|
Name |
Accession |
Description |
Interval |
E-value |
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
13-454 |
2.07e-164 |
|
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: 470.72 E-value: 2.07e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 13 FTWRYGSPEMRKIFSEKHKVELWRKIWVALAEAQHQAGLVTKKELDDLKKNQNSF--NIEEIQKIEKETRHDVVAAIYEF 90
Cdd:COG0015 2 ISPRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGLIPAEAAAAIRAAADDFeiDAERIKEIEKETRHDVKAFVYAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 91 ASQAKIGGGK-IHLGATSMDIVDNADMMRIKEALEIIEKRLKIVLLNFAEKIKKYAHFPCIGYTHFQPAEPTTVGYRLAF 169
Cdd:COG0015 82 KEKVGAEAGEyIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 170 YGQDLLMAWEFIQFVKKIIKAKGVKGAVGTAASFKALlknsqikVDQLEKKVMESLGIEASLITTQVYPRQYDFILLTAL 249
Cdd:COG0015 162 WAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGEA-------WPEVEERVAEKLGLKPNPVTTQIEPRDRHAELFSAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 250 ALVGSSMAKFCGDLRILQSANFGEWSEPFGKKQVGSSAMPFKKNPITSENICSLARYLAALPQVALENATlSYLERTLDD 329
Cdd:COG0015 235 ALIAGSLEKIARDIRLLQRTEVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEALA-SWHERDLSD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 330 SANKRTIIPEGFLITDQILISSEKIITGLVVNEPRISYNLNQYAPFAASEAILIEAVKNGANRQELHETLRQISLLAWQE 409
Cdd:COG0015 314 SSVERNILPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAWEE 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1276893371 410 tqrgkPNPMNQLLLNNKNIANYLKKDQIKKLLDVRNHIGDAPERA 454
Cdd:COG0015 394 -----GNDLRELLAADPEIPAELSKEELEALFDPANYLGAADEIV 433
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
16-448 |
3.84e-151 |
|
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: 437.13 E-value: 3.84e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 16 RYGSPEMRKIFSEKHKVELWRKIWVALAEAQHQAGL-VTKKELDDLKKNQNSFNIEEIQKIEKETRHDVVAAIYEFASQA 94
Cdd:cd03302 4 RYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLdISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHAFGLLC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 95 KIGGGKIHLGATSMDIVDNADMMRIKEALEIIEKRLKIVLLNFAEKIKKYAHFPCIGYTHFQPAEPTTVGYRLAFYGQDL 174
Cdd:cd03302 84 PAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 175 LMAWEFIQFVKKIIKAKGVKGAVGTAASFKALLKNSQIKVDQLEKKVMESLGIEAS-LITTQVYPRQYDFILLTALALVG 253
Cdd:cd03302 164 LMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVyPVTGQTYSRKVDIDVLNALSSLG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 254 SSMAKFCGDLRILqsANFGEWSEPFGKKQVGSSAMPFKKNPITSENICSLARYLAALPQVALENATLSYLERTLDDSANK 333
Cdd:cd03302 244 ATAHKIATDIRLL--ANLKEVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDSANR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 334 RTIIPEGFLITDQILISSEKIITGLVVNEPRISYNLNQYAPFAASEAILIEAVKNGANRQELHETLRQISLLAWQE-TQR 412
Cdd:cd03302 322 RIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERIRVLSHQAAAVvKQE 401
|
410 420 430
....*....|....*....|....*....|....*.
gi 1276893371 413 GKPNPMNQLLLNNKNIAnyLKKDQIKKLLDVRNHIG 448
Cdd:cd03302 402 GGDNDLIERIKNDAYFK--PIWDELDALLDPKTFIG 435
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
16-457 |
5.69e-133 |
|
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: 390.94 E-value: 5.69e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 16 RYGSPEMRKIFSEKHKVELWRKIWVALAEAQHQAGLVTKKELDDLKKNQNS--FNIEEIQKIEKETRHDVVAAIYEFASQ 93
Cdd:TIGR00928 4 RYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGVIPAEAVKEIREKANFteVDLERIKEIEAVTRHDVKAVVYALKEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 94 AKIGGGKIHLGATSMDIVDNADMMRIKEALEIIEKRLKIVLLNFAEKIKKYAHFPCIGYTHFQPAEPTTVGYRLAFYGQD 173
Cdd:TIGR00928 84 CGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 174 LLMAWEFIQFVKKIIKAKGVKGAVGTAASFKALLKnsqikvdQLEKKVMESLGIEASLITTQVYPRQYDFILLTALALVG 253
Cdd:TIGR00928 164 MLRQLERLLQAKERIKVGGISGAVGTHAAAYPLVE-------EVEERVTEFLGLKPVPISTQIEPRDRHAELLDALALLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 254 SSMAKFCGDLRILQSANFGEWSEPFGKKQVGSSAMPFKKNPITSENICSLARYLAALPQVALENATLsYLERTLDDSANK 333
Cdd:TIGR00928 237 TTLEKFAVDIRLLQRTEHFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENAPL-WHERDLTDSSVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 334 RTIIPEGFLITDQILISSEKIITGLVVNEPRISYNLNQYAPFAASEAILIEAVKNGANRQELHETLRQISLLAWQETQRG 413
Cdd:TIGR00928 316 RVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAAEVDEPD 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1276893371 414 kpnpMNQLLLNNKNIANYLKKDQIKKLLDVRNHIGDAPERALKL 457
Cdd:TIGR00928 396 ----LLEFLLEDERITKYLKEEELAELLDPETYIGNAGEIVERV 435
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
248-448 |
2.11e-57 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 188.70 E-value: 2.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 248 ALALVGSSMAKFCGDLRILQSANFGEWSEPFGKKQVGSSAMPFKKNPITSENICSLARYLAALPQVALENATLsYLERTL 327
