|
Name |
Accession |
Description |
Interval |
E-value |
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
14-449 |
1.34e-179 |
|
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: 509.94 E-value: 1.34e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 14 LAGRYASTELATLWSPEQKVKLERQLWLAVLRAQKDLGIEVPDAALADYERVLDTVDLASIAEREKVTRHDVKARIEEFN 93
Cdd:cd03302 1 LASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLDISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 94 DLAG--HEHVHKGMTSRDLTENVEQLQIRLSLELVRDRTVAVLARLGKLSGEYGELVMAGRSHNVAAQATTLGKRFATAT 171
Cdd:cd03302 81 LLCPaaAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 172 DELLVAYGRVEELLGRYPLRGIKGPVGTAQDMLDLLGGDAGKLADLEQRIATHLGFSQAFTSVGQVYPRSLDYEVVTALV 251
Cdd:cd03302 161 QDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVYPVTGQTYSRKVDIDVLNALS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 252 QLAAAPSSLAKTIRLMAGHELVTEGFKPGQVGSSAMPHKMNTRSCERVNGLMVILRGYASMTGELAGDQWNEGDVSCSVV 331
Cdd:cd03302 241 SLGATAHKIATDIRLLANLKEVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDSAN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 332 RRVALPDAFFALDGLLETFLTVLDEFGAFPAVVARELDRYLPFLATTKVLMGAVRAGVGRELAHEAIKENAVASALAMRE 411
Cdd:cd03302 321 RRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERIRVLSHQAAAVVKQ 400
|
410 420 430
....*....|....*....|....*....|....*...
gi 2747622691 412 QGAErNELLDKLAADARIPLDRDQLDALMaDKLSFTGA 449
Cdd:cd03302 401 EGGD-NDLIERIKNDAYFKPIWDELDALL-DPKTFIGR 436
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
14-454 |
6.81e-158 |
|
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: 454.88 E-value: 6.81e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 14 LAGRYASTELATLWSPEQKVKLERQLWLAVLRAQKDLGIEVPDAALADYERV-LDTVDLASIAEREKVTRHDVKARIEEF 92
Cdd:TIGR00928 1 LDERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGVIPAEAVKEIREKAnFTEVDLERIKEIEAVTRHDVKAVVYAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 93 ND--LAGHEHVHKGMTSRDLTENVEQLQIRLSLELVRDRTVAVLARLGKLSGEYGELVMAGRSHNVAAQATTLGKRFATA 170
Cdd:TIGR00928 81 KEkcGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 171 TDELLVAYGRVEELLGRYPLRGIKGPVGTAQDMLDLLggdagklADLEQRIATHLGFSQAFTSVgQVYPRSLDYEVVTAL 250
Cdd:TIGR00928 161 AEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPLV-------EEVEERVTEFLGLKPVPIST-QIEPRDRHAELLDAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 251 VQLAAAPSSLAKTIRLMAG--HELVTEGFKPGQVGSSAMPHKMNTRSCERVNGLMVILRGYASMTGELAGdQWNEGDVSC 328
Cdd:TIGR00928 233 ALLATTLEKFAVDIRLLQRteHFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENAP-LWHERDLTD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 329 SVVRRVALPDAFFALDGLLETFLTVLDEFGAFPAVVARELDRYLPFLATTKVLMGAVRAGVGRELAHEAIKENAVASALa 408
Cdd:TIGR00928 312 SSVERVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAAE- 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2747622691 409 mreqgAERNELLDKLAADARIPLDRDQLD-ALMADKLSFTGAAGDQV 454
Cdd:TIGR00928 391 -----VDEPDLLEFLLEDERITKYLKEEElAELLDPETYIGNAGEIV 432
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
14-457 |
2.61e-140 |
|
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: 409.86 E-value: 2.61e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 14 LAGRYASTELATLWSPEQKVKLERQLWLAVLRAQKDLGIeVPDAALADYERVLDT--VDLASIAEREKVTRHDVKARIEE 91
Cdd:COG0015 2 ISPRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGL-IPAEAAAAIRAAADDfeIDAERIKEIEKETRHDVKAFVYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 92 FNDLAG---HEHVHKGMTSRDLTENVEQLQIRLSLELVRDRTVAVLARLGKLSGEYGELVMAGRSHNVAAQATTLGKRFA 168
Cdd:COG0015 81 LKEKVGaeaGEYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 169 TATDELLVAYGRVEELLGRYPLRGIKGPVGTAQDMLDLlggdagkLADLEQRIATHLGFsQAFTSVGQVYPRSLDYEVVT 248
Cdd:COG0015 161 VWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGEA-------WPEVEERVAEKLGL-KPNPVTTQIEPRDRHAELFS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 249 ALVQLAAAPSSLAKTIRLMAGHEL--VTEGFKPGQVGSSAMPHKMNTRSCERVNGLMVILRGYAsMTGELAGDQWNEGDV 326
Cdd:COG0015 233 ALALIAGSLEKIARDIRLLQRTEVgeVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALA-AALLEALASWHERDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 327 SCSVVRRVALPDAFFALDGLLETFLTVLDEFGAFPAVVARELDRYLPFLATTKVLMGAVRAGVGRELAHEAIKENAvasa 406
