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Conserved domains on  [gi|2506507536|ref|WP_282871462|]
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adenylosuccinate lyase [Streptomyces albus]

Protein Classification

lyase family protein( domain architecture ID 97)

lyase family protein belongs to a superfamily of enzymes that catalyze beta-elimination reactions in which a C-N or C-O bond is cleaved and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits

CATH:  1.20.200.10
EC:  4.-.-.-
SCOP:  3001572

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Lyase_I_like super family cl00013
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ...
26-313 1.56e-59

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.


The actual alignment was detected with superfamily member cd03302:

Pssm-ID: 469578 [Multi-domain]  Cd Length: 436  Bit Score: 197.15  E-value: 1.56e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536  26 LACEYASPRIAAIWSPRTQVVLERRLWLTVLRAQHAEGLRVPDQVFRDYARAVDRVDLASIRRREHATRHDLKARIEEFN 105
Cdd:cd03302     1 LASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLDISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536 106 ALAG--HQHIHKGLTSCDITDNIAQTRVRMSLRHLRSRAAVLARAAGAETGGAATGAVLGSA------------------ 165
Cdd:cd03302    81 LLCPaaAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFThyqpaqlttvgkraclwi 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536 166 ------AAALDALLERYPLRGLKGPVGTAQDMLDLLGGDRAALARIEERVAAHLGFPRVLRSVGQLYFRSLDYEVLSSLS 239
Cdd:cd03302   161 qdllmdLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVYPVTGQTYSRKVDIDVLNALS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536 240 EFAARAGSLV--------------PAAPGE-GRDT----RGPVRS-----FAVLLRGYTAMAAQLAGEQWNEGDVSCSVV 295
Cdd:cd03302   241 SLGATAHKIAtdirllanlkeveePFEKGQiGSSAmpykRNPMRSerccsLARHLMNLASNAAQTASTQWFERTLDDSAN 320
                         330
                  ....*....|....*...
gi 2506507536 296 RRIALPGACYAADATLNT 313
Cdd:cd03302   321 RRIAIPEAFLAADAILIT 338
 
Name Accession Description Interval E-value
Adenylsuccinate_lyase_2 cd03302
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ...
26-313 1.56e-59

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: 197.15  E-value: 1.56e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536  26 LACEYASPRIAAIWSPRTQVVLERRLWLTVLRAQHAEGLRVPDQVFRDYARAVDRVDLASIRRREHATRHDLKARIEEFN 105
Cdd:cd03302     1 LASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLDISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536 106 ALAG--HQHIHKGLTSCDITDNIAQTRVRMSLRHLRSRAAVLARAAGAETGGAATGAVLGSA------------------ 165
Cdd:cd03302    81 LLCPaaAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFThyqpaqlttvgkraclwi 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536 166 ------AAALDALLERYPLRGLKGPVGTAQDMLDLLGGDRAALARIEERVAAHLGFPRVLRSVGQLYFRSLDYEVLSSLS 239
Cdd:cd03302   161 qdllmdLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVYPVTGQTYSRKVDIDVLNALS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536 240 EFAARAGSLV--------------PAAPGE-GRDT----RGPVRS-----FAVLLRGYTAMAAQLAGEQWNEGDVSCSVV 295
Cdd:cd03302   241 SLGATAHKIAtdirllanlkeveePFEKGQiGSSAmpykRNPMRSerccsLARHLMNLASNAAQTASTQWFERTLDDSAN 320
                         330
                  ....*....|....*...
gi 2506507536 296 RRIALPGACYAADATLNT 313
Cdd:cd03302   321 RRIAIPEAFLAADAILIT 338
PurB COG0015
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ...
30-319 4.97e-31

