|
Name |
Accession |
Description |
Interval |
E-value |
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
17-481 |
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: 665.26 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 17 ALWGGRFSSGPSAELAKLSKSTQFDWRLADDDIAGSRAHAHALHRAGLLTNQEYEDLQKALDELQNRVDNGTFTPIEEDE 96
Cdd:COG0165 4 KLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAFEFDPELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 97 DEATALERGLLDIAGsELGGKLRAGRSRNDQIAALIRMFLRRHSRVLATLVLDVCNALVAQSLAAKDSVMPGRTHMQHAQ 176
Cdd:COG0165 84 DIHMNIERRLIERIG-DVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRAQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 177 PILLAHQLMAHVWPLLRDVNRLADWDSRANESPYGAGALAGNTLGLDPEEVSKELGFSAVCANSIDATASRDIVAEFSFI 256
Cdd:COG0165 163 PVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFLSA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 257 AAMIGVDISRLSEEIIIWNTQEFAFVTLDDAYSTGSSIMPQKKNPDIAELARGKAGRLIGDLTGLMATLKGLPTAYARDL 336
Cdd:COG0165 243 ASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNKDL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 337 QEDKEAVFDQIDTLEVLLPAFAGMVRTMRFNIARLREQSATGFALATDIAEWLVKQGVPFRNAHKLSGLCVKRAEELGGD 416
Cdd:COG0165 323 QEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGFSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKGKD 402
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490223448 417 LDVLSDDDFANILNDFvdRADIENlklVLSSDGSVASRCGKGGTAFVRVKEQITQAQLAIDEYKK 481
Cdd:COG0165 403 LEDLTLEELQAFSPLI--EEDVYE---ALDPEGSVAARDSYGGTAPEAVREQIARARARLAALRA 462
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
18-473 |
0e+00 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 657.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 18 LWGGRFSSGPSAELAKLSKSTQFDWRLADDDIAGSRAHAHALHRAGLLTNQEYEDLQKALDELQNRVDNGTFTPIEEDED 97
Cdd:PRK00855 6 LWGGRFSEGPDELVERFTASISFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILEEIEAGKFEFSPELED 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 98 EATALERGLLDIAGsELGGKLRAGRSRNDQIAALIRMFLRRHSRVLATLVLDVCNALVAQSLAAKDSVMPGRTHMQHAQP 177
Cdd:PRK00855 86 IHMAIEARLTERIG-DVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 178 ILLAHQLMAHVWPLLRDVNRLADWDSRANESPYGAGALAGNTLGLDPEEVSKELGFSAVCANSIDATASRDIVAEFSFIA 257
Cdd:PRK00855 165 VTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAALAGTTFPIDRERTAELLGFDGVTENSLDAVSDRDFALEFLSAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 258 AMIGVDISRLSEEIIIWNTQEFAFVTLDDAYSTGSSIMPQKKNPDIAELARGKAGRLIGDLTGLMATLKGLPTAYARDLQ 337
Cdd:PRK00855 245 SLLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLAYNRDLQ 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 338 EDKEAVFDQIDTLEVLLPAFAGMVRTMRFNIARLREQSATGFALATDIAEWLVKQGVPFRNAHKLSGLCVKRAEELGGDL 417
Cdd:PRK00855 325 EDKEPLFDAVDTLKLSLEAMAGMLETLTVNKERMREAAGKGFSTATDLADYLVRKGVPFREAHEIVGKAVREAEERGVDL 404
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 490223448 418 DVLSDDDFANIlNDFVDRADIEnlklVLSSDGSVASRCGKGGTAFVRVKEQITQAQ 473
Cdd:PRK00855 405 ADLSLEELQAF-SPLITEDVYE----VLTPEGSVAARNSIGGTAPEQVREQIARAK 455
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
18-473 |
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: 555.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 18 LWGGRFSSGPSAELAKLSKSTQFDWRLADDDIAGSRAHAHALHRAGLLTNQEYEDLQKALDELQNRVDNGTFTPIEEDED 97
Cdd:TIGR00838 1 LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPFILDPDDED 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 98 EATALERGLLDIAGSELGGKLRAGRSRNDQIAALIRMFLRRHSRVLATLVLDVCNALVAQSLAAKDSVMPGRTHMQHAQP 177
Cdd:TIGR00838 81 IHMAIERELIDRVGEDLGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 178 ILLAHQLMAHVWPLLRDVNRLADWDSRANESPYGAGALAGNTLGLDPEEVSKELGFSAVCANSIDATASRDIVAEFSFIA 257
