLGKK-LHTGRSRNDQV 113
Cdd:cd01595 19 AALAEAQAELGLIPKEAAE----EIRAAADVFEIDAERIAEIEKEtghDVIA-FVYALAEKCGEDAGEyVHFGATSQDIN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 114 ATDLKLWCKDQVALLLEAVTELQKALVITAENNQDAVMPGYTHLQRAQPVTFAHWCLAYSEMLARDESRLKDTLKRLDVS 193
Cdd:cd01595 94 DTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 194 PLG--CGALAgTAYDID---REQLASWLGFasaTRNSLDT-VSDRDHVLELLSdaSIGMVH--LSRFAEDLIFFNSGEAG 265
Cdd:cd01595 174 GISgaVGTHA-SLGPKGpevEERVAEKLGL---KVPPITTqIEPRDRIAELLS--ALALIAgtLEKIATDIRLLQRTEIG 247
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 757599009 266 FVEL-SDKVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTL 310
Cdd:cd01595 248 EVEEpFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENL 293
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
106-407 |
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 757599009 106 GRSRNDQVATDLKLWCKDQVALLLEAVTELQKALVITAENNQDAVMPGYTHLQRAQPVTFAHWCLAYSEMLARDESRLKD 185
Cdd:cd01357 133 SQSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 186 TLKRLDVspLGCGALA-GTAYDIDR-------EQLA--SWLGFASATrNSLDTVSDRDHVLELLSDASIGMVHLSRFAED 255
Cdd:cd01357 213 ARERLRE--VNLGGTAiGTGINAPPgyielvvEKLSeiTGLPLKRAE-NLIDATQNTDAFVEVSGALKRLAVKLSKIAND 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 256 LIFFNSG-EAGFVELS-DKVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLKG--------LPL-AYNkdmqed 324
Cdd:cd01357 290 LRLLSSGpRAGLGEINlPAVQPGSSIMPGKVNPVIPEVVNQVAFQVIGNDLTITMAAEAgqlelnvfEPViAYN------ 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 325 kegLFDALDTWLDCMHM-AALVLDGIQIRRPRCEDAAKQGYANATELADYLvakgvpfreAHHIVGEAVVTAIAQGKALE 403
Cdd:cd01357 364 ---LLESIDILTNAVRTlRERCIDGITANEERCREYVENSIGIVTALNPYI---------GYEAAAEIAKEALETGRSVR 431
|
....
gi 757599009 404 EMAL 407
Cdd:cd01357 432 ELVL 435
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
121-409 |
3.29e-17 |
|
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: 83.59 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 121 CKDQVALLLEAVTELQKALVITAENNQDAVMPGYTHLQRAQPVTF----AHWclaYSEMLaRDESRLKDTLKRLDVSPLG 196
Cdd:COG0015 111 LREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFgkklAVW---AAELL-RQLERLEEARERVLVGKIG 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 197 cGAlAGT--AYDID----REQLASWLGFasaTRNSLDT-VSDRDHVLELLSD-ASIGMVhLSRFAEDLIFFNSGEAGFV- 267
Cdd:COG0015 187 -GA-VGTyaAHGEAwpevEERVAEKLGL---KPNPVTTqIEPRDRHAELFSAlALIAGS-LEKIARDIRLLQRTEVGEVe 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 268 ELSDKVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMMMTLkglplaynkdMQEDKEGLFD----------------- 330
Cdd:COG0015 261 EPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEAL----------ASWHERDLSDssvernilpdafllldg 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 331 ALDTWLDcmhmaalVLDGIQIRRPRCE-DAAKQGYANATE---LAdyLVAKGVPFREAHHIVGEAVVTAIAQGKALEEMA 406
Cdd:COG0015 331 ALERLLK-------LLEGLVVNPERMRaNLDLTGGLVLSEavlMA--LVRRGLGREEAYELVKELARGAWEEGNDLRELL 401
|
...
gi 757599009 407 LSD 409
Cdd:COG0015 402 AAD 404
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
128-384 |
4.71e-16 |
|
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains aspartase (L-aspartate ammonia-lyase), fumarase class II enzymes, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.