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: 121.34  E-value: 4.97e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536  30 YASPRIAAIWSPRTQVVLERRLWLTVLRAQHAEGLrVPDQVFRDYARAVD--RVDLASIRRREHATRHDLKARIEEFNAL 107
Cdd:COG0015     6 YASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGL-IPAEAAAAIRAAADdfEIDAERIKEIEKETRHDVKAFVYALKEK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536 108 AG---HQHIHKGLTSCDITDNIAQTRVRMSLRHLRSRAAVLARAAGAETGGAATGAVLG--------------------- 163
Cdd:COG0015    85 VGaeaGEYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGrthgqhaepttfgkklavwaa 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536 164 ---SAAAALDALLERYPLRGLKGPVGTAQDMLDllggdraALARIEERVAAHLGFpRVLRSVGQLYFRSLDYEVLSSLSE 240
Cdd:COG0015   165 ellRQLERLEEARERVLVGKIGGAVGTYAAHGE-------AWPEVEERVAEKLGL-KPNPVTTQIEPRDRHAELFSALAL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536 241 FAARAGSLV----------------PAAPGEGrdtrG---------PVRS-----FAVLLRGYtAMAAQLAGEQWNEGDV 290
Cdd:COG0015   237 IAGSLEKIArdirllqrtevgeveePFAKGQV----GssamphkrnPIDSeniegLARLARAL-AAALLEALASWHERDL 311
                         330       340
                  ....*....|....*....|....*....
gi 2506507536 291 SCSVVRRIALPGACYAADATLNTVERALG 319
Cdd:COG0015   312 SDSSVERNILPDAFLLLDGALERLLKLLE 340
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
265-313 9.12e-10

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 57.73  E-value: 9.12e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2506507536 265 SFAVLLRGYTAMAAQLAgEQWNEGDVSCSVVRRIALPGACYAADATLNT 313
Cdd:PRK08937   76 GLARVLRSYLVTALENV-PLWHERDLSHSSAERIALPDAFLALDYILNR 123
 
Name Accession Description Interval E-value
Adenylsuccinate_lyase_2 cd03302
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ...
26-313 1.56e-59

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: 197.15  E-value: 1.56e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536  26 LACEYASPRIAAIWSPRTQVVLERRLWLTVLRAQHAEGLRVPDQVFRDYARAVDRVDLASIRRREHATRHDLKARIEEFN 105
Cdd:cd03302     1 LASRYASKEMVYIFSPRKKFSTWRKLWLWLAEAEKELGLDISDEQIEEMKANVENIDFEIAAAEEKKLRHDVMAHVHAFG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536 106 ALAG--HQHIHKGLTSCDITDNIAQTRVRMSLRHLRSRAAVLARAAGAETGGAATGAVLGSA------------------ 165
Cdd:cd03302    81 LLCPaaAGIIHLGATSCFVTDNTDLIQIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFThyqpaqlttvgkraclwi 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536 166 ------AAALDALLERYPLRGLKGPVGTAQDMLDLLGGDRAALARIEERVAAHLGFPRVLRSVGQLYFRSLDYEVLSSLS 239
Cdd:cd03302   161 qdllmdLRNLERLRDDLRFRGVKGTTGTQASFLDLFEGDHDKVEALDELVTKKAGFKKVYPVTGQTYSRKVDIDVLNALS 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536 240 EFAARAGSLV--------------PAAPGE-GRDT----RGPVRS-----FAVLLRGYTAMAAQLAGEQWNEGDVSCSVV 295
Cdd:cd03302   241 SLGATAHKIAtdirllanlkeveePFEKGQiGSSAmpykRNPMRSerccsLARHLMNLASNAAQTASTQWFERTLDDSAN 320
                         330
                  ....*....|....*...
gi 2506507536 296 RRIALPGACYAADATLNT 313
Cdd:cd03302   321 RRIAIPEAFLAADAILIT 338
PurB COG0015
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ...
30-319 4.97e-31