Cdd:COG0015 312 SDSSVERNILPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELA---- 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2747622691 407 lamREQGAERNELLDKLAADARIP--LDRDQLDALMaDKLSFTGAAGDQVAAV 457
Cdd:COG0015 388 ---RGAWEEGNDLRELLAADPEIPaeLSKEELEALF-DPANYLGAADEIVDRV 436
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
249-448 |
8.04e-73 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 229.14 E-value: 8.04e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 249 ALVQLAAAPSSLAKTIRLMAGHE--LVTEGFKPGQVGSSAMPHKMNTRSCERVNGLMVILRGYASMTGELAgDQWNEGDV 326
Cdd:PRK08937 22 VLALIATSLEKFANEIRLLQRSEirEVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENV-PLWHERDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 327 SCSVVRRVALPDAFFALDGLLETFLTVLDEFGAFPAVVARELDRYLPFLATTKVLMGAVRAGVGRELAHEAIKENAVASA 406
Cdd:PRK08937 101 SHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIREKAMEAW 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2747622691 407 LAMreqgaerNELLDKLAADARI--PLDRDQLDALMaDKLSFTG 448
Cdd:PRK08937 181 KNQ-------KDLRELLEADERFtkQLTKEELDELF-DPEAFVG 216
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
25-301 |
1.27e-16 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 80.49 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 25 TLWSPEQK-VKLERQLWLAVL-RAQKDLGIEVPDAAlADYERVLDTV-------DLASIAEREKVTRHDVKARIEEF--- 92
Cdd:pfam00206 15 TDRSRFNFrLGEEDIKGLAALkKAAAKANVILKEEA-AAIIKALDEVaeegkldDQFPLKVWQEGSGTAVNMNLNEVige 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 93 ---NDLAGHEHVHKGMTSRDltenveQLQIRLSLELVRDRTVAVLARLGKL-------SGEYGELVMAGRSHNVAAQATT 162
Cdd:pfam00206 94 llgQLVHPNDHVHTGQSSND------QVPTALRLALKDALSEVLLPALRQLidalkekAKEFADIVKPGRTHLQDATPVT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 163 LGKRFATATDELLVAYGRVEELLGRYplrgIKGPVGTAQDMLDLLGGDAGkladLEQRIATHLGFsqaFTSVGQVYPRSL 242
Cdd:pfam00206 168 LGQELSGYAVALTRDRERLQQLLPRL----LVLPLGGGTAVGTGLNADPE----FAELVAKELGF---FTGLPVKAPNSF 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2747622691 243 DY--------EVVTALVQLAAAPSSLAKTIRLMAGHE--LVTEGFKPGQVGSSAMPHKMNTRSCERVNG 301
Cdd:pfam00206 237 EAtsdrdavvELSGALALLATSLSKFAEDLRLLSSGPagLVELSLAEGEPGSSIMPGKVNPDQLELLTG 305
|
|
| ADSL_C |
smart00998 |
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ... |
372-458 |
1.33e-12 |
|
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis of purine nucleotides: the conversion of succinylaminoimidazole-carboxamide ribotide into aminoimidazole-carboxamide ribotide (the fifth step of de novo IMP biosynthesis); the formation of adenosine monophosphate (AMP) from adenylosuccinate (the final step in the synthesis of AMP from IMP). This entry represents the C-terminal, seven alpha-helical, domain of adenylosuccinate lyase.
Pssm-ID: 198066 [Multi-domain] Cd Length: 81 Bit Score: 63.24 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 372 LPFLATTKVLMGAVRAGVGRELAHEAIKENAVASAlamreqgAERNELLDKLAADARIP--LDRDQLDALMaDKLSFTGA 449
Cdd:smart00998 1 GGLIFSERVLLALVEKGLGREEAYELVQRAAMKAW-------EEGKDLRELLLADPEVTayLSEEELEELF-DPEYYLGH 72
|
....*....
gi 2747622691 450 AGDQVAAVV 458
Cdd:smart00998 73 ADAIVDRVL 81
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
14-449 |
1.34e-179 |
|
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: 509.94 E-value: 1.34e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 14 LAGRYASTELATLWSPEQKVKLERQLWLAVLRAQKDLGIEVPDAALADYERVLDTVDLASIAEREKVTRHDVKARIEEFN 93
Cdd:cd03302 1 LASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLDISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 94 DLAG--HEHVHKGMTSRDLTENVEQLQIRLSLELVRDRTVAVLARLGKLSGEYGELVMAGRSHNVAAQATTLGKRFATAT 171
Cdd:cd03302 81 LLCPaaAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 172 DELLVAYGRVEELLGRYPLRGIKGPVGTAQDMLDLLGGDAGKLADLEQRIATHLGFSQAFTSVGQVYPRSLDYEVVTALV 251
Cdd:cd03302 161 QDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVYPVTGQTYSRKVDIDVLNALS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 252 QLAAAPSSLAKTIRLMAGHELVTEGFKPGQVGSSAMPHKMNTRSCERVNGLMVILRGYASMTGELAGDQWNEGDVSCSVV 331
Cdd:cd03302 241 SLGATAHKIATDIRLLANLKEVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDSAN 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 332 RRVALPDAFFALDGLLETFLTVLDEFGAFPAVVARELDRYLPFLATTKVLMGAVRAGVGRELAHEAIKENAVASALAMRE 411
Cdd:cd03302 321 RRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERIRVLSHQAAAVVKQ 400
|
410 420 430
....*....|....*....|....*....|....*...