Pssm-ID: 176468 [Multi-domain] Cd Length: 450 Bit Score: 80.16 E-value: 4.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 128 LLEAVTELQKALVITAENNQDAVMPGYTHLQRAQPVTFAHWCLAYSEMLARDESRLKDTLKRLDVSPLGcgalaGTA--- 204
Cdd:cd01596 155 LLPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLG-----GTAvgt 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 205 -------YdIDR--EQLA--SWLGFASATrNSLDTVSDRDHVLELLSDASIGMVHLSRFAEDLIFFNSG-EAGFVELS-D 271
Cdd:cd01596 230 glnappgY-AEKvaAELAelTGLPFVTAP-NLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGpRAGLGEINlP 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 272 KVTSGSSLMPQKKNP---DALELIrgkCGRVQGALTGMMMTLKG--------LPL-AYNkdmqedkegLFDALDTWLDCM 339
Cdd:cd01596 308 ANQPGSSIMPGKVNPvipEAVNMV---AAQVIGNDTAITMAGSAgqlelnvfKPViAYN---------LLQSIRLLANAC 375
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 757599009 340 HM-AALVLDGIQIRRPRCEDAAKQ------------GYANATELADYLVAKGVPFREA 384
Cdd:cd01596 376 RSfRDKCVEGIEANEERCKEYVENslmlvtalnphiGYEKAAEIAKEALKEGRTLREA 433
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
59-294 |
2.73e-15 |
|
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: 77.21 E-value: 2.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 59 EQALNALLKEVQDNPEIILQSDAE---DIHSWVEGkLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVALLLEAVTEL 135
Cdd:cd01360 39 AEAAEEIRKKAKFDVERVKEIEAEtkhDVIAFVTA-IAEYCGEAGRYIHFGLTSSDVVDTALALQLREALDIILKDLKEL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 136 QKALVITAENNQDAVMPGYTHLQRAQPVTFAH-WCLAYSEMlARDESRLKDTLKRLDVSPLGcGALaGTAYDID---REQ 211
Cdd:cd01360 118 LEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLkFALWYAEF-KRHLERLKEARERILVGKIS-GAV-GTYANLGpevEER 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 212 LASWLGFASATRNSldTVSDRDHVLELLSDASIGMVHLSRFAEDLIFFNSGEAGFVELS-DKVTSGSSLMPQKKNPDALE 290
Cdd:cd01360 195 VAEKLGLKPEPIST--QVIQRDRHAEYLSTLALIASTLEKIATEIRHLQRTEVLEVEEPfSKGQKGSSAMPHKRNPILSE 272
|
....
gi 757599009 291 LIRG 294
Cdd:cd01360 273 NICG 276
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
108-428 |
1.45e-13 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 72.47 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 108 SRNDQVATDLKLWCKDQVALLLEAVTELQKALVITAENNQDAVMPGYTHLQRAQPVT----FAhwclAYSEMLARDESRL 183
Cdd:PRK12273 142 STNDAYPTAIRIALLLSLRKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTlgqeFG----AYAVALAEDRKRL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 184 KDTLKRLDVSPLGcgalaGTA----------YdIDR--EQLA--SWLGFASATrNSLDTVSDRDHVLELLSDASIGMVHL 249
Cdd:PRK12273 218 YRAAELLREVNLG-----ATAigtglnappgY-IELvvEKLAeiTGLPLVPAE-DLIEATQDTGAFVEVSGALKRLAVKL 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 250 SRFAEDLIFFNSG-EAGFVELS-DKVTSGSSLMPQKKNPDALELIRGKCGRVQGA-LTGMMMTLKG-------LPL-AYN 318
Cdd:PRK12273 291 SKICNDLRLLSSGpRAGLNEINlPAVQAGSSIMPGKVNPVIPEVVNQVCFQVIGNdTTVTMAAEAGqlelnvmEPViAYN 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 319 kdmqedkegLFDALDTwldcMHMAALVL-----DGIQIRRPRCEDAAKQGYANATELADYLvakgvpfreAHHIVGEAVV 393
Cdd:PRK12273 371 ---------LFESISI----LTNACRTLrekciDGITANEERCREYVENSIGIVTALNPYI---------GYENAAEIAK 428
|
330 340 350
....*....|....*....|....*....|....*
gi 757599009 394 TAIAQGKALEEMALSDlQKFSDTiQLDvyEILSLQ 428