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: 121.34  E-value: 4.97e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536  30 YASPRIAAIWSPRTQVVLERRLWLTVLRAQHAEGLrVPDQVFRDYARAVD--RVDLASIRRREHATRHDLKARIEEFNAL 107
Cdd:COG0015     6 YASPEMRAIFSEEAKIRAWLDVEIALAEAQAELGL-IPAEAAAAIRAAADdfEIDAERIKEIEKETRHDVKAFVYALKEK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536 108 AG---HQHIHKGLTSCDITDNIAQTRVRMSLRHLRSRAAVLARAAGAETGGAATGAVLG--------------------- 163
Cdd:COG0015    85 VGaeaGEYIHFGATSQDINDTALALQLREALELLLPDLDALIAALAELAEEHKDTPMLGrthgqhaepttfgkklavwaa 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536 164 ---SAAAALDALLERYPLRGLKGPVGTAQDMLDllggdraALARIEERVAAHLGFpRVLRSVGQLYFRSLDYEVLSSLSE 240
Cdd:COG0015   165 ellRQLERLEEARERVLVGKIGGAVGTYAAHGE-------AWPEVEERVAEKLGL-KPNPVTTQIEPRDRHAELFSALAL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536 241 FAARAGSLV----------------PAAPGEGrdtrG---------PVRS-----FAVLLRGYtAMAAQLAGEQWNEGDV 290
Cdd:COG0015   237 IAGSLEKIArdirllqrtevgeveePFAKGQV----GssamphkrnPIDSeniegLARLARAL-AAALLEALASWHERDL 311
                         330       340
                  ....*....|....*....|....*....
gi 2506507536 291 SCSVVRRIALPGACYAADATLNTVERALG 319
Cdd:COG0015   312 SDSSVERNILPDAFLLLDGALERLLKLLE 340
Adenylsuccinate_lyase_like cd01595
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ...
35-313 2.33e-22

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: 96.42  E-value: 2.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536  35 IAAIWSPRTQVVLERRLWLTVLRAQHAEGLrVPDQVFRDYARAVD--RVDLASIRRREHATRHDLKARIEEFNALAG--- 109
Cdd:cd01595     1 MRAIFSEENKLRTWLDVEAALAEAQAELGL-IPKEAAEEIRAAADvfEIDAERIAEIEKETGHDVIAFVYALAEKCGeda 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536 110 HQHIHKGLTSCDITDNIAQTRVRMSLRHLRSRAAVLARAAGAETGGAATGAVLG------------------------SA 165
Cdd:cd01595    80 GEYVHFGATSQDINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGrthgqhalpttfgkkfavwaaellRH 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536 166 AAALDALLERYPLRGLKGPVGTAQDMLDllggdraALARIEERVAAHLGFPRVLRSvGQLYFRSLDYEVLSSLSEFAARA 245
Cdd:cd01595   160 LERLEEARERVLVGGISGAVGTHASLGP-------KGPEVEERVAEKLGLKVPPIT-TQIEPRDRIAELLSALALIAGTL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536 246 GSL----------------VPAAPGE-GRDT----RGPVRS-----FAVLLRGYTAMAAQlAGEQWNEGDVSCSVVRRIA 299
Cdd:cd01595   232 EKIatdirllqrteigeveEPFEKGQvGSSTmphkRNPIDSeniegLARLVRALAAPALE-NLVQWHERDLSDSSVERNI 310
                         330
                  ....*....|....
gi 2506507536 300 LPGACYAADATLNT 313
Cdd:cd01595   311 LPDAFLLLDAALSR 324
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
265-313 9.12e-10

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 57.73  E-value: 9.12e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2506507536 265 SFAVLLRGYTAMAAQLAgEQWNEGDVSCSVVRRIALPGACYAADATLNT 313
Cdd:PRK08937   76 GLARVLRSYLVTALENV-PLWHERDLSHSSAERIALPDAFLALDYILNR 123
Adenylsuccinate_lyase_1 cd01360
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ...
30-124 2.60e-06

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: 48.70  E-value: 2.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2506507536  30 YASPRIAAIWSPRTQVvlerRLWLTV----LRAQHAEGLrVPDQVFRDYARAVDrVDLASIRRREHATRHDLKA---RIE 102
Cdd:cd01360     2 YGRPEMKKIWSEENKF----RKWLEVeaavCEAWAKLGV-IPAEAAEEIRKKAK-FDVERVKEIEAETKHDVIAfvtAIA 75
                          90       100
                  ....*....|....*....|..
gi 2506507536 103 EFNALAGhQHIHKGLTSCDITD 124
Cdd:cd01360    76 EYCGEAG-RYIHFGLTSSDVVD 96
 
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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