Cdd:PRK08937 22 VLALIATSLEKFANEIRLLQRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENVPL-WHERDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 328 DDSANKRTIIPEGFLITDQILISSEKIITGLVVNEPRISYNLNQYAPFAASEAILIEAVKNGANRQELHETLRQISLLAW 407
Cdd:PRK08937 101 SHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIREKAMEAW 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1276893371 408 QETqrgkpNPMNQLLLNNKNIANYLKKDQIKKLLDVRNHIG 448
Cdd:PRK08937 181 KNQ-----KDLRELLEADERFTKQLTKEELDELFDPEAFVG 216
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
16-300 |
8.74e-35 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 131.72 E-value: 8.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 16 RYG--SPEMRKIFSEKHKVELW-----RKIWVALAEAQHQAGLVTKKELDD----LKKNQNSFNIEEIQKIEKETRHDVV 84
Cdd:pfam00206 2 RFTvpADALMGIFTDRSRFNFRlgeedIKGLAALKKAAAKANVILKEEAAAiikaLDEVAEEGKLDDQFPLKVWQEGSGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 85 AA-------IYEFASQAKIGGGKIHLGATSMDIVDNAdmMRI--KEAL-EIIEKRLKIVLLNFAEKIKKYAHFPCIGYTH 154
Cdd:pfam00206 82 AVnmnlnevIGELLGQLVHPNDHVHTGQSSNDQVPTA--LRLalKDALsEVLLPALRQLIDALKEKAKEFADIVKPGRTH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 155 FQPAEPTTVGYRLAFYGQDLLMAWEFI-QFVKKIIKAK-GVKGAVGTAAsfkallkNSQIKVDQL---EKKVMESLGIEA 229
Cdd:pfam00206 160 LQDATPVTLGQELSGYAVALTRDRERLqQLLPRLLVLPlGGGTAVGTGL-------NADPEFAELvakELGFFTGLPVKA 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276893371 230 SLITTQVYPRqyDFI--LLTALALVGSSMAKFCGDLRILQSANFGEWSEPFGKKQVGSSAMPFKKNPITSENI 300
Cdd:pfam00206 233 PNSFEATSDR--DAVveLSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEPGSSIMPGKVNPDQLELL 303
|
|
| ADSL_C |
smart00998 |
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ... |
374-452 |
3.62e-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: 61.70 E-value: 3.62e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276893371 374 PFAASEAILIEAVKNGANRQELHETLRQISLLAWQEtqrGKpnPMNQLLLNNKNIANYLKKDQIKKLLDVRNHIGDAPE 452
Cdd:smart00998 2 GLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEE---GK--DLRELLLADPEVTAYLSEEELEELFDPEYYLGHADA 75
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
13-454 |
2.07e-164 |
|
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: 470.72 E-value: 2.07e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 13 FTWRYGSPEMRKIFSEKHKVELWRKIWVALAEAQHQAGLVTKKELDDLKKNQNSF--NIEEIQKIEKETRHDVVAAIYEF 90
Cdd:COG0015 2 ISPRYASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGLIPAEAAAAIRAAADDFeiDAERIKEIEKETRHDVKAFVYAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 91 ASQAKIGGGK-IHLGATSMDIVDNADMMRIKEALEIIEKRLKIVLLNFAEKIKKYAHFPCIGYTHFQPAEPTTVGYRLAF 169
Cdd:COG0015 82 KEKVGAEAGEyIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 170 YGQDLLMAWEFIQFVKKIIKAKGVKGAVGTAASFKALlknsqikVDQLEKKVMESLGIEASLITTQVYPRQYDFILLTAL 249
Cdd:COG0015 162 WAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGEA-------WPEVEERVAEKLGLKPNPVTTQIEPRDRHAELFSAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 250 ALVGSSMAKFCGDLRILQSANFGEWSEPFGKKQVGSSAMPFKKNPITSENICSLARYLAALPQVALENATlSYLERTLDD 329
Cdd:COG0015 235 ALIAGSLEKIARDIRLLQRTEVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEALA-SWHERDLSD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 330 SANKRTIIPEGFLITDQILISSEKIITGLVVNEPRISYNLNQYAPFAASEAILIEAVKNGANRQELHETLRQISLLAWQE 409
Cdd:COG0015 314 SSVERNILPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARGAWEE 393
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1276893371 410 tqrgkPNPMNQLLLNNKNIANYLKKDQIKKLLDVRNHIGDAPERA 454
Cdd:COG0015 394 -----GNDLRELLAADPEIPAELSKEELEALFDPANYLGAADEIV 433
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
16-448 |
3.84e-151 |
|
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: 437.13 E-value: 3.84e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 16 RYGSPEMRKIFSEKHKVELWRKIWVALAEAQHQAGL-VTKKELDDLKKNQNSFNIEEIQKIEKETRHDVVAAIYEFASQA 94
Cdd:cd03302 4 RYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLdISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHAFGLLC 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 95 KIGGGKIHLGATSMDIVDNADMMRIKEALEIIEKRLKIVLLNFAEKIKKYAHFPCIGYTHFQPAEPTTVGYRLAFYGQDL 174
Cdd:cd03302 84 PAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 175 LMAWEFIQFVKKIIKAKGVKGAVGTAASFKALLKNSQIKVDQLEKKVMESLGIEAS-LITTQVYPRQYDFILLTALALVG 253
Cdd:cd03302 164 LMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVyPVTGQTYSRKVDIDVLNALSSLG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 254 SSMAKFCGDLRILqsANFGEWSEPFGKKQVGSSAMPFKKNPITSENICSLARYLAALPQVALENATLSYLERTLDDSANK 333
Cdd:cd03302 244 ATAHKIATDIRLL--ANLKEVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDSANR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 334 RTIIPEGFLITDQILISSEKIITGLVVNEPRISYNLNQYAPFAASEAILIEAVKNGANRQELHETLRQISLLAWQE-TQR 412
Cdd:cd03302 322 RIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERIRVLSHQAAAVvKQE 401
|
410 420 430
....*....|....*....|....*....|....*.