gi 2747622691 412 QGAErNELLDKLAADARIPLDRDQLDALMaDKLSFTGA 449
Cdd:cd03302 401 EGGD-NDLIERIKNDAYFKPIWDELDALL-DPKTFIGR 436
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
14-454 |
6.81e-158 |
|
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: 454.88 E-value: 6.81e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 14 LAGRYASTELATLWSPEQKVKLERQLWLAVLRAQKDLGIEVPDAALADYERV-LDTVDLASIAEREKVTRHDVKARIEEF 92
Cdd:TIGR00928 1 LDERYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGVIPAEAVKEIREKAnFTEVDLERIKEIEAVTRHDVKAVVYAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 93 ND--LAGHEHVHKGMTSRDLTENVEQLQIRLSLELVRDRTVAVLARLGKLSGEYGELVMAGRSHNVAAQATTLGKRFATA 170
Cdd:TIGR00928 81 KEkcGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 171 TDELLVAYGRVEELLGRYPLRGIKGPVGTAQDMLDLLggdagklADLEQRIATHLGFSQAFTSVgQVYPRSLDYEVVTAL 250
Cdd:TIGR00928 161 AEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPLV-------EEVEERVTEFLGLKPVPIST-QIEPRDRHAELLDAL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 251 VQLAAAPSSLAKTIRLMAG--HELVTEGFKPGQVGSSAMPHKMNTRSCERVNGLMVILRGYASMTGELAGdQWNEGDVSC 328
Cdd:TIGR00928 233 ALLATTLEKFAVDIRLLQRteHFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENAP-LWHERDLTD 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 329 SVVRRVALPDAFFALDGLLETFLTVLDEFGAFPAVVARELDRYLPFLATTKVLMGAVRAGVGRELAHEAIKENAVASALa 408
Cdd:TIGR00928 312 SSVERVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAAE- 390
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2747622691 409 mreqgAERNELLDKLAADARIPLDRDQLD-ALMADKLSFTGAAGDQV 454
Cdd:TIGR00928 391 -----VDEPDLLEFLLEDERITKYLKEEElAELLDPETYIGNAGEIV 432
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
14-457 |
2.61e-140 |
|
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: 409.86 E-value: 2.61e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 14 LAGRYASTELATLWSPEQKVKLERQLWLAVLRAQKDLGIeVPDAALADYERVLDT--VDLASIAEREKVTRHDVKARIEE 91
Cdd:COG0015 2 ISPRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGL-IPAEAAAAIRAAADDfeIDAERIKEIEKETRHDVKAFVYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 92 FNDLAG---HEHVHKGMTSRDLTENVEQLQIRLSLELVRDRTVAVLARLGKLSGEYGELVMAGRSHNVAAQATTLGKRFA 168
Cdd:COG0015 81 LKEKVGaeaGEYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 169 TATDELLVAYGRVEELLGRYPLRGIKGPVGTAQDMLDLlggdagkLADLEQRIATHLGFsQAFTSVGQVYPRSLDYEVVT 248
Cdd:COG0015 161 VWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGEA-------WPEVEERVAEKLGL-KPNPVTTQIEPRDRHAELFS 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 249 ALVQLAAAPSSLAKTIRLMAGHEL--VTEGFKPGQVGSSAMPHKMNTRSCERVNGLMVILRGYAsMTGELAGDQWNEGDV 326
Cdd:COG0015 233 ALALIAGSLEKIARDIRLLQRTEVgeVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALA-AALLEALASWHERDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 327 SCSVVRRVALPDAFFALDGLLETFLTVLDEFGAFPAVVARELDRYLPFLATTKVLMGAVRAGVGRELAHEAIKENAvasa 406
Cdd:COG0015 312 SDSSVERNILPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELA---- 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2747622691 407 lamREQGAERNELLDKLAADARIP--LDRDQLDALMaDKLSFTGAAGDQVAAV 457
Cdd:COG0015 388 ---RGAWEEGNDLRELLAADPEIPaeLSKEELEALF-DPANYLGAADEIVDRV 436
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
23-400 |
1.99e-102 |
|
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: 311.36 E-value: 1.99e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 23 LATLWSPEQKVKLERQLWLAVLRAQKDLGIeVPDAALADYERVLDT--VDLASIAEREKVTRHDVKARIEEFNDLAG--- 97
Cdd:cd01595 1 MRAIFSEENKLRTWLDVEAALAEAQAELGL-IPKEAAEEIRAAADVfeIDAERIAEIEKETGHDVIAFVYALAEKCGeda 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 98 HEHVHKGMTSRDLTENVEQLQIRLSLELVRDRTVAVLARLGKLSGEYGELVMAGRSHNVAAQATTLGKRFATATDELLVA 177
Cdd:cd01595 80 GEYVHFGATSQDINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 178 YGRVEELLGRYPLRGIKGPVGTAQDMLDllggdagKLADLEQRIATHLGFSqAFTSVGQVYPRSLDYEVVTALVQLAAAP 257
