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Conserved domains on  [gi|17508577|ref|NP_492049|]
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Adenylosuccinate lyase [Caenorhabditis elegans]

Protein Classification

adenylosuccinate lyase( domain architecture ID 10129463)

adenylosuccinate lyase catalyzes two non-sequential steps in de novo AMP synthesis: converts (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- carboxamido)succinate (SAICAR) to fumarate plus 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, and thereby also contributes to de novo IMP synthesis, and converts succinyladenosine monophosphate (SAMP) to AMP and fumarate

CATH:  1.10.275.10|1.10.40.30|1.20.200.10
EC:  4.3.2.2
Gene Ontology:  GO:0004018|GO:0006188|GO:0009152
PubMed:  10673438
SCOP:  4001433

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Adenylsuccinate_lyase_2 cd03302
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ...
 11-446 0e+00

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: 677.88  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  11 LSTRYCKNsPLVSILSETNKATLWRQLWIWLAEAEKELGLKqVTQDAIDEMKSNRDVFDWPFIRSEERKLKHDVMAHNHA 90
Cdd:cd03302   1 LASRYASK-EMVYIFSPRKKFSTWRKLWLWLAEAEKELGLD-ISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  91 FGKLCPTAAGIIHLGATSCFVQDNADLIAYRDSIDHILKRFATVIDRLAAFSLKNKEVVTVGRTHYQTASLVTVGKRGVL 170
Cdd:cd03302  79 FGLLCPAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 171 WAQELLMAFQSLSEFRDKMRFRGIKGATGTQDSFLTLFAGDESKVEALDELVTKKANFSNRFLITGQTYSRQQDSQLVFS 250
Cdd:cd03302 159 WIQDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVYPVTGQTYSRKVDIDVLNA 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 251 LSLLGAAAKKVCTDIRVLQAFGELLEPFEKDQIGSSAMPYKKNPMKSERCCALSRKLINAPQEALTILADQGLERTLDDS 330
Cdd:cd03302 239 LSSLGATAHKIATDIRLLANLKEVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDS 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 331 AGRRMLIPDVLLTAEALLTTLQNIFEGLSVQTDNVKKIVEDEIAFLGLEKAMMMLTEEGVDRQQAHAVIRKTALEA--KQ 408
Cdd:cd03302 319 ANRRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERIRVLSHQAaaVV 398

                       410       420       430
                ....*....|....*....|....*....|....*....
gi 17508577 409 LQATQKVDIRQTM-ADPFFDSVRDRVVGLVnNPINFTGR 446
Cdd:cd03302 399 KQEGGDNDLIERIkNDAYFKPIWDELDALL-DPKTFIGR 436
 
Name Accession Description Interval E-value
Adenylsuccinate_lyase_2 cd03302
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ...
 11-446 0e+00

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: 677.88  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  11 LSTRYCKNsPLVSILSETNKATLWRQLWIWLAEAEKELGLKqVTQDAIDEMKSNRDVFDWPFIRSEERKLKHDVMAHNHA 90
Cdd:cd03302   1 LASRYASK-EMVYIFSPRKKFSTWRKLWLWLAEAEKELGLD-ISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  91 FGKLCPTAAGIIHLGATSCFVQDNADLIAYRDSIDHILKRFATVIDRLAAFSLKNKEVVTVGRTHYQTASLVTVGKRGVL 170
Cdd:cd03302  79 FGLLCPAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 171 WAQELLMAFQSLSEFRDKMRFRGIKGATGTQDSFLTLFAGDESKVEALDELVTKKANFSNRFLITGQTYSRQQDSQLVFS 250
Cdd:cd03302 159 WIQDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVYPVTGQTYSRKVDIDVLNA 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 251 LSLLGAAAKKVCTDIRVLQAFGELLEPFEKDQIGSSAMPYKKNPMKSERCCALSRKLINAPQEALTILADQGLERTLDDS 330
Cdd:cd03302 239 LSSLGATAHKIATDIRLLANLKEVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDS 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 331 AGRRMLIPDVLLTAEALLTTLQNIFEGLSVQTDNVKKIVEDEIAFLGLEKAMMMLTEEGVDRQQAHAVIRKTALEA--KQ 408
Cdd:cd03302 319 ANRRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERIRVLSHQAaaVV 398

                       410       420       430
                ....*....|....*....|....*....|....*....
gi 17508577 409 LQATQKVDIRQTM-ADPFFDSVRDRVVGLVnNPINFTGR 446
Cdd:cd03302 399 KQEGGDNDLIERIkNDAYFKPIWDELDALL-DPKTFIGR 436
PurB COG0015
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ...
 11-452 1.17e-110