gi 1276893371 413 GKPNPMNQLLLNNKNIAnyLKKDQIKKLLDVRNHIG 448
Cdd:cd03302 402 GGDNDLIERIKNDAYFK--PIWDELDALLDPKTFIG 435
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
22-401 |
2.82e-140 |
|
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: 407.28 E-value: 2.82e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 22 MRKIFSEKHKVELWRKIWVALAEAQHQAGLVTKKELDDLKKN--QNSFNIEEIQKIEKETRHDVVAAIYEFASQAKIGGG 99
Cdd:cd01595 1 MRAIFSEENKLRTWLDVEAALAEAQAELGLIPKEAAEEIRAAadVFEIDAERIAEIEKETGHDVIAFVYALAEKCGEDAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 100 K-IHLGATSMDIVDNADMMRIKEALEIIEKRLKIVLLNFAEKIKKYAHFPCIGYTHFQPAEPTTVGYRLAFYGQDLLMAW 178
Cdd:cd01595 81 EyVHFGATSQDINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 179 EFIQFVKKIIKAKGVKGAVGTAASFKAllknsqiKVDQLEKKVMESLGIEASLITTQVYPRQYDFILLTALALVGSSMAK 258
Cdd:cd01595 161 ERLEEARERVLVGGISGAVGTHASLGP-------KGPEVEERVAEKLGLKVPPITTQIEPRDRIAELLSALALIAGTLEK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 259 FCGDLRILQSANFGEWSEPFGKKQVGSSAMPFKKNPITSENICSLARYLAALPQVALENATlSYLERTLDDSANKRTIIP 338
Cdd:cd01595 234 IATDIRLLQRTEIGEVEEPFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENLV-QWHERDLSDSSVERNILP 312
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276893371 339 EGFLITDQILISSEKIITGLVVNEPRISYNLNQYAPFAASEAILIEAVKNGANRQELHETLRQ 401
Cdd:cd01595 313 DAFLLLDAALSRLQGLLEGLVVNPERMRRNLDLTWGLILSEAVMMALAKKGLGRQEAYELVKE 375
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
16-457 |
5.69e-133 |
|
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: 390.94 E-value: 5.69e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 16 RYGSPEMRKIFSEKHKVELWRKIWVALAEAQHQAGLVTKKELDDLKKNQNS--FNIEEIQKIEKETRHDVVAAIYEFASQ 93
Cdd:TIGR00928 4 RYGSPEMRAIWSEENKFKTWLDVEVAVLRALAELGVIPAEAVKEIREKANFteVDLERIKEIEAVTRHDVKAVVYALKEK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 94 AKIGGGKIHLGATSMDIVDNADMMRIKEALEIIEKRLKIVLLNFAEKIKKYAHFPCIGYTHFQPAEPTTVGYRLAFYGQD 173
Cdd:TIGR00928 84 CGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 174 LLMAWEFIQFVKKIIKAKGVKGAVGTAASFKALLKnsqikvdQLEKKVMESLGIEASLITTQVYPRQYDFILLTALALVG 253
Cdd:TIGR00928 164 MLRQLERLLQAKERIKVGGISGAVGTHAAAYPLVE-------EVEERVTEFLGLKPVPISTQIEPRDRHAELLDALALLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 254 SSMAKFCGDLRILQSANFGEWSEPFGKKQVGSSAMPFKKNPITSENICSLARYLAALPQVALENATLsYLERTLDDSANK 333
Cdd:TIGR00928 237 TTLEKFAVDIRLLQRTEHFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLARVIRGYASPALENAPL-WHERDLTDSSVE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 334 RTIIPEGFLITDQILISSEKIITGLVVNEPRISYNLNQYAPFAASEAILIEAVKNGANRQELHETLRQISLLAWQETQRG 413
Cdd:TIGR00928 316 RVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAAEVDEPD 395
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1276893371 414 kpnpMNQLLLNNKNIANYLKKDQIKKLLDVRNHIGDAPERALKL 457
Cdd:TIGR00928 396 ----LLEFLLEDERITKYLKEEELAELLDPETYIGNAGEIVERV 435
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
16-401 |
8.44e-114 |
|
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: 339.91 E-value: 8.44e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 16 RYGSPEMRKIFSEKHKVELWRKIWVALAEAQHQAGLVTKKELDDLKKNQNsFNIEEIQKIEKETRHDVVAAIYEFASQAK 95
Cdd:cd01360 1 RYGRPEMKKIWSEENKFRKWLEVEAAVCEAWAKLGVIPAEAAEEIRKKAK-FDVERVKEIEAETKHDVIAFVTAIAEYCG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 96 IGGGKIHLGATSMDIVDNADMMRIKEALEIIEKRLKIVLLNFAEKIKKYAHFPCIGYTHFQPAEPTTVGYRLAFYGQDLL 175
Cdd:cd01360 80 EAGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 176 MAWEFIQFVKKIIKAKGVKGAVGTAASFKAllknsqikvdQLEKKVMESLGIEASLITTQVYPRQYDFILLTALALVGSS 255
Cdd:cd01360 160 RHLERLKEARERILVGKISGAVGTYANLGP----------EVEERVAEKLGLKPEPISTQVIQRDRHAEYLSTLALIAST 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 256 MAKFCGDLRILQSANFGEWSEPFGKKQVGSSAMPFKKNPITSENICSLARYLAALPQVALENATLsYLERTLDDSANKRT 335
Cdd:cd01360 230 LEKIATEIRHLQRTEVLEVEEPFSKGQKGSSAMPHKRNPILSENICGLARVIRSNVIPALENVAL-WHERDISHSSVERV 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1276893371 336 IIPEGFLITDQILISSEKIITGLVVNEPRISYNLNQYAPFAASEAILIEAVKNGANRQELHETLRQ 401
Cdd:cd01360 309 ILPDATILLDYILRRMTRVLENLVVYPENMRRNLNLTKGLIFSQRVLLALVEKGMSREEAYEIVQR 374
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
32-361 |
2.02e-81 |
|