Cdd:TIGR00838 161 ITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFVA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 258 AMIGVDISRLSEEIIIWNTQEFAFVTLDDAYSTGSSIMPQKKNPDIAELARGKAGRLIGDLTGLMATLKGLPTAYARDLQ 337
Cdd:TIGR00838 241 ALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 338 EDKEAVFDQIDTLEVLLPAFAGMVRTMRFNIARLREQSATGFALATDIAEWLVKQGVPFRNAHKLSGLCVKRAEELGGDL 417
Cdd:TIGR00838 321 EDKEPLFDALKTVELSLEMATGMLDTITVNKERMEEAASAGFSNATELADYLVRKGVPFREAHHIVGELVATAIERGKGL 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 490223448 418 DVLSDDDFANILNDFVdradiENLKLVLSSDGSVASRCGKGGTAFVRVKEQITQAQ 473
Cdd:TIGR00838 401 EELTLEELQKFSPEFD-----EDVYEALDPESSVEKRDAKGGTAPEEVLQAIAEAK 451
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
37-472 |
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: 544.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 37 STQFDWRLADDDIAGSRAHAHALHRAGLLTNQEYEDLQKALDELQNRVDNGTFTPIEEDEDEATALERGLLDIAGsELGG 116
Cdd:cd01359 1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIG-DVGG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 117 KLRAGRSRNDQIAALIRMFLRRHSRVLATLVLDVCNALVAQSLAAKDSVMPGRTHMQHAQPILLAHQLMAHVWPLLRDVN 196
Cdd:cd01359 80 KLHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 197 RLADWDSRANESPYGAGALAGNTLGLDPEEVSKELGFSAVCANSIDATASRDIVAEFSFIAAMIGVDISRLSEEIIIWNT 276
Cdd:cd01359 160 RLADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWST 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 277 QEFAFVTLDDAYSTGSSIMPQKKNPDIAELARGKAGRLIGDLTGLMATLKGLPTAYARDLQEDKEAVFDQIDTLEVLLPA 356
Cdd:cd01359 240 QEFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 357 FAGMVRTMRFNIARLREQSATGFALATDIAEWLVKQ-GVPFRNAHKLSGLCVKRAEELGGDLDVLSDDDFANILNdfVDR 435
Cdd:cd01359 320 LTGVISTLTVNPERMREAAEAGFSTATDLADYLVREkGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISP--LFE 397
|
410 420 430
....*....|....*....|....*....|....*..
gi 490223448 436 ADIenlKLVLSSDGSVASRCGKGGTAFVRVKEQITQA 472
Cdd:cd01359 398 EDV---REALDPENSVERRTSYGGTAPAEVREQIARA 431
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
18-469 |
2.03e-164 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 473.83 E-value: 2.03e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 18 LWGGRFSSGPSAELAKLSKSTQFDWRLADDDIAGSRAHAHALHRAGLLTNQEYEDLQKALDELQNRVDNGTFTPIEEDED 97
Cdd:PLN02646 18 LWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAGKFEWRPDRED 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 98 EATALERGLLDIAGsELGGKLRAGRSRNDQIAALIRMFLRRHSRVLATLVLDVCNALVAQSLAAKDSVMPGRTHMQHAQP 177
Cdd:PLN02646 98 VHMNNEARLTELIG-EPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 178 ILLAHQLMAHVWPLLRDVNRLADWDSRANESPYGAGALAGNTLGLDPEEVSKELGFSAVCANSIDATASRDIVAEFSFIA 257
Cdd:PLN02646 177 VLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRDFVLEFLFAN 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 258 AMIGVDISRLSEEIIIWNTQEFAFVTLDDAYSTGSSIMPQKKNPDIAELARGKAGRLIGDLTGLMATLKGLPTAYARDLQ 337
Cdd:PLN02646 257 SITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTAYNRDLQ 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 338 EDKEAVFDQIDTLEVLLPAFAGMVRTMRFNIARLREQSATGFALATDIAEWLVKQGVPFRNAHKLSGLCVKRAEELGGDL 417
Cdd:PLN02646 337 EDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLDATTLADYLVRKGVPFRETHHIVGAAVALAESKGCEL 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 490223448 418 DVLSDDDFANILNDFvdRADIENlklVLSSDGSVASRCGKGGTAFVRVKEQI 469
Cdd:PLN02646 417 SDLTLEDLKSINPVF--EEDVYE---VLGVENSVEKFDSYGSTGSRSVLEQL 463
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
17-473 |
1.33e-129 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 384.34 E-value: 1.33e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 17 ALWGGRFSSGPSAELAKLSKSTQFDWRLADDDIAGSRAHAHALHRAGLLTNQEYEDLQKALDELQNRVDNGTFTPIEED- 95