Cdd:cd01595 160 LERLEEARERVLVGGISGAVGTHASLGP-------KGPEVEERVAEKLGLK-VPPITTQIEPRDRIAELLSALALIAGTL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 258 SSLAKTIRLMAGHEL--VTEGFKPGQVGSSAMPHKMNTRSCERVNGLMVILRGYASMTGElAGDQWNEGDVSCSVVRRVA 335
Cdd:cd01595 232 EKIATDIRLLQRTEIgeVEEPFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALE-NLVQWHERDLSDSSVERNI 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2747622691 336 LPDAFFALDGLLETFLTVLDEFGAFPAVVARELDRYLPFLATTKVLMGAVRAGVGRELAHEAIKE 400
Cdd:cd01595 311 LPDAFLLLDAALSRLQGLLEGLVVNPERMRRNLDLTWGLILSEAVMMALAKKGLGRQEAYELVKE 375
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
249-448 |
8.04e-73 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 229.14 E-value: 8.04e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 249 ALVQLAAAPSSLAKTIRLMAGHE--LVTEGFKPGQVGSSAMPHKMNTRSCERVNGLMVILRGYASMTGELAgDQWNEGDV 326
Cdd:PRK08937 22 VLALIATSLEKFANEIRLLQRSEirEVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENV-PLWHERDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 327 SCSVVRRVALPDAFFALDGLLETFLTVLDEFGAFPAVVARELDRYLPFLATTKVLMGAVRAGVGRELAHEAIKENAVASA 406
Cdd:PRK08937 101 SHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIREKAMEAW 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2747622691 407 LAMreqgaerNELLDKLAADARI--PLDRDQLDALMaDKLSFTG 448
Cdd:PRK08937 181 KNQ-------KDLRELLEADERFtkQLTKEELDELF-DPEAFVG 216
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
17-401 |
1.68e-63 |
|
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: 210.87 E-value: 1.68e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 17 RYASTELATLWSPEQKVKLERQLWLAVLRAQKDLGIeVPDAALADYERVLDTvDLASIAEREKVTRHDVKARIEEFNDLA 96
Cdd:cd01360 1 RYGRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLGV-IPAEAAEEIRKKAKF-DVERVKEIEAETKHDVIAFVTAIAEYC 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 97 GHE--HVHKGMTSRDLTENVEQLQIRLSLELVRDRTVAVLARLGKLSGEYGELVMAGRSHNVAAQATTLGKRFATATDEL 174
Cdd:cd01360 79 GEAgrYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 175 LVAYGRVEELLGRYPLRGIKGPVGTAQDmLDLlggdagklaDLEQRIATHLGFSQAFTSVgQVYPRSLDYEVVTALVQLA 254
Cdd:cd01360 159 KRHLERLKEARERILVGKISGAVGTYAN-LGP---------EVEERVAEKLGLKPEPIST-QVIQRDRHAEYLSTLALIA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 255 AAPSSLAKTIRLMAGHEL--VTEGFKPGQVGSSAMPHKMNTRSCERVNGLMVILRGYASMTGElAGDQWNEGDVSCSVVR 332
Cdd:cd01360 228 STLEKIATEIRHLQRTEVleVEEPFSKGQKGSSAMPHKRNPILSENICGLARVIRSNVIPALE-NVALWHERDISHSSVE 306
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2747622691 333 RVALPDAFFALDGLLETFLTVLDEFGAFPAVVARELDRYLPFLATTKVLMGAVRAGVGRELAHEAIKEN 401
Cdd:cd01360 307 RVILPDATILLDYILRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALVEKGMSREEAYEIVQRE 375
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
37-355 |
2.51e-51 |
|
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: 176.92 E-value: 2.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 37 RQLWLAVLRAQKDLGIeVPDAALADYERVLDTVD---LASIAEREKVTRHDVKARIEEFNDLAGH---EHVHKGMTSRDL 110
Cdd:cd01334 5 LQVEKAHAKALAELGL-LPKEAAEAILAALDEILegiAADQVEQEGSGTHDVMAVEEVLAERAGElngGYVHTGRSSNDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 111 TENVEQLQIRLSLELVRDRTVAVLARLGKLSGEYGELVMAGRSHNVAAQATTLGKRFATATDELLVAYGRVEELLGRYPL 190
Cdd:cd01334 84 VDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKRLNV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 191 RGIKGpvgTAqdmldlLGGDAGKLADLEQRIATHLGFSQAFT-SVGQVYPRSLDYEVVTALVQLAAAPSSLAKTIRLMAG 269
Cdd:cd01334 164 LPLGG---GA------VGTGANAPPIDRERVAELLGFFGPAPnSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSS 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 270 HEL--VTEGFKPgQVGSSAMPHKMNTRSCERVNGLMVILRGYAsMTGELAGDQWNEGDVSCSVVRRVALPDAFFALDGLL 347
Cdd:cd01334 235 GEFgeVELPDAK-QPGSSIMPQKVNPVILELVRGLAGRVIGNL-AALLEALKGGPLEDNVDSPVEREALPDSFDLLDAAL 312
|
....*...