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: 254.73 E-value: 2.02e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 32 VELWRKIWVALAEAQHQAGLVTKKELDDLKK--NQNSFNIEEIQK-IEKETRHDVVAAIYEFASQA-KIGGGKIHLGATS 107
Cdd:cd01334 1 IRADLQVEKAHAKALAELGLLPKEAAEAILAalDEILEGIAADQVeQEGSGTHDVMAVEEVLAERAgELNGGYVHTGRSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 108 MDIVDNADMMRIKEALEIIEKRLKIVLLNFAEKIKKYAHFPCIGYTHFQPAEPTTVGYRLAFYGQDLLMAWEFIQFVKKI 187
Cdd:cd01334 81 NDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 188 IKAKGVK-GAVGTAASFkallknsqikVDQLEKKVMESLGI-EASLITTQ-VYPRqyDFI--LLTALALVGSSMAKFCGD 262
Cdd:cd01334 161 LNVLPLGgGAVGTGANA----------PPIDRERVAELLGFfGPAPNSTQaVSDR--DFLveLLSALALLAVSLSKIAND 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 263 LRILQSANFGEWSEPFgKKQVGSSAMPFKKNPITSENICSLARYLAALPQVALENATLSYlERTLDDSANKRTIIPEGFL 342
Cdd:cd01334 229 LRLLSSGEFGEVELPD-AKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGP-LEDNVDSPVEREALPDSFD 306
|
330
....*....|....*....
gi 1276893371 343 ITDQILISSEKIITGLVVN 361
Cdd:cd01334 307 LLDAALRLLTGVLEGLEVN 325
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
17-452 |
5.54e-75 |
|
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: 241.76 E-value: 5.54e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 17 YGSPEMRKIFSEKHKVELWRKIWVALAEAQHQAGLVTKKELDDLKKN--QNSFNIEEIQKIEKETRHDVVAAIYEFASQA 94
Cdd:cd01597 6 FGTPAMREIFSDENRVQAMLDVEAALARAQAELGVIPKEAAAEIAAAadVERLDLEALAEATARTGHPAIPLVKQLTAAC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 95 KIGGGK-IHLGATSMDIVDNADMMRIKEALEIIEKRLKIVLLNFAEKIKKYAHFPCIGYTHFQPAEPTTVGYRLAFYGQD 173
Cdd:cd01597 86 GDAAGEyVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 174 LLMAWEFIQFVKKIIKAKGVKGAVGTAASF--KALlknsqikvdQLEKKVMESLGIEASLITTQVyprQYDFI--LLTAL 249
Cdd:cd01597 166 LLRHRERLDELRPRVLVVQFGGAAGTLASLgdQGL---------AVQEALAAELGLGVPAIPWHT---ARDRIaeLASFL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 250 ALVGSSMAKFCGDLRILQSANFGEWSEPFGKKQVGSSAMPFKKNPITSENICSLARYLAALPQVALEnATLSYLERtlDD 329
Cdd:cd01597 234 ALLTGTLGKIARDVYLLMQTEIGEVAEPFAKGRGGSSTMPHKRNPVGCELIVALARRVPGLAALLLD-AMVQEHER--DA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 330 SA--NKRTIIPEGFLITDQILISSEKIITGLVVNEPRISYNLNQYAPFAASEAILIE-AVKNGanRQELHETLRQISLLA 406
Cdd:cd01597 311 GAwhAEWIALPEIFLLASGALEQAEFLLSGLEVNEDRMRANLDLTGGLILSEAVMMAlAPKLG--RQEAHDLVYEACMRA 388
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1276893371 407 WQETQrgkpnPMNQLLLNNKNIANYLKKDQIKKLLDVRNHIGDAPE 452
Cdd:cd01597 389 VEEGR-----PLREVLLEDPEVAAYLSDEELDALLDPANYLGSAPA 429
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
248-448 |
2.11e-57 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 188.70 E-value: 2.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 248 ALALVGSSMAKFCGDLRILQSANFGEWSEPFGKKQVGSSAMPFKKNPITSENICSLARYLAALPQVALENATLsYLERTL 327
Cdd:PRK08937 22 VLALIATSLEKFANEIRLLQRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENVPL-WHERDL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 328 DDSANKRTIIPEGFLITDQILISSEKIITGLVVNEPRISYNLNQYAPFAASEAILIEAVKNGANRQELHETLRQISLLAW 407
Cdd:PRK08937 101 SHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIREKAMEAW 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1276893371 408 QETqrgkpNPMNQLLLNNKNIANYLKKDQIKKLLDVRNHIG 448
Cdd:PRK08937 181 KNQ-----KDLRELLEADERFTKQLTKEELDELFDPEAFVG 216
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
95-348 |
4.72e-38 |
|
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: 138.51 E-value: 4.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 95 KIGGGKIHLGATSMDIVDNADMMRIKEALEIIEKRLKIVLLNFAEKIKKYAHFPCIGYTHFQPAEPTTVGYRLAFYGQDL 174
Cdd:cd01594 31 LHGSALVHKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDAQPVTLGYELRAWAQVL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 175 LMAWEFIQFVkkiikakgvkgAVGTAASfkallknsqikvdqlekkvmeslgieaslittqvyprqydfilltALALVGS 254
Cdd:cd01594 111 GRDLERLEEA-----------AVAEALD---------------------------------------------ALALAAA 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 255 SMAKFCGDLRILQSANFGEWSEPFGKKQVGSSAMPFKKNPITSENICSLARYLAALPQVALENATLSyLERTLDDSANKR 334
Cdd:cd01594 135 HLSKIAEDLRLLLSGEFGELGEPFLPGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGG-PERDNEDSPSMR 213
|
250
....*....|....