Cdd:PRK04833 2 ALWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQQQLEEALNELLEEVRANPQQILASDa 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 96 EDEATALERGLLDIAGsELGGKLRAGRSRNDQIAALIRMFLRRHSRVLATLVLDVCNALVAQSLAAKDSVMPGRTHMQHA 175
Cdd:PRK04833 82 EDIHSWVEGKLIDKVG-DLGKKLHTGRSRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 176 QPILLAHQLMAHVWPLLRDVNRLADWDSRANESPYGAGALAGNTLGLDPEEVSKELGFSAVCANSIDATASRDIVAEFSF 255
Cdd:PRK04833 161 QPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 256 IAAMIGVDISRLSEEIIIWNTQEFAFVTLDDAYSTGSSIMPQKKNPDIAELARGKAGRLIGDLTGLMATLKGLPTAYARD 335
Cdd:PRK04833 241 DASISMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPLAYNKD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 336 LQEDKEAVFDQIDTLEVLLPAFAGMVRTMRFNIARLREQSATGFALATDIAEWLVKQGVPFRNAHKLSGLCVKRAEELGG 415
Cdd:PRK04833 321 MQEDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYANATELADYLVAKGVPFREAHHIVGEAVVEAIRQGK 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490223448 416 DLDVLSDDD---FANILNDfvdraDIENlklVLSSDGSVASRCGKGGTAFVRVKEQITQAQ 473
Cdd:PRK04833 401 PLEDLPLAElqkFSSVIGD-----DVYP---ILSLQSCLDKRAAKGGVSPQQVAQAIAAAK 453
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
16-473 |
5.55e-112 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 344.46 E-value: 5.55e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 16 IALWGGRFSSGPSAELAKLSKSTQFDWRLADDDIAGSRAHAHALHRAGLLTNQEYEDLQKALDELQNRV-DNGTFTPIEE 94
Cdd:PRK12308 1 MALWGGRFSQAADTRFKQFNDSLRFDYRLAEQDIVGSIAWSKALLSVGVLSEEEQQKLELALNELKLEVmEDPEQILLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 95 DEDEATALERGLLDIAGsELGGKLRAGRSRNDQIAALIRMFLRRHSRVLATLVLDVCNALVAQSLAAKDSVMPGRTHMQH 174
Cdd:PRK12308 81 AEDIHSWVEQQLIGKVG-DLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 175 AQPILLAHQLMAHVWPLLRDVNRLADWDSRANESPYGAGALAGNTLGLDPEEVSKELGFSAVCANSIDATASRDIVAEFS 254
Cdd:PRK12308 160 AQPVTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGSGALAGTAYPIDREALAHNLGFRRATRNSLDSVSDRDHVMELM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 255 FIAAMIGVDISRLSEEIIIWNTQEFAFVTLDDAYSTGSSIMPQKKNPDIAELARGKAGRLIGDLTGLMATLKGLPTAYAR 334
Cdd:PRK12308 240 SVASISMLHLSRLAEDLIFYNSGESGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNK 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 335 DLQEDKEAVFDQIDTLEVLLPAFAGMVRTMRFNIARLREQSATGFALATDIAEWLVKQGVPFRNAHKLSGLCVKRAEELG 414
Cdd:PRK12308 320 DMQEDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYANATELADYLVAKGIPFREAHHIVGVAVVGAIAKG 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 490223448 415 GDLDVLSDDDFanilNDFVDRADiENLKLVLSSDGSVASRCGKGGTAFVRVKEQITQAQ 473
Cdd:PRK12308 400 CALEELSLEQL----KEFSDVIE-DDVYQILTIESCLEKRCALGGVSPEQVAYAVEQAD 453
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
48-367 |
3.57e-111 |
|
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: 332.16 E-value: 3.57e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 48 DIAGSRAHAHALHRAGLLTNQEYEDLQKALDELQNRVDNGTFTPIEEDEDEATALERGLLDIAGSELGGKLRAGRSRNDQ 127
Cdd:cd01334 4 DLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVEQEGSGTHDVMAVEEVLAERAGELNGGYVHTGRSSNDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 128 IAALIRMFLRRHSRVLATLVLDVCNALVAQSLAAKDSVMPGRTHMQHAQPILLAHQLMAHVWPLLRDVNRLADWDSRANE 207
Cdd:cd01334 84 VDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKRLNV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 208 SPYGAGALAG--NTLGLDPEEVSKELGFSAVCANSIDATASRDIVAEFSFIAAMIGVDISRLSEEIIIWNTQEFAFVTLD 285
Cdd:cd01334 164 LPLGGGAVGTgaNAPPIDRERVAELLGFFGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEVELP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 286 DAYSTGSSIMPQKKNPDIAELARGKAGRLIGDLTGLMATLKGLPTAYARDLQEDKEAVFDQIDTLEVLLPAFAGMVRTMR 365
Cdd:cd01334 244 DAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVLEGLE 323
|
..