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: 333.97  E-value: 1.17e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  11 LSTRYcKNSPLVSILSETNKATLWRQLWIWLAEAEKELGLkqVTQDAIDEMKSN--RDVFDWPFIRSEERKLKHDVMAHN 88
Cdd:COG0015   2 ISPRY-ASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGL--IPAEAAAAIRAAadDFEIDAERIKEIEKETRHDVKAFV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  89 HAFGKLCPTAAG-IIHLGATSCFVQDNADLIAYRDSIDHILKRFATVIDRLAAFSLKNKEVVTVGRTHYQTASLVTVGKR 167
Cdd:COG0015  79 YALKEKVGAEAGeYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 168 GVLWAQELLMAFQSLSEFRDKMRFRGIKGATGTQDSFLTLfagdeskVEALDELVTKKANFSnRFLITGQTYSRQQDSQL 247
Cdd:COG0015 159 LAVWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGEA-------WPEVEERVAEKLGLK-PNPVTTQIEPRDRHAEL 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 248 VFSLSLLGAAAKKVCTDIRVLQA--FGELLEPFEKDQIGSSAMPYKKNPMKSERCCALSRKLINAPQEALTILAdQGLER 325
Cdd:COG0015 231 FSALALIAGSLEKIARDIRLLQRteVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEALA-SWHER 309

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 326 TLDDSAGRRMLIPDVLLTAEALLTTLQNIFEGLSVQTDNVKKIVEDEIAFLGLEKAMMMLTEEGVDRQQAHAVIRKTALE 405
Cdd:COG0015 310 DLSDSSVERNILPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARG 389

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 17508577 406 AkqlqATQKVDIRQTM-ADPFFDSV--RDRVVGLVnNPINFTGRCVSQTE 452
Cdd:COG0015 390 A----WEEGNDLRELLaADPEIPAElsKEELEALF-DPANYLGAADEIVD 434
purB TIGR00928
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ...
 11-454 2.76e-100

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: 307.74  E-value: 2.76e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577    11 LSTRYcKNSPLVSILSETNKATLWRQLWIWLAEAEKELGLKQVTQDAIDEMKSNRDVFDWPFIRSEERKLKHDVMAHNHA 90
Cdd:TIGR00928   1 LDERY-GSPEMRAIWSEENKFKTWLDVEVAVLRALAELGVIPAEAVKEIREKANFTEVDLERIKEIEAVTRHDVKAVVYA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577    91 FGKLCPTAAGIIHLGATSCFVQDNADLIAYRDSIDHILKRFATVIDRLAAFSLKNKEVVTVGRTHYQTASLVTVGKRGVL 170
Cdd:TIGR00928  80 LKEKCGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFAL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577   171 WAQELLMAFQSLSEFRDKMRFRGIKGATGTQDSFLTLFagdeskvEALDELVTKKANFSnRFLITGQTYSRQQDSQLVFS 250
Cdd:TIGR00928 160 WAEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPLV-------EEVEERVTEFLGLK-PVPISTQIEPRDRHAELLDA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577   251 LSLLGAAAKKVCTDIRVLQA--FGELLEPFEKDQIGSSAMPYKKNPMKSERCCALSRkLINAPQEALTILADQGLERTLD 328
Cdd:TIGR00928 232 LALLATTLEKFAVDIRLLQRteHFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLAR-VIRGYASPALENAPLWHERDLT 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577   329 DSAGRRMLIPDVLLTAEALLTTLQNIFEGLSVQTDNVKKIVEDEIAFLGLEKAMMMLTEEGVDRQQAHAVIRKTALEAKq 408
Cdd:TIGR00928 311 DSSVERVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAA- 389

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 17508577   409 lqATQKVDIRQTM-ADPFF-DSVRDRVVGLVNNPINFTGRCVSQTESF 454
Cdd:TIGR00928 390 --EVDEPDLLEFLlEDERItKYLKEEELAELLDPETYIGNAGEIVERV 435
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
 248-410 4.89e-39

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 140.93  E-value: 4.89e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  248 VFSLSLLGAAAKKVCTDIRVLQA--FGELLEPFEKDQIGSSAMPYKKNPMKSERCCALSRKLINAPQEALtILADQGLER 325
Cdd:PRK08937  20 EIVLALIATSLEKFANEIRLLQRseIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTAL-ENVPLWHER 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  326 TLDDSAGRRMLIPDVLLTAEALLTTLQNIFEGLSVQTDNVKKIVEDEIAFLGLEKAMMMLTEEGVDRQQAHAVIRKTALE 405
Cdd:PRK08937  99 DLSHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIREKAME 178


                 ....*
gi 17508577  406 AKQLQ 410
Cdd:PRK08937 179 AWKNQ 183
Lyase_1 pfam00206
Lyase;
42-298 2.61e-15

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 76.64  E-value: 2.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577    42 AEAEKELGLKQVTQDAIDEMKSNRDVFDWPF---IRSEERKLKHDV-MAHNHAFGKLC---PTAAGIIHLGATSCFVQDN 114
Cdd:pfam00206  38 AAAKANVILKEEAAAIIKALDEVAEEGKLDDqfpLKVWQEGSGTAVnMNLNEVIGELLgqlVHPNDHVHTGQSSNDQVPT 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577   115 ADLIAYRDSI-DHILKRFATVIDRLAAFSLKNKEVVTVGRTHYQTASLVTVGKRGVLWAQELLMAFQSLSEFRDKMRFRG 193
Cdd:pfam00206 118 ALRLALKDALsEVLLPALRQLIDALKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLP 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577   194 IKGATGTqdsfltlFAGDESKVEaLDELVTKKANFsnrflITG----------QTYSRQQDSQLVFSLSLLGAAAKKVCT 263
Cdd:pfam00206 198 LGGGTAV-------GTGLNADPE-FAELVAKELGF-----FTGlpvkapnsfeATSDRDAVVELSGALALLATSLSKFAE 264