gi 1276893371 335 TIIPEGFLITDQIL 348
Cdd:cd01594 214 EILADSLLLLIDAL 227
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
16-300 |
8.74e-35 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 131.72 E-value: 8.74e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 16 RYG--SPEMRKIFSEKHKVELW-----RKIWVALAEAQHQAGLVTKKELDD----LKKNQNSFNIEEIQKIEKETRHDVV 84
Cdd:pfam00206 2 RFTvpADALMGIFTDRSRFNFRlgeedIKGLAALKKAAAKANVILKEEAAAiikaLDEVAEEGKLDDQFPLKVWQEGSGT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 85 AA-------IYEFASQAKIGGGKIHLGATSMDIVDNAdmMRI--KEAL-EIIEKRLKIVLLNFAEKIKKYAHFPCIGYTH 154
Cdd:pfam00206 82 AVnmnlnevIGELLGQLVHPNDHVHTGQSSNDQVPTA--LRLalKDALsEVLLPALRQLIDALKEKAKEFADIVKPGRTH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 155 FQPAEPTTVGYRLAFYGQDLLMAWEFI-QFVKKIIKAK-GVKGAVGTAAsfkallkNSQIKVDQL---EKKVMESLGIEA 229
Cdd:pfam00206 160 LQDATPVTLGQELSGYAVALTRDRERLqQLLPRLLVLPlGGGTAVGTGL-------NADPEFAELvakELGFFTGLPVKA 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276893371 230 SLITTQVYPRqyDFI--LLTALALVGSSMAKFCGDLRILQSANFGEWSEPFGKKQVGSSAMPFKKNPITSENI 300
Cdd:pfam00206 233 PNSFEATSDR--DAVveLSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEPGSSIMPGKVNPDQLELL 303
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
23-371 |
2.10e-28 |
|
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: 116.57 E-value: 2.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 23 RKIFSE----KHKVE---LWRKIWVALAEAQHQAGLV--TKKELDDLKKNQNSFNIEEIQKIEKETRHDVVAAIY---EF 90
Cdd:cd01598 2 RPYFSEyaliKYRVQvevEWLIALSNLEEIPEVPPLTkeELKFLRAIIENFSEEDALRIKEIEATTNHDVKAVEYflkEK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 91 ASQAKIGGGK---IHLGATSMDIVDNADMMRIKEALE-IIEKRLKIVLLNFAEKIKKYAHFPCIGYTHFQPAEPTTVGYR 166
Cdd:cd01598 82 FETLGLLKKIkefIHFACTSEDINNLAYALMIKEARNeVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 167 LAFYGQDLlmAWEFIQFVKKIIKAKgVKGAVGTAASFKALLKNsqIKVDQLEKKVMESLGIEASLITTQVYPrqYDFI-- 244
Cdd:cd01598 162 LAVFVYRL--ERQYKQLKQIEILGK-FNGAVGNFNAHLVAYPD--VDWRKFSEFFVTSLGLTWNPYTTQIEP--HDYIae 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 245 LLTALALVGSSMAKFCGDlrILQSANFGEWSEPFGKKQVGSSAMPFKKNPITSENI-------CSLARYLAA-LPQvale 316
Cdd:cd01598 235 LFDALARINTILIDLCRD--IWGYISLGYFKQKVKKGEVGSSTMPHKVNPIDFENAegnlglsNALLNHLSAkLPI---- 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1276893371 317 natlSYLERTLDDSANKRTI-IPEGFlitdqILISSEKIITGL---VVNEPRISYNLNQ 371
Cdd:cd01598 309 ----SRLQRDLTDSTVLRNIgVAFGH-----SLIAYKSLLRGLdklELNEARLLEDLDA 358
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
16-386 |
2.13e-27 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 114.08 E-value: 2.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 16 RYGS--PEMRKIFSE----KH--KVEL-WRKiwvALAEAQHQAGL-----VTKKELDDLKKNQNSFNIEEIQKIEKETRH 81
Cdd:PRK09285 15 RYASktAALRPIFSEfgliRYrvQVEVeWLI---ALAAHPGIPEVppfsaEANAFLRAIVENFSEEDAARIKEIERTTNH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 82 DVVAAIY----EFASQAKIGGGK--IHLGATSMDIVDNADMMRIKEALEiiekrlkIVLLNFAEKI--------KKYAHF 147
Cdd:PRK09285 92 DVKAVEYflkeKLAGLPELEAVSefIHFACTSEDINNLSHALMLKEARE-------EVLLPALRELidalkelaHEYADV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 148 PCIGYTHFQPAEPTTVGYRLAFYgqdllmAWEFIQFVKKIIKAK--G-VKGAVGT-AASFKALlknsqIKVD--QLEKKV 221
Cdd:PRK09285 165 PMLSRTHGQPATPTTLGKEMANV------AYRLERQLKQLEAVEilGkINGAVGNyNAHLAAY-----PEVDwhAFSREF 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 222 MESLGIEASLITTQVYPrqYDFI--LLTALALVGSSMAKFCGDLrilqsanfgeWS----EPFGKK----QVGSSAMPFK 291
Cdd:PRK09285 234 VESLGLTWNPYTTQIEP--HDYIaeLFDAVARFNTILIDLDRDV----------WGyislGYFKQKtkagEIGSSTMPHK 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 292 KNPITSEN-------ICSLARYLAA-LPQvalenatlSYLERTLDDSANKRTI-IPEGflitdQILISSEKIITG---LV 359
Cdd:PRK09285 302 VNPIDFENsegnlglANALLEHLAAkLPI--------SRWQRDLTDSTVLRNLgVAFG-----YSLIAYDSLLKGlgkLE 368
|
410 420
....*....|....*....|....*..