Cdd:PRK12273 429 EALETGKSVRELVLER-GLLTEE-ELD--DILSPE 459
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
107-292 |
4.05e-12 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 68.10 E-value: 4.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 107 RSRNDQVATDLKLWCKDQVALLLEAVTELQKALVITAENNQDAVMPGYTHLQRAQPVTFAHWCLAYSEMLARDESRLKDT 186
Cdd:PRK14515 145 QSTNDAFPTAIHIATLNALEGLLQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQS 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 187 LKRLDVSPLGCGALaGTAYDIDREQLASWLGFASA--------TRNSLDTVSDRDHVLELLSDASIGMVHLSRFAEDLIF 258
Cdd:PRK14515 225 RQHLYEVNMGATAV-GTGLNADPEYIEAVVKHLAAiselplvgAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRL 303
|
170 180 190
....*....|....*....|....*....|....*.
gi 757599009 259 FNSG-EAGFVELS-DKVTSGSSLMPQKKNPDALELI 292
Cdd:PRK14515 304 MASGpRVGLAEIMlPARQPGSSIMPGKVNPVMPEVI 339
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
128-384 |
6.36e-12 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 67.42 E-value: 6.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 128 LLEAVTELQKALVITAENNQDAVMPGYTHLQRAQPVTFAHWCLAYSEMLARDESRLKDTLKRLdvSPLgcgALAGTA--- 204
Cdd:PRK00485 160 LLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHL--YEL---ALGGTAvgt 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 205 -------YDiDR--EQLASWLGfasatrnsLDTVSDRDHVlELLS--DAsigMVHLS-----------RFAEDLIFFNSG 262
Cdd:PRK00485 235 glnahpgFA-ERvaEELAELTG--------LPFVTAPNKF-EALAahDA---LVEASgalktlavslmKIANDIRWLASG 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 263 -EAGFVELS-DKVTSGSSLMPQKKNP---DALELIrgkCGRVQG--------ALTG-----MMMTLkglpLAYNkdMQED 324
Cdd:PRK00485 302 pRCGLGEISlPENEPGSSIMPGKVNPtqcEALTMV---CAQVMGndaavtfaGSQGnfelnVFKPV----IAYN--FLQS 372
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 757599009 325 KEGLFDAldtwldCMHMAALVLDGIQIRRPRCEDAAKQ------------GYANATELADYLVAKGVPFREA 384
Cdd:PRK00485 373 IRLLADA------MRSFADHCVVGIEPNRERIKELLERslmlvtalnphiGYDKAAKIAKKAHKEGLTLKEA 438
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
106-384 |
4.04e-11 |
|
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial fumarase, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.
Pssm-ID: 176465 [Multi-domain] Cd Length: 455 Bit Score: 64.83 E-value: 4.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 106 GRSRND------QVATDLKLwckdqVALLLEAVTELQKALVITAENNQDAVMPGYTHLQRAQPVTFAHWCLAYSEMLARD 179
Cdd:cd01362 133 SQSSNDtfptamHIAAALAL-----QERLLPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHA 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 180 ESRLKDTLKRLDVSPLGcGALAGTAYDIDRE-------QLA--SWLGFASATrNSLDTVSDRDHVLELLSDASIGMVHLS 250
Cdd:cd01362 208 IARIEAALPRLYELALG-GTAVGTGLNAHPGfaekvaaELAelTGLPFVTAP-NKFEALAAHDALVEASGALKTLAVSLM 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 251 RFAEDLIFFNSG-EAGFVELS-DKVTSGSSLMPQKKNP---DALELIrgkCGRVQGALTGmmMTLKG----------LPL 315
Cdd:cd01362 286 KIANDIRWLGSGpRCGLGELSlPENEPGSSIMPGKVNPtqcEALTMV---AAQVMGNDAA--ITIAGssgnfelnvfKPV 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 316 -AYNkdMQEDKEGLFDAldtwldCMHMAALVLDGIQIRRPRCEDAAKQ------------GYANATELADYLVAKGVPFR 382
Cdd:cd01362 361 iIYN--LLQSIRLLADA------CRSFADKCVAGIEPNRERIAELLERslmlvtalnphiGYDKAAKIAKKAHKEGLTLK 432
|
..