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 17508577   264 DIRVLQA--FGELLEPFEKDQIGSSAMPYKKNPMKSE 298
Cdd:pfam00206 265 DLRLLSSgpAGLVELSLAEGEPGSSIMPGKVNPDQLE 301
ADSL_C smart00998
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ...
 379-455 4.11e-08

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: 50.53  E-value: 4.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577    379 EKAMMMLTEEGVDRQQAHAVIRKTALEAkqlqATQKVDIRQT-MADPFFDSV--RDRVVGLVnNPINFTGRCVSQTESFI 455
Cdd:smart00998   7 ERVLLALVEKGLGREEAYELVQRAAMKA----WEEGKDLRELlLADPEVTAYlsEEELEELF-DPEYYLGHADAIVDRVL 81
 
Name Accession Description Interval E-value
Adenylsuccinate_lyase_2 cd03302
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ...
 11-446 0e+00

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: 677.88  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  11 LSTRYCKNsPLVSILSETNKATLWRQLWIWLAEAEKELGLKqVTQDAIDEMKSNRDVFDWPFIRSEERKLKHDVMAHNHA 90
Cdd:cd03302   1 LASRYASK-EMVYIFSPRKKFSTWRKLWLWLAEAEKELGLD-ISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHA 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  91 FGKLCPTAAGIIHLGATSCFVQDNADLIAYRDSIDHILKRFATVIDRLAAFSLKNKEVVTVGRTHYQTASLVTVGKRGVL 170
Cdd:cd03302  79 FGLLCPAAAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACL 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 171 WAQELLMAFQSLSEFRDKMRFRGIKGATGTQDSFLTLFAGDESKVEALDELVTKKANFSNRFLITGQTYSRQQDSQLVFS 250
Cdd:cd03302 159 WIQDLLMDLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVYPVTGQTYSRKVDIDVLNA 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 251 LSLLGAAAKKVCTDIRVLQAFGELLEPFEKDQIGSSAMPYKKNPMKSERCCALSRKLINAPQEALTILADQGLERTLDDS 330
Cdd:cd03302 239 LSSLGATAHKIATDIRLLANLKEVEEPFEKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDS 318

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 331 AGRRMLIPDVLLTAEALLTTLQNIFEGLSVQTDNVKKIVEDEIAFLGLEKAMMMLTEEGVDRQQAHAVIRKTALEA--KQ 408
Cdd:cd03302 319 ANRRIAIPEAFLAADAILITLQNISEGLVVYPKVIERHIRQELPFMATENIIMAAVKAGGDRQDAHERIRVLSHQAaaVV 398

                       410       420       430
                ....*....|....*....|....*....|....*....
gi 17508577 409 LQATQKVDIRQTM-ADPFFDSVRDRVVGLVnNPINFTGR 446
Cdd:cd03302 399 KQEGGDNDLIERIkNDAYFKPIWDELDALL-DPKTFIGR 436
Adenylsuccinate_lyase_like cd01595
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ...
 21-401 5.02e-137

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: 399.57  E-value: 5.02e-137
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  21 LVSILSETNKATLWRQLWIWLAEAEKELGLkqVTQDAIDEMKSNRDVF--DWPFIRSEERKLKHDVMAHNHAFGKLCPT- 97
Cdd:cd01595   1 MRAIFSEENKLRTWLDVEAALAEAQAELGL--IPKEAAEEIRAAADVFeiDAERIAEIEKETGHDVIAFVYALAEKCGEd 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  98 AAGIIHLGATSCFVQDNADLIAYRDSIDHILKRFATVIDRLAAFSLKNKEVVTVGRTHYQTASLVTVGKRGVLWAQELLM 177
Cdd:cd01595  79 AGEYVHFGATSQDINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLR 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 178 AFQSLSEFRDKMRFRGIKGATGTQDSFLtlfagdeSKVEALDELVTKKANFsNRFLITGQTYSRQQDSQLVFSLSLLGAA 257
Cdd:cd01595 159 HLERLEEARERVLVGGISGAVGTHASLG-------PKGPEVEERVAEKLGL-KVPPITTQIEPRDRIAELLSALALIAGT 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 258 AKKVCTDIRVLQ--AFGELLEPFEKDQIGSSAMPYKKNPMKSERCCALSRKLINAPQEALTILAdQGLERTLDDSAGRRM 335
Cdd:cd01595 231 LEKIATDIRLLQrtEIGEVEEPFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENLV-QWHERDLSDSSVERN 309

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17508577 336 LIPDVLLTAEALLTTLQNIFEGLSVQTDNVKKIVEDEIAFLGLEKAMMMLTEEGVDRQQAHAVIRK 401
Cdd:cd01595 310 ILPDAFLLLDAALSRLQGLLEGLVVNPERMRRNLDLTWGLILSEAVMMALAKKGLGRQEAYELVKE 375
PurB COG0015
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ...
 11-452 1.17e-110