gi 490223448 366 FN 367
Cdd:cd01334 324 VN 325
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
21-316 |
1.43e-65 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 214.54 E-value: 1.43e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 21 GRFSSGPSAELAKLSKSTQFDWRLADDDIAGSRAHAHALHRAGLLTNQEYEDLQKALDELQNRVDNGTFTPIEE-DEDEA 99
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDDQFPLKVwQEGSG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 100 TALERGLLDIAGSELG------GKLRAGRSRNDQIAALIRMFLRRH-SRVLATLVLDVCNALVAQSLAAKDSVMPGRTHM 172
Cdd:pfam00206 81 TAVNMNLNEVIGELLGqlvhpnDHVHTGQSSNDQVPTALRLALKDAlSEVLLPALRQLIDALKEKAKEFADIVKPGRTHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 173 QHAQPILLAHQLMAHVWPLLRDVNRLADWDSRANESPYGAGALAGNTLGLDPE-------EVSKELGFSAVCANSIDATA 245
Cdd:pfam00206 161 QDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEfaelvakELGFFTGLPVKAPNSFEATS 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490223448 246 SRDIVAEFSFIAAMIGVDISRLSEEIIIWNTQEFAFVTLDDAYST-GSSIMPQKKNPDIAELARGKAGRLIG 316
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEpGSSIMPGKVNPDQLELLTGKAGRVMG 312
|
|
| PRK02186 |
PRK02186 |
argininosuccinate lyase; Provisional |
41-439 |
1.32e-51 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235010 [Multi-domain] Cd Length: 887 Bit Score: 188.13 E-value: 1.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 41 DWRLADDDIAGSRAHAHALHRAGLLTNQEYEDLQKALDELQNrvdnGTFTPIEE-DEDEAT--ALERGLLDIAGSELGGK 117
Cdd:PRK02186 434 PLAELDHLAAIDEAHLVMLGDTGIVAPERARPLLDAHRRLRD----AGFAPLLArPAPRGLymLYEAYLIERLGEDVGGV 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 118 LRAGRSRNDQIAALIRMFLRRHSRVLATLVLDVCNALVAQSLAAKDSVMPGRTHMQHAQPILLAHQLMAHVWPLLRDVNR 197
Cdd:PRK02186 510 LQTARSRNDINATTTKLHLREATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHA 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 198 LADWDSRANESPYGAGALAGNTLGLDPEEVSKELGFSAVCANSIDATASRDIVAEFSFIAAMIGVDISRLSEEIIIWNTQ 277
Cdd:PRK02186 590 LFALFEHIDVCPLGAGAGGGTTFPIDPEFVARLLGFEQPAPNSLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQLWTTR 669
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 278 EFAFVTLDDAYSTGSSIMPQKKNPDIAELARGKAGRLIGDLTGLMATLKGLPTA-------YARDLQEDKEAVFDQIDTL 350
Cdd:PRK02186 670 EFALVSLPDALTGGSSMLPQKKNPFLLEFVKGRAGVVAGALASASAALGKTPFSnsfeagsPMNGPIAQACAAIEDAAAV 749
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 351 EVLlpafagMVRTMRFNIARLREQSATGFALATDIAEWLVKQ-GVPFRNAHKLSGLCVKRAEELGGDldvlSDDDFANIL 429
Cdd:PRK02186 750 LVL------LIDGLEADQARMRAHLEDGGVSATAVAESLVVRrSISFRSAHTQVGQAIRQSLDQGRS----SADALAALD 819
|
410
....*....|
gi 490223448 430 NDFVDRADIE 439
Cdd:PRK02186 820 PQFVSRAPLE 829
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
102-358 |
8.99e-48 |
|
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: 165.09 E-value: 8.99e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 102 LERGLLDIAGSELGGKLRA-----GRSRNDQIAALIRMFLRRHSRVLATLVLDVCNALVAQSLAAKDSVMPGRTHMQHAQ 176
Cdd:cd01594 16 VEEVLAGRAGELAGGLHGSalvhkGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDAQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 177 PILLAHQLMAHVWPLLRDVNRLADWDsranespygagalagntlgldpeevskelgfsavcansidatasrdiVAEFSFI 256
Cdd:cd01594 96 PVTLGYELRAWAQVLGRDLERLEEAA-----------------------------------------------VAEALDA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 257 AAMIGVDISRLSEEIIIWNTQEFAFVTLDDA-YSTGSSIMPQKKNPDIAELARGKAGRLIGDLTGLMATLKGLPTAYARD 335
Cdd:cd01594 129 LALAAAHLSKIAEDLRLLLSGEFGELGEPFLpGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDNED 208
|
250 260
....*....|....*....|...