gi 757599009 383 EA 384
Cdd:cd01362 433 EA 434
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
106-384 |
6.34e-11 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 63.94 E-value: 6.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 106 GRSRNDQVATDLKLWCKDQV-ALLLEAVTELQKALVITAENNQDAVMPGYTHLQRAQPVTFAHWCLAYSEMLARDESRLK 184
Cdd:PLN00134 129 SQSSNDTFPTAMHIAAATEIhSRLIPALKELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQ 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 185 DTLKRLDVSPLGcGALAGTAYDIDR-------EQLA--SWLGFASAtRNSLDTVSDRDHVLELLSDASIGMVHLSRFAED 255
Cdd:PLN00134 209 CTLPRLYELAQG-GTAVGTGLNTKKgfdekiaAAVAeeTGLPFVTA-PNKFEALAAHDAFVELSGALNTVAVSLMKIAND 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 256 LIFFNSG-EAGFVELS-DKVTSGSSLMPQKKNPDALELIRGKCGRVQGalTGMMMTLKGL----------PL-AYNkdMQ 322
Cdd:PLN00134 287 IRLLGSGpRCGLGELNlPENEPGSSIMPGKVNPTQCEALTMVCAQVMG--NHVAITVGGSaghfelnvfkPLiAYN--LL 362
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 757599009 323 EDKEGLFDALDTwldcmhMAALVLDGIQIRRPRCEDAA------------KQGYANATELADYLVAKGVPFREA 384
Cdd:PLN00134 363 HSIRLLGDASAS------FRKNCVRGIEANRERISKLLheslmlvtalnpKIGYDKAAAVAKKAHKEGTTLKEA 430
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
100-411 |
7.23e-09 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 57.72 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 100 GKKLHTGRSRNDQVATDLKLWCKDQVALLLEAVTELQKALVITAENNQDAVMPGYTHLQRAQPVTFAHWCLAYSEMLARD 179
Cdd:PRK09053 99 ARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 180 ESRLKDTLKRLDVspLGCGALAGTAYDIDREQLASWLGFASATRNSLDTVS---DRDHVLELLSdaSIGMV--HLSRFAE 254
Cdd:PRK09053 179 RQRLAALRPRALV--LQFGGAAGTLASLGEQALPVAQALAAELQLALPALPwhtQRDRIAEFAS--ALGLLagTLGKIAR 254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 255 DLIFFNSGEAGFV-ELSDKVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMmmtLKGLPlaynkdmQEDKE--GLFDA 331
Cdd:PRK09053 255 DVSLLMQTEVGEVfEPAAAGKGGSSTMPHKRNPVGCAAVLTAATRAPGLVATL---FAAMP-------QEHERalGGWHA 324
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 332 -LDTWLDCMHMAA-------LVLDGIQIRRPRCED--AAKQG--YANATELAdylVAKGVPFREAHHIVGEAVVTAIAQG 399
Cdd:PRK09053 325 eWDTLPELACLAAgalaqmaQIVEGLEVDAARMRAnlDLTHGliLAEAVMLA---LADRIGRLDAHHLVEQASKRAVAEG 401
|
330
....*....|..