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: 333.97  E-value: 1.17e-110
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  11 LSTRYcKNSPLVSILSETNKATLWRQLWIWLAEAEKELGLkqVTQDAIDEMKSN--RDVFDWPFIRSEERKLKHDVMAHN 88
Cdd:COG0015   2 ISPRY-ASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGL--IPAEAAAAIRAAadDFEIDAERIKEIEKETRHDVKAFV 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  89 HAFGKLCPTAAG-IIHLGATSCFVQDNADLIAYRDSIDHILKRFATVIDRLAAFSLKNKEVVTVGRTHYQTASLVTVGKR 167
Cdd:COG0015  79 YALKEKVGAEAGeYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKK 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 168 GVLWAQELLMAFQSLSEFRDKMRFRGIKGATGTQDSFLTLfagdeskVEALDELVTKKANFSnRFLITGQTYSRQQDSQL 247
Cdd:COG0015 159 LAVWAAELLRQLERLEEARERVLVGKIGGAVGTYAAHGEA-------WPEVEERVAEKLGLK-PNPVTTQIEPRDRHAEL 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 248 VFSLSLLGAAAKKVCTDIRVLQA--FGELLEPFEKDQIGSSAMPYKKNPMKSERCCALSRKLINAPQEALTILAdQGLER 325
Cdd:COG0015 231 FSALALIAGSLEKIARDIRLLQRteVGEVEEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEALA-SWHER 309

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 326 TLDDSAGRRMLIPDVLLTAEALLTTLQNIFEGLSVQTDNVKKIVEDEIAFLGLEKAMMMLTEEGVDRQQAHAVIRKTALE 405
Cdd:COG0015 310 DLSDSSVERNILPDAFLLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVLSEAVLMALVRRGLGREEAYELVKELARG 389

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|
gi 17508577 406 AkqlqATQKVDIRQTM-ADPFFDSV--RDRVVGLVnNPINFTGRCVSQTE 452
Cdd:COG0015 390 A----WEEGNDLRELLaADPEIPAElsKEELEALF-DPANYLGAADEIVD 434
purB TIGR00928
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ...
 11-454 2.76e-100

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: 307.74  E-value: 2.76e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577    11 LSTRYcKNSPLVSILSETNKATLWRQLWIWLAEAEKELGLKQVTQDAIDEMKSNRDVFDWPFIRSEERKLKHDVMAHNHA 90
Cdd:TIGR00928   1 LDERY-GSPEMRAIWSEENKFKTWLDVEVAVLRALAELGVIPAEAVKEIREKANFTEVDLERIKEIEAVTRHDVKAVVYA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577    91 FGKLCPTAAGIIHLGATSCFVQDNADLIAYRDSIDHILKRFATVIDRLAAFSLKNKEVVTVGRTHYQTASLVTVGKRGVL 170
Cdd:TIGR00928  80 LKEKCGAEGEFIHFGATSNDIVDTALALLLRDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFAL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577   171 WAQELLMAFQSLSEFRDKMRFRGIKGATGTQDSFLTLFagdeskvEALDELVTKKANFSnRFLITGQTYSRQQDSQLVFS 250
Cdd:TIGR00928 160 WAEEMLRQLERLLQAKERIKVGGISGAVGTHAAAYPLV-------EEVEERVTEFLGLK-PVPISTQIEPRDRHAELLDA 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577   251 LSLLGAAAKKVCTDIRVLQA--FGELLEPFEKDQIGSSAMPYKKNPMKSERCCALSRkLINAPQEALTILADQGLERTLD 328
Cdd:TIGR00928 232 LALLATTLEKFAVDIRLLQRteHFEVEEPFGKGQVGSSAMPHKRNPIDFENVCGLAR-VIRGYASPALENAPLWHERDLT 310

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577   329 DSAGRRMLIPDVLLTAEALLTTLQNIFEGLSVQTDNVKKIVEDEIAFLGLEKAMMMLTEEGVDRQQAHAVIRKTALEAKq 408
Cdd:TIGR00928 311 DSSVERVILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIALVERGMGREEAYEIVRELAMGAA- 389

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 17508577   409 lqATQKVDIRQTM-ADPFF-DSVRDRVVGLVNNPINFTGRCVSQTESF 454
Cdd:TIGR00928 390 --EVDEPDLLEFLlEDERItKYLKEEELAELLDPETYIGNAGEIVERV 435
Lyase_I cd01334
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ...
 34-360 1.36e-79

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: 250.50  E-value: 1.36e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  34 WRQLWIWLAEAEKELGLkqVTQDAIDEMKSNRDVFDWPFIRSE---ERKLKHDVMAHNHAFGKLC-PTAAGIIHLGATSC 109
Cdd:cd01334   4 DLQVEKAHAKALAELGL--LPKEAAEAILAALDEILEGIAADQveqEGSGTHDVMAVEEVLAERAgELNGGYVHTGRSSN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 110 FVQDNADLIAYRDSIDHILKRFATVIDRLAAFSLKNKEVVTVGRTHYQTASLVTVGKRGVLWAQELLMAFQSLSEFRDKM 189
Cdd:cd01334  82 DIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKRL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 190 RFRGIK-GATGTQDSFltlfagdeskVEALDELVTKKANFSNRFLITGQ-TYSRQQDSQLVFSLSLLGAAAKKVCTDIRV 267
Cdd:cd01334 162 NVLPLGgGAVGTGANA----------PPIDRERVAELLGFFGPAPNSTQaVSDRDFLVELLSALALLAVSLSKIANDLRL 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 268 LQA--FGELLEPFEKdQIGSSAMPYKKNPMKSERCCALSRKLINAPQEALTILAdQGLERTLDDSAGRRMLIPDVLLTAE 345
Cdd:cd01334 232 LSSgeFGEVELPDAK-QPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALK-GGPLEDNVDSPVEREALPDSFDLLD 309