gi 2747622691 348 ETFLTVLD 355
Cdd:cd01334 313 RLLTGVLE 320
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
13-460 |
6.63e-46 |
|
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: 165.49 E-value: 6.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 13 VLAGRYASTELATLWSPEQKVklerQLWLAVL----RAQKDLGIeVPDAALADYERVLDT--VDLASIAEREKVTRHD-- 84
Cdd:cd01597 1 LLGDLFGTPAMREIFSDENRV----QAMLDVEaalaRAQAELGV-IPKEAAAEIAAAADVerLDLEALAEATARTGHPai 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 85 --VKARIEEFNDLAGhEHVHKGMTSRDLTENVEQLQIRLSLELVRDRTVAVLARLGKLSGEYGELVMAGRSHNVAAQATT 162
Cdd:cd01597 76 plVKQLTAACGDAAG-EYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPIT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 163 LGKRFATATDELLVAYGRVEELLGRYPLRGIKGPVGTaqdmLDLLGGDAgklADLEQRIATHLGFSQA----FTSvgqvy 238
Cdd:cd01597 155 FGLKVAVWLSELLRHRERLDELRPRVLVVQFGGAAGT----LASLGDQG---LAVQEALAAELGLGVPaipwHTA----- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 239 pRSLDYEVVTALVQLAAAPSSLAKTIRLMAGHEL--VTEGFKPGQVGSSAMPHKMNTRSCERVNGLMVILRGYASmTGEL 316
Cdd:cd01597 223 -RDRIAELASFLALLTGTLGKIARDVYLLMQTEIgeVAEPFAKGRGGSSTMPHKRNPVGCELIVALARRVPGLAA-LLLD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 317 AGDQWNEGDVSCSVVRRVALPDAFFALDGLLETFLTVLDEFGAFPAVVARELDRYLPFLATTKVLMgAVRAGVGRELAHE 396
Cdd:cd01597 301 AMVQEHERDAGAWHAEWIALPEIFLLASGALEQAEFLLSGLEVNEDRMRANLDLTGGLILSEAVMM-ALAPKLGRQEAHD 379
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2747622691 397 AIKEnavASALAMREQGaernELLDKLAADARI--PLDRDQLDALMaDKLSFTGAAGDQVAAVVAR 460
Cdd:cd01597 380 LVYE---ACMRAVEEGR----PLREVLLEDPEVaaYLSDEELDALL-DPANYLGSAPALVDRVLAR 437
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
89-351 |
4.81e-22 |
|
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: 94.60 E-value: 4.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 89 IEEFNDLAGHEH----VHKGMTSRDLTENVEQLQIRLSLELVRDRTVAVLARLGKLSGEYGELVMAGRSHNVAAQATTLG 164
Cdd:cd01594 21 AGRAGELAGGLHgsalVHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDAQPVTLG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 165 KRFATATDELLVAYGRVEELlgryplrgikgpvgtaqdmldllggdagkladleqRIAthlgfsqaftsvgqvyprsldy 244
Cdd:cd01594 101 YELRAWAQVLGRDLERLEEA-----------------------------------AVA---------------------- 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 245 EVVTALVQLAAAPSSLAKTIRLMAGHEL--VTEGFKPGQVGSSAMPHKMNTRSCERVNGLMVILRGyASMTGELAGDQWN 322
Cdd:cd01594 124 EALDALALAAAHLSKIAEDLRLLLSGEFgeLGEPFLPGQPGSSIMPQKVNPVAAELVRGLAGLVIG-NLVAVLTALKGGP 202
|
250 260
....*....|....*....|....*....