gi 490223448 336 LQEDKEAVFDQIDTLEVLLPAFA 358
Cdd:cd01594 209 SPSMREILADSLLLLIDALRLLL 231
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
53-400 |
8.60e-37 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 142.05 E-value: 8.60e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 53 RAHAHALHRAGLLTNQEYEDLQKALDELQnRVDNGTFTPIEEDEDEATALERGLLDIAGSELGGKLRAGRSRNDQIAALI 132
Cdd:PRK06705 46 KAHIVMLTEENLMKKEEAKFILHALKKVE-EIPEEQLLYTEQHEDLFFLVEHLISQEAKSDFVSNMHIGRSRNDMGVTMY 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 133 RMFLRRHSRVLATLVLDVCNALVAQSLAAKDSVMPGRTHMQHAQPILLAHQLMAHVWPLLRDVNRLADWDSRANESPYGA 212
Cdd:PRK06705 125 RMSLRRYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKTYKLLNQSPMGA 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 213 GALAGNTLGLDPEEVSKELGFSAVCANSIDATASRDIVAEFSFIAAMIGVDISRLSEEIIIWNTQEFAFVTLDDAYSTGS 292
Cdd:PRK06705 205 AALSTTSFPIKRERVADLLGFTNVIENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLATKEYDGITVARPYVQIS 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 293 SIMPQKKNPDIAELARGKAGRLIGDLTGLMATLKGLPTAYARDLQEDKEA-VFDQIDTLEVLLPAFAGMVRTMRFNIARL 371
Cdd:PRK06705 285 SIMPQKRNPVSIEHARAITSSALGEAFTVFQMIHNTPFGDIVDTEDDLQPyLYKGIEKAIRVFCIMNAVIRTMKVEEDTL 364
|
330 340 350
....*....|....*....|....*....|
gi 490223448 372 REQSATGFALATDIAEWLVKQ-GVPFRNAH 400
Cdd:PRK06705 365 KRRSYKHAITITDFADVLTKNyGIPFRHAH 394
|
|
| PRK06389 |
PRK06389 |
argininosuccinate lyase; Provisional |
54-442 |
1.69e-28 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 235791 [Multi-domain] Cd Length: 434 Bit Score: 117.30 E-value: 1.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 54 AHAHALHRAGLLTNQEYEDLQKAL-DELQNRVdngTFTPieEDEDEATALERGLLDIAGsELGGKLRAGRSRNDQIAALI 132
Cdd:PRK06389 41 AYHVALAQRRLITEKAPKCVINALiDIYKNGI---EIDL--DLEDVHTAIENFVIRRCG-DMFKNFRLFLSRNEQVHADL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 133 RMFLRRHSRVLATLVLDVCNALVAQSLAAKdsvMPGRTHMQHAQPILLAhQLMAHVWPLL-RDVNRLADWDSRANESPYG 211
Cdd:PRK06389 115 NLFIIDKIIEIEKILYEIIKVIPGFNLKGR---LPGYTHFRQAMPMTVN-TYINYIKSILyHHINNLDSFLMDLREMPYG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 212 AGALAGNTLGLDPEEVSKELGFSAVCANSIDATaSRDI--VAEFSFIAAMIGVDISRLSEEIIIWNtqEFAFVTLDDAYS 289
Cdd:PRK06389 191 YGSGYGSPSSVKFNQMSELLGMEKNIKNPVYSS-SLYIktIENISYLISSLAVDLSRICQDIIIYY--ENGIITIPDEFT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 290 TGSSIMPQKKNPDIAELARGKAGRLIGDLTGLMATLKGLPTAYARDLQEDKEAVFDQIDTLEVLLPAFAGMVRTMRFNIA 369
Cdd:PRK06389 268 TGSSLMPNKRNPDYLELFQGIAAESISVLSFIAQSELNKTTGYHRDFQIVKDSTISFINNFERILLGLPDLLYNIKFEIT 347
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490223448 370 rlREQSATGFALATDIAEWLVKQGVPFRNAHKLSGLCVKRAEElggdldvLSDDDFanilNDFVDRADIENLK 442
Cdd:PRK06389 348 --NEKNIKNSVYATYNAWLAFKNGMDWKSAYAYIGNKIREGEV-------LDEYQP----EDLTDYIDVNELK 407
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
74-414 |
6.53e-23 |
|
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: 100.27 E-value: 6.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 74 QKALDELQNRVDNGTFTPIEEDEDEAT------ALERGLLDIAGSELGGKLRAGRSRNDQIAALIRMFLRRHSRVLATLV 147
Cdd:cd01595 33 KEAAEEIRAAADVFEIDAERIAEIEKEtghdviAFVYALAEKCGEDAGEYVHFGATSQDINDTALALQLRDALDIILPDL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 148 LDVCNALVAQSLAAKDSVMPGRTHMQHAQPILLAHQLMAHVWPLLRDVNRLADwdsraNESPYGAGALAGNT-----LGL 222
Cdd:cd01595 113 DALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEE-----ARERVLVGGISGAVgthasLGP 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 223 DPEEVS----KELGFSAVCANSidATASRDIVAEFSFIAAMIGVDISRLSEEIIIWNTQEFAFVTLD-DAYSTGSSIMPQ 297
Cdd:cd01595 188 KGPEVEervaEKLGLKVPPITT--QIEPRDRIAELLSALALIAGTLEKIATDIRLLQRTEIGEVEEPfEKGQVGSSTMPH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 298 KKNPDIAELARGKAGRLIGDLTGLMATLkglptayARDLQEDkeavfdqID---TLEVLLPAFA-----------GMVRT 363
Cdd:cd01595 266 KRNPIDSENIEGLARLVRALAAPALENL-------VQWHERD-------LSdssVERNILPDAFllldaalsrlqGLLEG 331
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 490223448 364 MRFNIARLRE--QSATGFALATDIAEWLVKQGVPFRNAHKLsglcVKRAEELG 414
Cdd:cd01595 332 LVVNPERMRRnlDLTWGLILSEAVMMALAKKGLGRQEAYEL----VKEENYLG 380
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
56-441 |
8.82e-20 |
|
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: 91.68 E-value: 8.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 56 AHALHRAGLLTnqeyedlQKALDELQNRVDNGTFTPIEEDEDEAT------ALERGLLDIAGSElggklrAGR------- 122