                       330
                ....*....|....*
gi 17508577 346 ALLTTLQNIFEGLSV 360
Cdd:cd01334 310 AALRLLTGVLEGLEV 324
Adenylsuccinate_lyase_1 cd01360
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ...
 24-401 8.20e-57

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: 193.15  E-value: 8.20e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  24 ILSETNKATLWRQLWIWLAEAEKELGLkqVTQDAIDEMKSNRDvFDWPFIRSEERKLKHDVMAHNHAFGKLCPTAAGIIH 103
Cdd:cd01360  10 IWSEENKFRKWLEVEAAVCEAWAKLGV--IPAEAAEEIRKKAK-FDVERVKEIEAETKHDVIAFVTAIAEYCGEAGRYIH 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 104 LGATSCFVQDNADLIAYRDSIDHILKRFATVIDRLAAFSLKNKEVVTVGRTHYQTASLVTVGKRGVLWAQELLMAFQSLS 183
Cdd:cd01360  87 FGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLK 166

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 184 EFRDKMRFRGIKGATGTqdsfltlFAGDESKVEAL--DELVTKKANFSNrflitgQTYSRQQDSQLVFSLSLLGAAAKKV 261
Cdd:cd01360 167 EARERILVGKISGAVGT-------YANLGPEVEERvaEKLGLKPEPIST------QVIQRDRHAEYLSTLALIASTLEKI 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 262 CTDIRVLQ--AFGELLEPFEKDQIGSSAMPYKKNPMKSERCCALSRkLINApqEALTILADQGL--ERTLDDSAGRRMLI 337
Cdd:cd01360 234 ATEIRHLQrtEVLEVEEPFSKGQKGSSAMPHKRNPILSENICGLAR-VIRS--NVIPALENVALwhERDISHSSVERVIL 310

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 17508577 338 PDVLLTAEALLTTLQNIFEGLSVQTDNVKKIVEdeiAFLGL---EKAMMMLTEEGVDRQQAHAVIRK 401
Cdd:cd01360 311 PDATILLDYILRRMTRVLENLVVYPENMRRNLN---LTKGLifsQRVLLALVEKGMSREEAYEIVQR 374
pCLME cd01597
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ...
 23-406 2.29e-41

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: 153.17  E-value: 2.29e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  23 SILSETNKATLWRQLWIWLAEAEKELGLkqVTQDAIDEM--KSNRDVFDWPFIRSEERKLKHDVMAHNHAFGKLCPTAAG 100
Cdd:cd01597  13 EIFSDENRVQAMLDVEAALARAQAELGV--IPKEAAAEIaaAADVERLDLEALAEATARTGHPAIPLVKQLTAACGDAAG 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 101 -IIHLGATSCFVQDNADLIAYRDSIDHILKRFATVIDRLAAFSLKNKEVVTVGRTHYQTASLVTVGKRGVLWAQELLMAF 179
Cdd:cd01597  91 eYVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHR 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 180 QSLSEFRDKMRFRGIKGATGTQDSFltlfagdESKVEALDELVTKKANFSNRfLITGQTySRQQDSQLVFSLSLLGAAAK 259
Cdd:cd01597 171 ERLDELRPRVLVVQFGGAAGTLASL-------GDQGLAVQEALAAELGLGVP-AIPWHT-ARDRIAELASFLALLTGTLG 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 260 KVCTDIRVLQ--AFGELLEPFEKDQIGSSAMPYKKNPMKSERCCALSRKlinAPQEALTILA--DQGLERtlDDSAGR-- 333
Cdd:cd01597 242 KIARDVYLLMqtEIGEVAEPFAKGRGGSSTMPHKRNPVGCELIVALARR---VPGLAALLLDamVQEHER--DAGAWHae 316

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17508577 334 RMLIPDVLLTAEALLTTLQNIFEGLSVQTDNVKKIVEDEIAFLGLEKAMMMLTEEgVDRQQAHAVIRKTALEA 406
Cdd:cd01597 317 WIALPEIFLLASGALEQAEFLLSGLEVNEDRMRANLDLTGGLILSEAVMMALAPK-LGRQEAHDLVYEACMRA 388
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
 248-410 4.89e-39

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 140.93  E-value: 4.89e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  248 VFSLSLLGAAAKKVCTDIRVLQA--FGELLEPFEKDQIGSSAMPYKKNPMKSERCCALSRKLINAPQEALtILADQGLER 325
Cdd:PRK08937  20 EIVLALIATSLEKFANEIRLLQRseIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTAL-ENVPLWHER 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  326 TLDDSAGRRMLIPDVLLTAEALLTTLQNIFEGLSVQTDNVKKIVEDEIAFLGLEKAMMMLTEEGVDRQQAHAVIRKTALE 405
Cdd:PRK08937  99 DLSHSSAERIALPDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHELIREKAME 178