gi 2747622691 323 EGDVSCSVVRRVALPDAFFALDGLLETFL 351
Cdd:cd01594 203 ERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
25-301 |
1.27e-16 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 80.49 E-value: 1.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 25 TLWSPEQK-VKLERQLWLAVL-RAQKDLGIEVPDAAlADYERVLDTV-------DLASIAEREKVTRHDVKARIEEF--- 92
Cdd:pfam00206 15 TDRSRFNFrLGEEDIKGLAALkKAAAKANVILKEEA-AAIIKALDEVaeegkldDQFPLKVWQEGSGTAVNMNLNEVige 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 93 ---NDLAGHEHVHKGMTSRDltenveQLQIRLSLELVRDRTVAVLARLGKL-------SGEYGELVMAGRSHNVAAQATT 162
Cdd:pfam00206 94 llgQLVHPNDHVHTGQSSND------QVPTALRLALKDALSEVLLPALRQLidalkekAKEFADIVKPGRTHLQDATPVT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 163 LGKRFATATDELLVAYGRVEELLGRYplrgIKGPVGTAQDMLDLLGGDAGkladLEQRIATHLGFsqaFTSVGQVYPRSL 242
Cdd:pfam00206 168 LGQELSGYAVALTRDRERLQQLLPRL----LVLPLGGGTAVGTGLNADPE----FAELVAKELGF---FTGLPVKAPNSF 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2747622691 243 DY--------EVVTALVQLAAAPSSLAKTIRLMAGHE--LVTEGFKPGQVGSSAMPHKMNTRSCERVNG 301
Cdd:pfam00206 237 EAtsdrdavvELSGALALLATSLSKFAEDLRLLSSGPagLVELSLAEGEPGSSIMPGKVNPDQLELLTG 305
|
|
| protocat_pcaB |
TIGR02426 |
3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis, ... |
14-321 |
4.54e-14 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Members of this family are 3-carboxy-cis,cis-muconate cycloisomerase, the enzyme the catalyzes the second step in the protocatechuate degradation to beta-ketoadipate and then to succinyl-CoA and acetyl-CoA. 4-hydroxybenzoate, 3-hydroxybenzoate, and vanillate all can be converted in one step to protocatechuate. All members of the seed alignment for this model were chosen from within protocatechuate degradation operons of at least three genes of the pathway, from genomes with the complete pathway through beta-ketoadipate. [Energy metabolism, Other]
Pssm-ID: 274128 [Multi-domain] Cd Length: 338 Bit Score: 73.24 E-value: 4.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 14 LAGRYAST-ELATLWSPEQKVKLERQLWLAVLRAQKDLGIeVPDAALADYERVLDTV--DLASIAERekvTRHD------ 84
Cdd:TIGR02426 1 LLDGLFGDpAALELFSDRAFLRAMLDFEAALARAQADAGL-IPAEAAAAIEAACAAAapDLEALAHA---AATAgnpvip 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 85 -VKARIEEFNDLAGhEHVHKGMTSRDLTENVEQLQIRLSLELVRDRTVAVLARLGKLSGEYGELVMAGRSHNVAAQATTL 163
Cdd:TIGR02426 77 lVKALRKAVAGEAA-RYVHRGATSQDVIDTSLMLQLRDALDLLLADLGRLADALADLAARHRDTPMTGRTLLQQAVPTTF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 164 GKRFATATDELLVAYGRVEELLGRYPLRGIKGPVGTaqdmLDLLGGDAGKLAD-LEQRIATHLGFSQAFTSvgqvypRSL 242
Cdd:TIGR02426 156 GLKAAGWLAAVLRARDRLAALRTRALPLQFGGAAGT----LAALGTRGGAVAAaLAARLGLPLPALPWHTQ------RDR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 243 DYEVVTALVQLAAAPSSLAKTIRLMAGHElVTEGFKPGQVGSSAMPHKMNTRSCE-------RVNGLMVILRGYASMTGE 315
Cdd:TIGR02426 226 IAEFGSALALVAGALGKIAGDIALLSQTE-VGEVFEAGGGGSSAMPHKRNPVGAAllaaaarRVPGLAATLHAALPQEHE 304
|
....*.
gi 2747622691 316 LAGDQW 321
Cdd:TIGR02426 305 RSLGGW 310
|
|
| ADSL_C |
smart00998 |
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ... |
372-458 |
1.33e-12 |
|
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis of purine nucleotides: the conversion of succinylaminoimidazole-carboxamide ribotide into aminoimidazole-carboxamide ribotide (the fifth step of de novo IMP biosynthesis); the formation of adenosine monophosphate (AMP) from adenylosuccinate (the final step in the synthesis of AMP from IMP). This entry represents the C-terminal, seven alpha-helical, domain of adenylosuccinate lyase.
Pssm-ID: 198066 [Multi-domain] Cd Length: 81 Bit Score: 63.24 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 372 LPFLATTKVLMGAVRAGVGRELAHEAIKENAVASAlamreqgAERNELLDKLAADARIP--LDRDQLDALMaDKLSFTGA 449
Cdd:smart00998 1 GGLIFSERVLLALVEKGLGREEAYELVQRAAMKAW-------EEGKDLRELLLADPEVTayLSEEELEELF-DPEYYLGH 72
|
....*....
gi 2747622691 450 AGDQVAAVV 458
Cdd:smart00998 73 ADAIVDRVL 81
|
|
| ADSL_C |
pfam10397 |
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ... |
373-457 |
3.32e-12 |
|
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure whose full length represents the enzyme adenylosuccinate lyase. This sequence lies C-terminal to the conserved motif necessary for beta-elimination reactions, Adenylosuccinate lyase catalyzes two steps in the synthesis of purine nucleotides: the conversion of succinylaminoimidazole-carboxamide ribotide into aminoimidazole-carboxamide ribotide, the eighth step of the de novo pathway, and the formation of adenosine monophosphate (AMP) from adenylosuccinate, the second step in the conversion of inosine monophosphate into AMP.