Cdd:COG0015 32 AEAQAELGLIP-------AEAAAAIRAAADDFEIDAERIKEIEKEtrhdvkAFVYALKEKVGAE------AGEyihfgat 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 123 SR--NDQIAALIrmfLRRHSRVLATLVLDVCNALVAQSLAAKDSVMPGRTHMQHAQPILLAHQLMAHVWPLLRDVNRLAd 200
Cdd:COG0015 99 SQdiNDTALALQ---LREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLE- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 201 wdsRANESPYgAGALAG-----NTLGLDPEEVSK----ELGFSAVCAnsidAT--ASRDIVAEFSFIAAMIGVDISRLSE 269
Cdd:COG0015 175 ---EARERVL-VGKIGGavgtyAAHGEAWPEVEErvaeKLGLKPNPV----TTqiEPRDRHAELFSALALIAGSLEKIAR 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 270 EiiIWNTQ-----EFA--FVtlddAYSTGSSIMPQKKNPDIAELARGKAGRLIGDLTGLMATlkgLPTAYARDLqeDKEA 342
Cdd:COG0015 247 D--IRLLQrtevgEVEepFA----KGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEA---LASWHERDL--SDSS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 343 VFDQIdtLEVLLPAFAGMVRTMRFNIARL--------REQSAT-GFALATDIAEWLVKQGVPFRNAH-KLSGLCVKRAEE 412
Cdd:COG0015 316 VERNI--LPDAFLLLDGALERLLKLLEGLvvnpermrANLDLTgGLVLSEAVLMALVRRGLGREEAYeLVKELARGAWEE 393
|
410 420 430
....*....|....*....|....*....|
gi 490223448 413 lGGDL-DVLSDDDfanILNDFVDRADIENL 441
Cdd:COG0015 394 -GNDLrELLAADP---EIPAELSKEELEAL 419
|
|
| ASL_C2 |
pfam14698 |
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of ... |
379-451 |
6.22e-17 |
|
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: 75.15 E-value: 6.22e-17
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490223448 379 FALATDIAEWLVKQGVPFRNAHKLSGLCVKRAEELGGDLDVLSDDDFANILNDFvdRADIENlklVLSSDGSV 451
Cdd:pfam14698 1 FSTATDLADYLVRKGVPFREAHEIVGRLVRLAEEKGKDLEDLTLEELQAISPLF--EEDVYE---ALDPEASV 68
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
136-325 |
1.54e-15 |
|
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: 78.44 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 136 LRRHSRVLATLVLDVCNALVAQSLAAKDSVMPGRTHMQHAQPILLAHQLMAHVWPLLRDVNRLADWDSRANESPYG--AG 213
Cdd:cd01597 111 LRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGgaAG 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 214 ALAGntLGLDPEEVSK----ELGFSAVcanSIDATASRDIVAEFSFIAAMIGVDISRLSEEIIIWNTQEFAFVTLDDAYS 289
Cdd:cd01597 191 TLAS--LGDQGLAVQEalaaELGLGVP---AIPWHTARDRIAELASFLALLTGTLGKIARDVYLLMQTEIGEVAEPFAKG 265
|
170 180 190
....*....|....*....|....*....|....*..
gi 490223448 290 TG-SSIMPQKKNPDIAELARGKAGRLIGDLTGLMATL 325
Cdd:cd01597 266 RGgSSTMPHKRNPVGCELIVALARRVPGLAALLLDAM 302
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
136-308 |
7.51e-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: 69.89 E-value: 7.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 136 LRRHSRVLATLVLDVCNALVAQSLAAKDSVMPGRTHMQHAQPILLAHQLMAHVWPLLRDVNRLAdwdsRANESpYGAGAL 215
Cdd:cd01360 103 LREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLK----EARER-ILVGKI 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 216 AG-----NTLGLDPEE-VSKELGF-SAVCANSIdatASRDIVAEFSFIAAMIGVDISRLSEEII------IWNTQEFaFv 282
Cdd:cd01360 178 SGavgtyANLGPEVEErVAEKLGLkPEPISTQV---IQRDRHAEYLSTLALIASTLEKIATEIRhlqrteVLEVEEP-F- 252
|
170 180 190
....*....|....*....|....*....|
gi 490223448 283 tldDAYSTGSSIMPQKKNPDIAE----LAR 308
Cdd:cd01360 253 ---SKGQKGSSAMPHKRNPILSEnicgLAR 279
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
101-336 |
1.25e-11 |
|
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that catalyzes step 8 in the purine biosynthesis pathway for de novo synthesis of IMP and also the final reaction in the two-step sequence from IMP to AMP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273345 [Multi-domain] Cd Length: 435 Bit Score: 66.60 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 101 ALERGLLDIAGSElGGKLRAGRSRNDQIAALIRMFLRR-HSRVLATLVlDVCNALVAQSLAAKDSVMPGRTHMQHAQPIL 179
Cdd:TIGR00928 75 AVVYALKEKCGAE-GEFIHFGATSNDIVDTALALLLRDaLEIILPKLK-QLIDRLKELAVEYKDTVMLGRTHGQHAEPTT 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 180 LAHQLMAHVWPLLRDVNRL----ADWDSRANESPYGAGALAGNTLGLDPEEVSKELGFSAVCANSidATASRDIVAEFSF 255
Cdd:TIGR00928 153 LGKRFALWAEEMLRQLERLlqakERIKVGGISGAVGTHAAAYPLVEEVEERVTEFLGLKPVPIST--QIEPRDRHAELLD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 256 IAAMIGVDISRLSEEiiIWNTQEFAFVTLDDAYST---GSSIMPQKKNPDIAELARGKAGRLIGDLTGLMATlkgLPTAY 332
Cdd:TIGR00928 231 ALALLATTLEKFAVD--IRLLQRTEHFEVEEPFGKgqvGSSAMPHKRNPIDFENVCGLARVIRGYASPALEN---APLWH 305
|
....