                 ....*
gi 17508577  406 AKQLQ 410
Cdd:PRK08937 179 AWKNQ 183
Lyase_I_like cd01594
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ...
 79-352 5.73e-33

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: 124.64  E-value: 5.73e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  79 KLKHDVMAHNHAFGKLCPTAAGIIH------LGATSCFVQDNADLIAYRDSIDHILKRFATVIDRLAAFSLKNKEVVTVG 152
Cdd:cd01594   8 ELAAALALVEEVLAGRAGELAGGLHgsalvhKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPG 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 153 RTHYQTASLVTVGKRGVLWAQELLMAFQSLSEFRDkmrfrgikgatgtqdsfltlfagdeskVEALDelvtkkanfsnrf 232
Cdd:cd01594  88 RTHLQDAQPVTLGYELRAWAQVLGRDLERLEEAAV---------------------------AEALD------------- 127

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 233 litgqtysrqqdsqlvfSLSLLGAAAKKVCTDIRVLQA--FGELLEPFEKDQIGSSAMPYKKNPMKSERCCALSRKLINA 310
Cdd:cd01594 128 -----------------ALALAAAHLSKIAEDLRLLLSgeFGELGEPFLPGQPGSSIMPQKVNPVAAELVRGLAGLVIGN 190

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 17508577 311 PQEALTILAdQGLERTLDDSAGRRMLIPDVLLTAEALLTTLQ 352
Cdd:cd01594 191 LVAVLTALK-GGPERDNEDSPSMREILADSLLLLIDALRLLL 231
Lyase_1 pfam00206
Lyase;
42-298 2.61e-15

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 76.64  E-value: 2.61e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577    42 AEAEKELGLKQVTQDAIDEMKSNRDVFDWPF---IRSEERKLKHDV-MAHNHAFGKLC---PTAAGIIHLGATSCFVQDN 114
Cdd:pfam00206  38 AAAKANVILKEEAAAIIKALDEVAEEGKLDDqfpLKVWQEGSGTAVnMNLNEVIGELLgqlVHPNDHVHTGQSSNDQVPT 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577   115 ADLIAYRDSI-DHILKRFATVIDRLAAFSLKNKEVVTVGRTHYQTASLVTVGKRGVLWAQELLMAFQSLSEFRDKMRFRG 193
Cdd:pfam00206 118 ALRLALKDALsEVLLPALRQLIDALKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLP 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577   194 IKGATGTqdsfltlFAGDESKVEaLDELVTKKANFsnrflITG----------QTYSRQQDSQLVFSLSLLGAAAKKVCT 263
Cdd:pfam00206 198 LGGGTAV-------GTGLNADPE-FAELVAKELGF-----FTGlpvkapnsfeATSDRDAVVELSGALALLATSLSKFAE 264

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 17508577   264 DIRVLQA--FGELLEPFEKDQIGSSAMPYKKNPMKSE 298
Cdd:pfam00206 265 DLRLLSSgpAGLVELSLAEGEPGSSIMPGKVNPDQLE 301
PRK09053 PRK09053
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 96-423 5.47e-14

3-carboxy-cis,cis-muconate cycloisomerase; Provisional


Pssm-ID: 181627 [Multi-domain]  Cd Length: 452  Bit Score: 73.90  E-value: 5.47e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577   96 PTAAGIIHLGATSCFVQDNADLIAYRDSIDHILKRFATVIDRLAAFSLKNKEVVTVGRTHYQTASLVTVGKRGVLWAQEL 175
Cdd:PRK09053  96 AEAARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDAL 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  176 LMAFQSLSEFRDKMRFRGIKGATGTQDSFltlfaGDESKV--EAL-DELvtkkanfsnRFLITGQTYSRQQDSQLVFS-- 250
Cdd:PRK09053 176 LRHRQRLAALRPRALVLQFGGAAGTLASL-----GEQALPvaQALaAEL---------QLALPALPWHTQRDRIAEFAsa 241

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  251 LSLLGAAAKKVCTDIRVLQA--FGELLEPFEKDQIGSSAMPYKKNPMKserCCALSRKLINAPQEALTILAD--QGLERT 326
Cdd:PRK09053 242 LGLLAGTLGKIARDVSLLMQteVGEVFEPAAAGKGGSSTMPHKRNPVG---CAAVLTAATRAPGLVATLFAAmpQEHERA 318

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  327 LDDSAGRRMLIPD-VLLTAEALLTTLQnIFEGLSVQTDNVKKIVeDEIAFLGLEKAMMMLTEEGVDRQQAHAVIRKTALE 405
Cdd:PRK09053 319 LGGWHAEWDTLPElACLAAGALAQMAQ-IVEGLEVDAARMRANL-DLTHGLILAEAVMLALADRIGRLDAHHLVEQASKR 396