Pssm-ID: 463073 [Multi-domain] Cd Length: 78 Bit Score: 62.05 E-value: 3.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 373 PFLATTKVLMGAVRaGVGRELAHEAIKENAVASALAMreqgaeRNELLDKLAADARIP-LDRDQLDALMaDKLSFTGAAG 451
Cdd:pfam10397 1 GLIFSERVLLALVK-GLGREEAHELVQEAAMKAWEEG------KNDLRELLAADPEVTyLSEEELDALF-DPAYYLGRAD 72
|
....*.
gi 2747622691 452 DQVAAV 457
Cdd:pfam10397 73 EIVDRV 78
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
70-292 |
2.52e-11 |
|
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the product of the purB gene in Escherichia coli, and related proteins. It is a member of the Lyase class I family of the Lyase_I superfamily. Members of the Lyase class I family function as homotetramers to catalyze similar beta-elimination reactions in which a Calpha-N or Calpha-O bond is cleaved with the subsequent release of fumarate as one of the products. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two non-sequential steps in the de novo purine biosynthesis pathway: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylosuccinate (SAMP) into adenosine monophosphate (AMP).
Pssm-ID: 176470 [Multi-domain] Cd Length: 425 Bit Score: 65.33 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 70 DLASIAEREKVTRHDVKA-------RIEEFNDLAG-HEHVHKGMTSRDltenVEQLQIRLSLELVRDRTV-----AVLAR 136
Cdd:cd01598 56 DALRIKEIEATTNHDVKAveyflkeKFETLGLLKKiKEFIHFACTSED----INNLAYALMIKEARNEVIlpllkEIIDS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 137 LGKLSGEYGELVMAGRSHNVAAQATTLGKRFATATDELLVAYGRVE--ELLGRyplrgIKGPVGTAqdmldllggDAGKL 214
Cdd:cd01598 132 LKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLKqiEILGK-----FNGAVGNF---------NAHLV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 215 AD-------LEQRIATHLGFS-QAFTSvgQVYPRslDY--EVVTALVQLAAAPSSLAKTIRLMAGHELVTEGFKPGQVGS 284
Cdd:cd01598 198 AYpdvdwrkFSEFFVTSLGLTwNPYTT--QIEPH--DYiaELFDALARINTILIDLCRDIWGYISLGYFKQKVKKGEVGS 273
|
....*...
gi 2747622691 285 SAMPHKMN 292
Cdd:cd01598 274 STMPHKVN 281
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
16-292 |
5.07e-11 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 64.39 E-value: 5.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 16 GRYAS--TELATLWSpEQ-------KVKLErqlWLAVLRAQKDLGiEVP---DAALAD----YERvLDTVDLASIAEREK 79
Cdd:PRK09285 14 GRYASktAALRPIFS-EFgliryrvQVEVE---WLIALAAHPGIP-EVPpfsAEANAFlraiVEN-FSEEDAARIKEIER 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 80 VTRHDVKA-------RIEEFNDL-AGHEHVHKGMTSrdltENVEQLQIRLSLELVRDRTV-----AVLARLGKLSGEYGE 146
Cdd:PRK09285 88 TTNHDVKAveyflkeKLAGLPELeAVSEFIHFACTS----EDINNLSHALMLKEAREEVLlpalrELIDALKELAHEYAD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 147 LVMAGRSHNVAAQATTLGKRFATATDELLVAYGRVE--ELLGRyplrgIKGPVGTaqdmldllggdagkladleqrIATH 224
Cdd:PRK09285 164 VPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLEavEILGK-----INGAVGN---------------------YNAH 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 225 L---------GFSQAF-TSVG--------QVYPRslDY--EVVTALvqlaaapsSLAKTI-----RLMAGHelVTEGF-- 277
Cdd:PRK09285 218 LaaypevdwhAFSREFvESLGltwnpyttQIEPH--DYiaELFDAV--------ARFNTIlidldRDVWGY--ISLGYfk 285
|
330
....*....|....*...