gi 1276893371 360 VNEPRISYNLNqyapfaASEAILIEAV 386
Cdd:PRK09285 369 VNEARLAEDLD------ANWEVLAEPI 389
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
17-455 |
2.09e-23 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 102.40 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 17 YGSPEMRKIFSEKHKVELWRKIWVALAEAQHQAGLVTKkelddlkknqnsfniEEIQKIEKETRhdvvAAIYEFAS--QA 94
Cdd:PRK09053 12 FGSPAMRAIFSDRATVQRMLDFEAALARAEAACGVIPA---------------AAVAPIEAACD----AERLDLDAlaQA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 95 KIGGGK-----------------------IHLGATSMDIVDNADMMRIKEALEIIEKRLKIVLLNFAEKIKKYAHFPCIG 151
Cdd:PRK09053 73 AALAGNlaiplvkqltaqvaardaeaaryVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 152 YTHFQPAEPTTVGYRLAFYGQDLLMAWEFIQFVKKIIKAKGVKGAVGTAASF--KALlknsqikvdqlekKVMESLGIEA 229
Cdd:PRK09053 153 RTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGGAAGTLASLgeQAL-------------PVAQALAAEL 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 230 SL-ITTQVYPRQYDFILLTA--LALVGSSMAKFCGDLRILQSANFGEWSEPFGKKQVGSSAMPFKKNPITSENICS---- 302
Cdd:PRK09053 220 QLaLPALPWHTQRDRIAEFAsaLGLLAGTLGKIARDVSLLMQTEVGEVFEPAAAGKGGSSTMPHKRNPVGCAAVLTaatr 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 303 ----LARYLAALPQvalENatlsylERTLDDSANKRTIIPEGFLITDQILISSEKIITGLVVNEPRISYNLNQYAPFAAS 378
Cdd:PRK09053 300 apglVATLFAAMPQ---EH------ERALGGWHAEWDTLPELACLAAGALAQMAQIVEGLEVDAARMRANLDLTHGLILA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 379 EAILIE-AVKNGanRQELHETLRQISLLAwQETQRgkpnPMNQLLLNNKNIANYLKKDQIKKLLDVRNHIGDAP---ERA 454
Cdd:PRK09053 371 EAVMLAlADRIG--RLDAHHLVEQASKRA-VAEGR----HLRDVLAEDPQVSAHLSPAALDRLLDPAHYLGQAHawvDRV 443
|
.
gi 1276893371 455 L 455
Cdd:PRK09053 444 L 444
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
2-310 |
6.75e-23 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 99.36 E-value: 6.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 2 SNFDYStYLSSFtwrYGSPEMRKIFSEKHKVELWRKIWVALAEAQHQAGLVTKKELDDLKKNQNSFNIEeIQKIEKETRH 81
Cdd:PRK05975 4 SVFDHP-FLSGL---FGDDEIAALFSAEADIAAMLAFEAALAEAEAEHGIIPAEAAERIAAACETFEPD-LAALRHATAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 82 DVVAaIYEFASQ--AKIG---GGKIHLGATSMDIVDNADMMRIKEALEIIEKRLKIVLLNFAEKIKKYAHFPCIGYTHFQ 156
Cdd:PRK05975 79 DGVV-VPALVRQlrAAVGeeaAAHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 157 PAEPTTVGYRLAFYGQDLLMAWEFIQFVKKIIKAKGVKGAVGTaasfkallknsqikVDQLEKK---VMESLGIEASLIT 233
Cdd:PRK05975 158 AAIPITVADRLASWRAPLLRHRDRLEALRADVFPLQFGGAAGT--------------LEKLGGKaaaVRARLAKRLGLED 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276893371 234 TQVYPRQYDFILLTA--LALVGSSMAKFCGDLrILQSANFGEWSEPFGKkqvGSSAMPFKKNPITSENICSLARYLAAL 310
Cdd:PRK05975 224 APQWHSQRDFIADFAhlLSLVTGSLGKFGQDI-ALMAQAGDEISLSGGG---GSSAMPHKQNPVAAETLVTLARFNATQ 298
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
8-371 |
8.34e-19 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 88.64 E-value: 8.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 8 TYLSSFTWRYGS--PEMRKIFSEkhkVELWR-KIWVALAEAQHQAGLVTKKELDDLKKNQNS--------FNIE---EIQ 73
Cdd:PLN02848 10 TALSPLDGRYWSkvKDLRPIFSE---FGLIRyRVLVEVKWLLKLSQIPEVTEVPPFSDEANSflegiiagFSVDdalEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 74 KIEKETRHDVVAAIY----EFASQAKIGggKI----HLGATSMDIVDNADMMRIKEALE-IIEKRLKIVLLNFAEKIKKY 144
Cdd:PLN02848 87 KIERVTNHDVKAVEYflkqKCKSHPELA--KVleffHFACTSEDINNLSHALMLKEGVNsVVLPTMDEIIKAISSLAHEF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 145 AHFPCIGYTHFQPAEPTTVGYRLAFYGQDLLMAWEFIQFVKkiIKAKgVKGAVGT-AASFKALlknSQIKVDQLEKKVME 223
Cdd:PLN02848 165 AYVPMLSRTHGQPASPTTLGKEMANFAYRLSRQRKQLSEVK--IKGK-FAGAVGNyNAHMSAY---PEVDWPAVAEEFVT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 224 SLGIEASLITTQVYPRQYDFILLTALALVGSSMAKFcgDLRILQSANFGEWSEPFGKKQVGSSAMPFKKNPITSENicsl 303
Cdd:PLN02848 239 SLGLTFNPYVTQIEPHDYMAELFNAVSRFNNILIDF--DRDIWSYISLGYFKQITKAGEVGSSTMPHKVNPIDFEN---- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 304 arylaALPQVALENATLSYL---------ERTLDDSANKRTiIPEGF---LITDQiliSSEKIITGLVVNEPRISYNLNQ 371
Cdd:PLN02848 313 -----SEGNLGLANAELSHLsmklpisrmQRDLTDSTVLRN-MGVGLghsLLAYK---STLRGIGKLQVNEARLAEDLDQ 383
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
38-298 |
1.91e-17 |
|