                        330
                 ....*....|....*...
gi 17508577  406 AKQLQATqkvdIRQTMAD 423
Cdd:PRK09053 397 AVAEGRH----LRDVLAE 410
PurB cd01598
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ...
 39-330 5.04e-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: 64.56  E-value: 5.04e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  39 IWLAEAEKELGLKQVTQDAIDEMKSNRDVF---DWPFIRSEERKLKHDVMA---------HNHafgKLCPTAAGIIHLGA 106
Cdd:cd01598  23 IALSNLEEIPEVPPLTKEELKFLRAIIENFseeDALRIKEIEATTNHDVKAveyflkekfETL---GLLKKIKEFIHFAC 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 107 TScfvQD--NadlIAY----RDSIDHILK-RFATVIDRLAAFSLKNKEVVTVGRTHYQTASLVTVGKRGVLWAQELLMAF 179
Cdd:cd01598 100 TS---EDinN---LAYalmiKEARNEVILpLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQY 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577 180 QSLSEFRDKMRFrgiKGATGTqdsfltlFAGDESKVEALDELVTKKaNFSNRFLITGQTYSRQ---QD--SQLVFSLSLL 254
Cdd:cd01598 174 KQLKQIEILGKF---NGAVGN-------FNAHLVAYPDVDWRKFSE-FFVTSLGLTWNPYTTQiepHDyiAELFDALARI 242

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 17508577 255 GAAAKKVCTDIRVLQAFGELLEPFEKDQIGSSAMPYKKNPM---KSERCCALSRKLINAPQEALTIladQGLERTLDDS 330
Cdd:cd01598 243 NTILIDLCRDIWGYISLGYFKQKVKKGEVGSSTMPHKVNPIdfeNAEGNLGLSNALLNHLSAKLPI---SRLQRDLTDS 318
PRK05975 PRK05975
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 96-312 3.39e-10

3-carboxy-cis,cis-muconate cycloisomerase; Provisional


Pssm-ID: 168324 [Multi-domain]  Cd Length: 351  Bit Score: 61.61  E-value: 3.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577   96 PTAAGIIHLGATSCFVQDNADLIAYRDSIDHILKRFATVIDRLAAFSLKNKEVVTVGRTHYQTASLVTVGKRGVLWAQEL 175
Cdd:PRK05975  96 EEAAAHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPL 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  176 LMAFQSLSEFRDKMRFRGIKGATGTQDSFltlfagdESKVEALDELVTKKANfsnrfLITGQTYSRQQDSQLVFS--LSL 253
Cdd:PRK05975 176 LRHRDRLEALRADVFPLQFGGAAGTLEKL-------GGKAAAVRARLAKRLG-----LEDAPQWHSQRDFIADFAhlLSL 243

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17508577  254 LGAAAKKVCTDIRVL-QAFGELlepfekdQI----GSSAMPYKKNPMKSERCCALSRklINAPQ 312
Cdd:PRK05975 244 VTGSLGKFGQDIALMaQAGDEI-------SLsgggGSSAMPHKQNPVAAETLVTLAR--FNATQ 298
ADSL_C smart00998
Adenylosuccinate lyase C-terminus; Adenylosuccinate lyase catalyses two steps in the synthesis ...
 379-455 4.11e-08

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: 50.53  E-value: 4.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577    379 EKAMMMLTEEGVDRQQAHAVIRKTALEAkqlqATQKVDIRQT-MADPFFDSV--RDRVVGLVnNPINFTGRCVSQTESFI 455
Cdd:smart00998   7 ERVLLALVEKGLGREEAYELVQRAAMKA----WEEGKDLRELlLADPEVTAYlsEEELEELF-DPEYYLGHADAIVDRVL 81
PRK09285 PRK09285
adenylosuccinate lyase; Provisional
 9-166 1.96e-07

adenylosuccinate lyase; Provisional


Pssm-ID: 236452 [Multi-domain]  Cd Length: 456  Bit Score: 53.22  E-value: 1.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577    9 SVLSTRYC-KNSPLVSILSEtnkATLWRQ------LW-IWLAEAEKELGLKQVTQDAI---DEMKSNRDVFDWPFIRSEE 77
Cdd:PRK09285  10 SPLDGRYAsKTAALRPIFSE---FGLIRYrvqvevEWlIALAAHPGIPEVPPFSAEANaflRAIVENFSEEDAARIKEIE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577   78 RKLKHDV----------MAHNHAFGKlcptAAGIIHLGATScfvQD--NadlIAY----RDSIDH-ILKRFATVIDRLAA 140
Cdd:PRK09285  87 RTTNHDVkaveyflkekLAGLPELEA----VSEFIHFACTS---EDinN---LSHalmlKEAREEvLLPALRELIDALKE 156

                        170       180
                 ....*....|....*....|....*.
gi 17508577  141 FSLKNKEVVTVGRTHYQTASLVTVGK 166
Cdd:PRK09285 157 LAHEYADVPMLSRTHGQPATPTTLGK 182
PLN00134 PLN00134
fumarate hydratase; Provisional
 126-298 1.92e-06

fumarate hydratase; Provisional


Pssm-ID: 215069 [Multi-domain]  Cd Length: 458  Bit Score: 50.07  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  126 HILKRFATVIDRLAAFSLKNKEVVTVGRTHYQTASLVTVGKRGVLWAQELLMAFQSLSEFRDKMRFRGIKG-ATGTQdsf 204
Cdd:PLN00134 151 RLIPALKELHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGtAVGTG--- 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  205 LTLFAG-DESKVEALDE-----LVTKKanfsNRFlitgqTYSRQQDSQLVFSLSLLGAAAK--KVCTDIRVLQA-----F 271
Cdd:PLN00134 228 LNTKKGfDEKIAAAVAEetglpFVTAP----NKF-----EALAAHDAFVELSGALNTVAVSlmKIANDIRLLGSgprcgL 298