gi 757599009 400 KALEEMALSDLQ 411
Cdd:PRK09053 402 RHLRDVLAEDPQ 413
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
97-292 |
1.19e-08 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 56.60 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 97 GDLGKKLHTGRSRNDQVATDLKLWCKDQVALLLEAVTELQKAL-VITAENNQDAVMpGYTHLQRAQPVTFAHWCLAYSEM 175
Cdd:PRK05975 96 EEAAAHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLdALEATFGQNALM-GHTRMQAAIPITVADRLASWRAP 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 176 LARDESRLKDTlkRLDVSPLGCGALAGT------AYDIDREQLASWLGFASATR--NSLDTVSDRDHVLELLSDAsigmv 247
Cdd:PRK05975 175 LLRHRDRLEAL--RADVFPLQFGGAAGTleklggKAAAVRARLAKRLGLEDAPQwhSQRDFIADFAHLLSLVTGS----- 247
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 757599009 248 hLSRFAEDLiffnsgeAGFVELSDKVT----SGSSLMPQKKNPDALELI 292
Cdd:PRK05975 248 -LGKFGQDI-------ALMAQAGDEISlsggGGSSAMPHKQNPVAAETL 288
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
106-290 |
3.35e-07 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 52.62 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 106 GRSRNDQVATDLKLWCKDQV-ALLLEAVTELQKALVITAENNQDAVMPGYTHLQRAQPVTFAHWCLAYSEMLARDESRLK 184
Cdd:PRK12425 135 SQSSNDCFPTAMHIAAAQAVhEQLLPAIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIR 214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 185 DTLKRldVSPLGCGALA---------GTAYDIDREQLA-SWLGFASATrNSLDTVSDRDHVLELLSDASIGMVHLSRFAE 254
Cdd:PRK12425 215 AALPA--VCELAQGGTAvgtglnaphGFAEAIAAELAAlSGLPFVTAP-NKFAALAGHEPLVSLSGALKTLAVALMKIAN 291
|
170 180 190
....*....|....*....|....*....|....*...
gi 757599009 255 DLIFFNSG-EAGFVELSDKVTS-GSSLMPQKKNPDALE 290
Cdd:PRK12425 292 DLRLLGSGpRAGLAEVRLPANEpGSSIMPGKVNPTQCE 329
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
249-427 |
6.79e-05 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 43.86 E-value: 6.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 249 LSRFAEDLIFFNSGEAGFVELSDKVTS-GSSLMPQKKNPDALELIrgkcgrvqgalTGMMMTLKGLPLAYNKDMQEDKEG 327
Cdd:PRK08937 30 LEKFANEIRLLQRSEIREVEEPFAKGQkGSSAMPHKRNPIGSERI-----------TGLARVLRSYLVTALENVPLWHER 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 328 --------------LFDALDTWLDCMHMaalVLDGIQIRRPRCED-AAKQGYANATE-LADYLVAKGVPFREAHHIVGEA 391
Cdd:PRK08937 99 dlshssaerialpdAFLALDYILNRFVN---ILENLVVFPENIERnLDKTLGFIATErVLLELVEKGMGREEAHELIREK 175
|
170 180 190
....*....|....*....|....*....|....*.
gi 757599009 392 VVTAIAQGKALEEMALSDlQKFSdtIQLDVYEILSL 427
Cdd:PRK08937 176 AMEAWKNQKDLRELLEAD-ERFT--KQLTKEELDEL 208
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| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
143-286 |
1.41e-03 |
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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: 40.76 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 757599009 143 AENNQDAVMPGYTHLQRAQPVTFA-HWCLAYSEMLA--RDESRLKDTLKRLDVS-PLGCGALAGTAYDIDREQ------- 211
Cdd:cd03302 130 ALEYKDLPTLGFTHYQPAQLTTVGkRACLWIQDLLMdlRNLERLRDDLRFRGVKgTTGTQASFLDLFEGDHDKvealdel 209
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90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 757599009 212 LASWLGFASATrNSLDTVSDRDHVLELLSD-ASIGMVhLSRFAEDLIFFnsgeAGFVELSD---KVTSGSSLMPQKKNP 286
Cdd:cd03302 210 VTKKAGFKKVY-PVTGQTYSRKVDIDVLNAlSSLGAT-AHKIATDIRLL----ANLKEVEEpfeKGQIGSSAMPYKRNP 282
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