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: 84.14 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 38 IWVALAEAQ--HQAGLVTKKELDDLkknqnsfnIEEIQKIEKETRH----------DVVAAIyEFASQAKIG--GGKIHL 103
Cdd:cd01359 13 IAGSIAHAVmlAEQGILTEEEAAKI--------LAGLAKIRAEIEAgafeldpedeDIHMAI-ERRLIERIGdvGGKLHT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 104 GATSMDIVDNADMMRIKEALEIIEKRLKIVLLNFAEKIKKYAHFPCIGYTHFQPAEPTTVGYRLAFYGQDLLMAWEFIQF 183
Cdd:cd01359 84 GRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLERLAD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 184 VKKIIKakgvKGAVGTAAsfkalLKNSQIKVDQleKKVMESLG----IEASLITTQVyprqYDFIL--LTALALVGSSMA 257
Cdd:cd01359 164 AYKRVN----VSPLGAGA-----LAGTTFPIDR--ERTAELLGfdgpTENSLDAVSD----RDFVLefLSAAALLMVHLS 228
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1276893371 258 KFCGDLRILQSANFG--EWSEPFGkkqVGSSAMPFKKNPITSE 298
Cdd:cd01359 229 RLAEDLILWSTQEFGfvELPDAYS---TGSSIMPQKKNPDVLE 268
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
47-305 |
9.45e-15 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 75.96 E-value: 9.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 47 HQAGLVTKKELDDLkknqnsfnIEEIQKIEKETRH----------DVVAAIyEFASQAKIG--GGKIHLG-------ATs 107
Cdd:PRK00855 48 AKQGILSEEEAEKI--------LAGLDEILEEIEAgkfefspeleDIHMAI-EARLTERIGdvGGKLHTGrsrndqvAT- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 108 mdivdnaDM-MRIKEAL-EIIE--KRLKIVLLNFAEKikkYAHFPCIGYTHFQPAEPTTVGYRLAFYGQDLLMAWEFIQF 183
Cdd:PRK00855 118 -------DLrLYLRDEIdEIAEllLELQKALLDLAEE---HADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLERLRD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 184 VKKIIKakgvKGAVGTAAsfkalLKNSQIKVDQleKKVMESLGIEAslittqVYP--------RqyDFIL--LTALALVG 253
Cdd:PRK00855 188 ARKRVN----RSPLGSAA-----LAGTTFPIDR--ERTAELLGFDG------VTEnsldavsdR--DFALefLSAASLLM 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1276893371 254 SSMAKFCGDLRILQSANFG------EWSepfgkkqVGSSAMPFKKNPITSEnicsLAR 305
Cdd:PRK00855 249 VHLSRLAEELILWSSQEFGfvelpdAFS-------TGSSIMPQKKNPDVAE----LIR 295
|
|
| ADSL_C |
pfam10397 |
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ... |
374-452 |
2.06e-13 |
|
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: 65.13 E-value: 2.06e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276893371 374 PFAASEAILIEAVKnGANRQELHETLRQISLLAWQETQrgkpNPMNQLLLNNKNIAnYLKKDQIKKLLDVRNHIGDAPE 452
Cdd:pfam10397 1 GLIFSERVLLALVK-GLGREEAHELVQEAAMKAWEEGK----NDLRELLAADPEVT-YLSEEELDALFDPAYYLGRADE 73
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
49-305 |
8.72e-13 |
|
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: 70.08 E-value: 8.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 49 AGLVTKKELDDLkknqnsfnIEEIQKIEKETR----------HDVVAAIyEFASQAKIG---GGKIHLGATSMDIVdnAD 115
Cdd:TIGR00838 45 AGILTEEEAAKI--------IEGLNELKEEGRegpfildpddEDIHMAI-ERELIDRVGedlGGKLHTGRSRNDQV--AT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 116 MMRI--KEALEIIEKRLKIVLLNFAEKIKKYAHFPCIGYTHFQPAEPTTVGYRLAFYGQDLLMAWE-FIQFVKKIIKAKG 192
Cdd:TIGR00838 114 DLRLylRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLRDYErLQDALKRVNVSPL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 193 VKGAVGTAA------------SFKALLKNSqikvdqlekkvMESlgieaslittqVYPRqyDFIL--LTALALVGSSMAK 258
Cdd:TIGR00838 194 GSGALAGTGfpidreylaellGFDAVTENS-----------LDA-----------VSDR--DFILelLFVAALIMVHLSR 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1276893371 259 FCGDLRILQSANFG------EWSEpfgkkqvGSSAMPFKKNPitseNICSLAR 305
Cdd:TIGR00838 250 FAEDLILWSTGEFGfvelpdEFSS-------GSSIMPQKKNP----DVAELIR 291
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
40-294 |
2.58e-12 |
|
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: 68.59 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 40 VALAEAqhqaGLVTKKELDDLkknqnsfnIEEIQKIEKETRH----------DVVAAIyEFASQAKIG--GGKIHLGATS 107
Cdd:COG0165 44 RMLAEQ----GIISAEEAAAI--------LAGLDEIEAEIEAgafefdpeleDIHMNI-ERRLIERIGdvGGKLHTGRSR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 108 MDIVdnADMMRI---KEALEIIE--KRLKIVLLNFAEKikkYAHFPCIGYTHFQPAEPTTVGYRLAFYGQDLLMAWEFIQ 182
Cdd:COG0165 111 NDQV--ATDFRLylrDEILELIEalLALQEALLDLAEE---HADTIMPGYTHLQRAQPVTFGHHLLAYAEMLLRDRERLA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 183 FVKKIIK-----AkgvkGAV-GTA--------AS---FKALLKNSqikvdqlekkvmeslgIEAslittqVYPRqyDFIL 245