                        170       180
                 ....*....|....*....|....*..
gi 17508577  272 GELLEPfeKDQIGSSAMPYKKNPMKSE 298
Cdd:PLN00134 299 GELNLP--ENEPGSSIMPGKVNPTQCE 323
ADSL_C pfam10397
Adenylosuccinate lyase C-terminus; This is the C-terminal seven alpha helices of the structure ...
 379-454 7.55e-06

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: 43.94  E-value: 7.55e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17508577   379 EKAMMMLTEeGVDRQQAHAVIRKTALEAkqlQATQKVDIRQT-MADPFF-DSVRDRVVGLVnNPINFTGRCVSQTESF 454
Cdd:pfam10397   6 ERVLLALVK-GLGREEAHELVQEAAMKA---WEEGKNDLRELlAADPEVtYLSEEELDALF-DPAYYLGRADEIVDRV 78
PLN02848 PLN02848
adenylosuccinate lyase
 77-298 6.85e-05

adenylosuccinate lyase


Pssm-ID: 178440 [Multi-domain]  Cd Length: 458  Bit Score: 45.11  E-value: 6.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577   77 ERKLKHDVMAHNHAFGKLCPTAAGI------IHLGATSCFVQDNADLIAYRDSIDH-ILKRFATVIDRLAAFSLKNKEVV 149
Cdd:PLN02848  89 ERVTNHDVKAVEYFLKQKCKSHPELakvlefFHFACTSEDINNLSHALMLKEGVNSvVLPTMDEIIKAISSLAHEFAYVP 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  150 TVGRTHYQTASLVTVGKRGVLWAQELLMAFQSLSEFRDKMRFrgiKGATGTQDSFltLFAGDESKVEALDElvtkkaNFS 229
Cdd:PLN02848 169 MLSRTHGQPASPTTLGKEMANFAYRLSRQRKQLSEVKIKGKF---AGAVGNYNAH--MSAYPEVDWPAVAE------EFV 237

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  230 NRFLITGQTYSRQQDSQLVFSlSLLGAaakkvctdirvLQAFGELLEPFEKD-----------------QIGSSAMPYKK 292
Cdd:PLN02848 238 TSLGLTFNPYVTQIEPHDYMA-ELFNA-----------VSRFNNILIDFDRDiwsyislgyfkqitkagEVGSSTMPHKV 305


                 ....*.
gi 17508577  293 NPMKSE 298
Cdd:PLN02848 306 NPIDFE 311
PRK00855 PRK00855
argininosuccinate lyase; Provisional
 121-192 1.05e-04

argininosuccinate lyase; Provisional


Pssm-ID: 179143 [Multi-domain]  Cd Length: 459  Bit Score: 44.76  E-value: 1.05e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 17508577  121 RDSIDHILKRFATVIDRLAAFSLKNKEVVTVGRTHYQTASLVTVGkrgvLWaqelLMA-FQSLSefRDKMRFR 192
Cdd:PRK00855 124 RDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFG----HH----LLAyAEMLA--RDLERLR 186
PRK13353 PRK13353
aspartate ammonia-lyase; Provisional
 126-381 1.20e-04

aspartate ammonia-lyase; Provisional


Pssm-ID: 183992 [Multi-domain]  Cd Length: 473  Bit Score: 44.59  E-value: 1.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  126 HILKRFATVIDRLA-AFSLKNKE---VVTVGRTHYQTASLVTVGKRGVLWAQELLMAFQSLSEFRDKMRFRGIKG-ATGT 200
Cdd:PRK13353 155 NLLEGLLAAMGALQdVFEEKAAEfdhVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGtAVGT 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  201 ----QDSFLTLFAGDESKVEALDelVTKKANfsnrfLItgqtYSRQQ-DSQLVFSLSLLGAAAK--KVCTDIRVLQA--- 270
Cdd:PRK13353 235 glnaDPEYIERVVKHLAAITGLP--LVGAED-----LV----DATQNtDAFVEVSGALKVCAVNlsKIANDLRLLSSgpr 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17508577  271 --FGELLEPfeKDQIGSSAMPYKKNPMKSErccalsrkLINapQEALTILA-DQGLerTLDDSAGRRML------IPDVL 341
Cdd:PRK13353 304 tgLGEINLP--AVQPGSSIMPGKVNPVMPE--------VVN--QIAFQVIGnDVTI--TLAAEAGQLELnvmepvIAFNL 369

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 17508577  342 LTAEALLTTLQNIF-----EGLSVQTDNVKKIVEDEIA-------FLGLEKA 381
Cdd:PRK13353 370 LESISILTNACRAFtdncvKGIEANEERCKEYVEKSVGiatalnpHIGYEAA 421
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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