gi 2747622691 278 ---KPGQVGSSAMPHKMN 292
Cdd:PRK09285 286 qktKAGEIGSSTMPHKVN 303
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
12-459 |
5.90e-11 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 64.27 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 12 NVLAGRYASTE-LATLWSPEQKVKLERQLWLAVLRAQKDLGIeVPDAALADYERVLD--TVDLASIAERE---------- 78
Cdd:PRK09053 5 ARLTDLYFGSPaMRAIFSDRATVQRMLDFEAALARAEAACGV-IPAAAVAPIEAACDaeRLDLDALAQAAalagnlaipl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 79 -KVTRHDVKARieefnDLAGHEHVHKGMTSRDLTENVEQLQIRLSLELVRDRTVAVLARLGKLSGEYGELVMAGRSHNVA 157
Cdd:PRK09053 84 vKQLTAQVAAR-----DAEAARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 158 AQATTLGKRFATATDELLVAYGRVEELLGRYPLRGIKGPVGTaqdmLDLLGGDAGKLAdleQRIATHLGFsqAFTSVGQV 237
Cdd:PRK09053 159 ALPVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGGAAGT----LASLGEQALPVA---QALAAELQL--ALPALPWH 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 238 YPRSLDYEVVTALVQLAAAPSSLAKTIRLMAGHElVTEGFKP---GQVGSSAMPHKMNTRSCE-------RVNGLMVILr 307
Cdd:PRK09053 230 TQRDRIAEFASALGLLAGTLGKIARDVSLLMQTE-VGEVFEPaaaGKGGSSTMPHKRNPVGCAavltaatRAPGLVATL- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 308 gYASMTG--ELAGDQWN-EGDvscsvvrrvALPDAFFALDGLLETFLTVLDEFGAFPAVVARELDrylpflATTKVLMG- 383
Cdd:PRK09053 308 -FAAMPQehERALGGWHaEWD---------TLPELACLAAGALAQMAQIVEGLEVDAARMRANLD------LTHGLILAe 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 384 ----AVRAGVGRELAHEAIKEnavASALAMREQgaerNELLDKLAADARIP--LDRDQLDALMaDKLSFTGAAGDQVAAV 457
Cdd:PRK09053 372 avmlALADRIGRLDAHHLVEQ---ASKRAVAEG----RHLRDVLAEDPQVSahLSPAALDRLL-DPAHYLGQAHAWVDRV 443
|
..
gi 2747622691 458 VA 459
Cdd:PRK09053 444 LA 445
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
14-292 |
3.39e-09 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 58.53 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 14 LAGRYASTELATLWSPEQKVKLERQLWLAVLRAQKDLGIEVPDAALADYERVLD-TVDLASIAEREKVTRHDVKARIEEF 92
Cdd:PRK05975 11 LSGLFGDDEIAALFSAEADIAAMLAFEAALAEAEAEHGIIPAEAAERIAAACETfEPDLAALRHATARDGVVVPALVRQL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 93 NDLAGHE---HVHKGMTSRDLTENVEQLQIRLSLELVRDRTVAVLARLGKLSGEYGELVMAGRSHNVAAQATTLGKRFAT 169
Cdd:PRK05975 91 RAAVGEEaaaHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLAS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 170 ATDELLVAYGRVEELLGRYPLRGIKGPVGTaqdmLDLLGGDAGKLADleqRIATHLGFSQAFTSVGQVYPrsldyeVVTA 249
Cdd:PRK05975 171 WRAPLLRHRDRLEALRADVFPLQFGGAAGT----LEKLGGKAAAVRA---RLAKRLGLEDAPQWHSQRDF------IADF 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2747622691 250 LVQLAAAPSSLAK---TIRLMAghELVTEGFKPGQVGSSAMPHKMN 292
Cdd:PRK05975 238 AHLLSLVTGSLGKfgqDIALMA--QAGDEISLSGGGGSSAMPHKQN 281
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
14-292 |
1.07e-08 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 57.06 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 14 LAGRYAS--TELATLWSP----EQKVKLERQlWLAVLRAQKDLgIEVP---DAALADYERVLD---TVDLASIAEREKVT 81
Cdd:PLN02848 15 LDGRYWSkvKDLRPIFSEfgliRYRVLVEVK-WLLKLSQIPEV-TEVPpfsDEANSFLEGIIAgfsVDDALEVKKIERVT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 82 RHDVKA-------RIEEFNDLAG-HEHVHKGMTSRDLTENVEQLQIRLSLELV----RDRTVAVLARLGKlsgEYGELVM 149
Cdd:PLN02848 93 NHDVKAveyflkqKCKSHPELAKvLEFFHFACTSEDINNLSHALMLKEGVNSVvlptMDEIIKAISSLAH---EFAYVPM 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2747622691 150 AGRSHNVAAQATTLGKRFATatdellVAYgRVEEL---LGRYPLRG-IKGPVGTAQ-DMLDLLGGDAGKLAdleQRIATH 224
Cdd:PLN02848 170 LSRTHGQPASPTTLGKEMAN------FAY-RLSRQrkqLSEVKIKGkFAGAVGNYNaHMSAYPEVDWPAVA---EEFVTS 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2747622691 225 LGFSqaFTS-VGQVYPRSLDYEVVTALVQLAaapSSLAKTIRLMAGHelVTEGF-----KPGQVGSSAMPHKMN 292
Cdd:PLN02848 240 LGLT--FNPyVTQIEPHDYMAELFNAVSRFN---NILIDFDRDIWSY--ISLGYfkqitKAGEVGSSTMPHKVN 306
|
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