Cdd:COG0165 186 DAYKRLNvsplgA----AALaGTTfpidrertAEllgFDGPTENS----------------LDA------VSDR--DFAL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1276893371 246 --LTALALVGSSMAKFCGDLrILQSanfgewSEPFGkkQV--------GSSAMPFKKNP 294
Cdd:COG0165 238 efLSAASLIMVHLSRLAEEL-ILWS------SSEFG--FVelpdafstGSSIMPQKKNP 287
|
|
| ADSL_C |
smart00998 |
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ... |
374-452 |
3.62e-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: 61.70 E-value: 3.62e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1276893371 374 PFAASEAILIEAVKNGANRQELHETLRQISLLAWQEtqrGKpnPMNQLLLNNKNIANYLKKDQIKKLLDVRNHIGDAPE 452
Cdd:smart00998 2 GLIFSERVLLALVEKGLGREEAYELVQRAAMKAWEE---GK--DLRELLLADPEVTAYLSEEELEELFDPEYYLGHADA 75
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
121-300 |
1.89e-05 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 46.90 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 121 EALEIIEKRLKIVLLNFAEKIKKYAHFPCIGYTHFQPAEPTTVGYRLAFYGQDLLMAWEFIQFVKKIIKAKGVKG-AVGT 199
Cdd:PRK13353 155 NLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGtAVGT 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 200 --AASFKALLKnsqiKVDQLEKKVMESLGIEASLI-TTQvyprQYD-FILLT-ALALVGSSMAKFCGDLRILQS---ANF 271
Cdd:PRK13353 235 glNADPEYIER----VVKHLAAITGLPLVGAEDLVdATQ----NTDaFVEVSgALKVCAVNLSKIANDLRLLSSgprTGL 306
|
170 180
....*....|....*....|....*....
gi 1276893371 272 GEWSEPfgKKQVGSSAMPFKKNPITSENI 300
Cdd:PRK13353 307 GEINLP--AVQPGSSIMPGKVNPVMPEVV 333
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
40-294 |
1.31e-04 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 44.33 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 40 VALAEAQHQAGLVTKKELDDLKKNqnsfnIEEIQK-IEKET------RHDVVAAIyEFASQAKIG--GGKIHLGATSMDI 110
Cdd:PLN02646 53 KAHASMLAKQGIITDEDRDSILDG-----LDEIEKeIEAGKfewrpdREDVHMNN-EARLTELIGepAKKLHTARSRNDQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 111 VDNADMMRIKEALEIIEKRLKIVLLNFAEKIKKYAHFPCIGYTHFQPAEPTtvgyRLafygQDLLMAwefiqFVKKIIKA 190
Cdd:PLN02646 127 VATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPV----LL----SHWLLS-----HVEQLERD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 191 KGVKGAVGTAASFKAL----LKNSQIKVDQleKKVMESLGIEASLITT--QVYPRqyDFIL--LTALALVGSSMAKFCGD 262
Cdd:PLN02646 194 AGRLVDCRPRVNFCPLgscaLAGTGLPIDR--FMTAKDLGFTAPMRNSidAVSDR--DFVLefLFANSITAIHLSRLGEE 269
|
250 260 270
....*....|....*....|....*....|..
gi 1276893371 263 LRILQSANFGeWSEPFGKKQVGSSAMPFKKNP 294
Cdd:PLN02646 270 WVLWASEEFG-FVTPSDAVSTGSSIMPQKKNP 300
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
245-298 |
5.48e-04 |
|
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: 42.12 E-value: 5.48e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1276893371 245 LLTALALvgsSMAKFCGDLRILQS---ANFGEWSEPfgKKQVGSSAMPFKKNPITSE 298
Cdd:cd01357 275 ALKRLAV---KLSKIANDLRLLSSgprAGLGEINLP--AVQPGSSIMPGKVNPVIPE 326
|
|
| PRK06705 |
PRK06705 |
argininosuccinate lyase; Provisional |
89-299 |
1.78e-03 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 180664 [Multi-domain] Cd Length: 502 Bit Score: 40.74 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 89 EFASQAKIGGGKIHLGATSMDIVDNADMMRIKEALEIIEKRLKIVLLNFAEKIKKyahfpciGYTHFQPAEPTTVG-YRL 167
Cdd:PRK06705 105 DFVSNMHIGRSRNDMGVTMYRMSLRRYVLRLMEHHLLLQESILQLAADHKETIMP-------AYTHTQPAQPTTFGhYTL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1276893371 168 AFY---GQDLLMAWEFIQFVKkiikakgvKGAVGTAAsfkalLKNSQIKVDQleKKVMESLGIeaslitTQVYPRQYDFI 244
Cdd:PRK06705 178 AIYdtmQRDLERMKKTYKLLN--------QSPMGAAA-----LSTTSFPIKR--ERVADLLGF------TNVIENSYDAV 236
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1276893371 245 -----LL---TALALVGSSMAKFCGDLRILQSANFGEWSEPFGKKQVgSSAMPFKKNPITSEN 299
Cdd:PRK06705 237 agadyLLevsSLLMVMMTNTSRWIHDFLLLATKEYDGITVARPYVQI-SSIMPQKRNPVSIEH 298
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
245-298 |
2.51e-03 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 40.11 E-value: 2.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1276893371 245 LLTALALvgsSMAKFCGDLRILQS---ANFGEWSEPfgKKQVGSSAMPFKKNPITSE 298
Cdd:PRK12273 282 ALKRLAV---KLSKICNDLRLLSSgprAGLNEINLP--AVQAGSSIMPGKVNPVIPE 333
|
|
| |