gi 490223448 333 ARDL 336
Cdd:TIGR00928 306 ERDL 309
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
122-432 |
2.90e-10 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 62.32 E-value: 2.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 122 RSRNDQIAALIRMFLRRH-SRVLATL--VLDVCNALVAQSlaakDSVMP-GRTHMQHAQPILLAHQLMAHVWPLLRDVNR 197
Cdd:PRK14515 145 QSTNDAFPTAIHIATLNAlEGLLQTMgyMHDVFELKAEQF----DHVIKmGRTHLQDAVPIRLGQEFKAYSRVLERDMKR 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 198 LADWDSRANESPYGAGALaGNTLGLDP---EEVSKEL----GFSAVCANS-IDATASRDIVAEFSFIAAMIGVDISRLSE 269
Cdd:PRK14515 221 IQQSRQHLYEVNMGATAV-GTGLNADPeyiEAVVKHLaaisELPLVGAEDlVDATQNTDAYTEVSAALKVCMMNMSKIAN 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 270 EIIIWNTQE---FAFVTLdDAYSTGSSIMPQKKNPDIAELARGKAGRLIG-DLTGLMATLKGlptAYARDLQEdKEAVFD 345
Cdd:PRK14515 300 DLRLMASGPrvgLAEIML-PARQPGSSIMPGKVNPVMPEVINQIAFQVIGnDHTICLASEAG---QLELNVME-PVLVFN 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 346 QIDTLEVLLPAFAGM----VRTMRFNIARLRE------------QSATGFALATDIAEWLVKQGVPFRNahklsgLCVKR 409
Cdd:PRK14515 375 LLQSISIMNNGFRAFtdncLKGIEANEDRLKEyveksvgiitavNPHIGYEAAARVAKEAIATGQSVRE------LCVKN 448
|
330 340
....*....|....*....|...
gi 490223448 410 aeelggdlDVLSDDDFANILNDF 432
Cdd:PRK14515 449 --------GVLSQEDLELILDPF 463
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
121-323 |
1.24e-08 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 57.30 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 121 GRSRNDQIAALIRMFLRRHSRVLATLVLDVCNALVAQSLAAKDSVMPGRTHMQHAQPILLAHQLMAHVWPLLRDVNRLAD 200
Cdd:PRK13353 138 AQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQ 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 201 WDSRANESPYGAGALaGNTLGLDPE---EVSKELgfSAVC-------ANSIDATASRDIVAEFSFIAAMIGVDISRLSEE 270
Cdd:PRK13353 218 AREHLYEVNLGGTAV-GTGLNADPEyieRVVKHL--AAITglplvgaEDLVDATQNTDAFVEVSGALKVCAVNLSKIAND 294
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490223448 271 IIIWNTQE---FAFVTLdDAYSTGSSIMPQKKNPDIAELARGKAGRLIG-DLTGLMA 323
Cdd:PRK13353 295 LRLLSSGPrtgLGEINL-PAVQPGSSIMPGKVNPVMPEVVNQIAFQVIGnDVTITLA 350
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
121-323 |
2.07e-08 |
|
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: 56.38 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 121 GRSRNDQIAALIRMFLRRHSRVLATLVLDVCNALVAQSLAAKDSVMPGRTHMQHAQPILLAHQLMAHVWPLLRDVNRLAD 200
Cdd:cd01357 133 SQSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYK 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 201 WDSRANESPYGAGALaGNTLGLDP-------EEVSKELGFS-AVCANSIDATASRDIVAEFSFIAAMIGVDISRLSE--- 269
Cdd:cd01357 213 ARERLREVNLGGTAI-GTGINAPPgyielvvEKLSEITGLPlKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANdlr 291
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490223448 270 -----------EIIIWNTQefafvtlddaysTGSSIMPQKKNPDIAELARGKAGRLIG-DLTGLMA 323
Cdd:cd01357 292 llssgpraglgEINLPAVQ------------PGSSIMPGKVNPVIPEVVNQVAFQVIGnDLTITMA 345
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
121-305 |
5.21e-08 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 55.08 E-value: 5.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 121 GRSRNDQI--AALIRMFLRRHSRVLATLVlDVCNALVAQSLAAKDSVMPGRTHMQHAQPILLAHQLMAHVWPLLRDVNRL 198
Cdd:PLN00134 129 SQSSNDTFptAMHIAAATEIHSRLIPALK-ELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRV 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 199 ADWDSRANESPYGAGALaGNTLGLDP-------EEVSKELGFSAVCA-NSIDATASRDIVAEFSFIAAMIGVDISRLSEE 270
Cdd:PLN00134 208 QCTLPRLYELAQGGTAV-GTGLNTKKgfdekiaAAVAEETGLPFVTApNKFEALAAHDAFVELSGALNTVAVSLMKIAND 286
|
170 180 190
....*....|....*....|....*....|....*...
gi 490223448 271 IIIWNTQE---FAFVTLdDAYSTGSSIMPQKKNPDIAE 305
Cdd:PLN00134 287 IRLLGSGPrcgLGELNL-PENEPGSSIMPGKVNPTQCE 323
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
136-423 |
1.07e-07 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 54.25 E-value: 1.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 136 LRRHSRVLATLVLDVCNALVAQSLAAKDSVMPGRTHMQHAQPILLAHQLMAHVWPLLRDVNRLADWDSRANESPYG--AG 213
Cdd:PRK09053 120 LRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGgaAG 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 214 ALAgnTLGLDPEEVSKELgfsavcANSIDAT-------ASRDIVAEFSFIAAMIGVDISRLSEEIIIWNTQEFAFVTLDD 286
Cdd:PRK09053 200 TLA--SLGEQALPVAQAL------AAELQLAlpalpwhTQRDRIAEFASALGLLAGTLGKIARDVSLLMQTEVGEVFEPA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 287 AYST-GSSIMPQKKNPDIAELARGKAGRligdLTGLMATLkglptaYARDLQEDKEAV---FDQIDTLEVLLPAFAGMVR 362
Cdd:PRK09053 272 AAGKgGSSTMPHKRNPVGCAAVLTAATR----APGLVATL------FAAMPQEHERALggwHAEWDTLPELACLAAGALA 341
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490223448 363 TMR-------FNIARLREQ----------SATGFALATDIAEwlvkqgvpfRNAHKLSGLCVKRAEELGGDL-DVLSDD 423
Cdd:PRK09053 342 QMAqivegleVDAARMRANldlthglilaEAVMLALADRIGR---------LDAHHLVEQASKRAVAEGRHLrDVLAED 411
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
127-305 |
2.56e-07 |
|
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: 52.81 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 127 QIAALIrMFLRRHSRVLATLVldvcNALVAQSLAAKDSVMPGRTHMQHAQPILLAHQLMAHVWPLLRDVNRLADWDSRAN 206
Cdd:cd01596 144 HIAAAL-ALLERLLPALEQLQ----DALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLR 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 207 ESPYGAGALaGNTLGLDP-------EEVSKELGFSAVCA-NSIDATASRDIVAEFSfiAAM---------IGVDISRLSE 269
Cdd:cd01596 219 ELNLGGTAV-GTGLNAPPgyaekvaAELAELTGLPFVTApNLFEATAAHDALVEVS--GALktlavslskIANDLRLLSS 295
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490223448 270 -------EIIIwntqefafvtldDAYSTGSSIMPQKKNPDIAE 305
Cdd:cd01596 296 gpraglgEINL------------PANQPGSSIMPGKVNPVIPE 326
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
101-316 |
9.42e-07 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 50.82 E-value: 9.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 101 ALERGLLDIAGSELGGKLRAGRSRNDQIAALIRMFLRRHSRVLATLVLDVCNALVAQSLAAKDSVMPGRTHMQHAQPILL 180
Cdd:PRK05975 85 ALVRQLRAAVGEEAAAHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITV 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490223448 181 AHQLMAHVWPLLRDVNRLAdwDSRANESPYGAGALAGNTLGLDP------EEVSKELGFSAV-CANSidataSRDIVAEF 253
Cdd:PRK05975 165 ADRLASWRAPLLRHRDRLE--ALRADVFPLQFGGAAGTLEKLGGkaaavrARLAKRLGLEDApQWHS-----QRDFIADF 237
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490223448 254 SFIAAMI-------GVDISRLSE---EIIIwntqefafvtlddAYSTGSSIMPQKKNPDIAE----LARGKAGRLIG 316
Cdd:PRK05975 238 AHLLSLVtgslgkfGQDIALMAQagdEISL-------------SGGGGSSAMPHKQNPVAAEtlvtLARFNATQVSG 301
|
|
| |
