Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad1c3ca_ All alpha proteins L-aspartase-like L-aspartase-like L-aspartase/fumarase Adenylosuccinate lyase (Thermotoga maritima ) [TaxId: 2336 ], SCOPe (2.08)
Bd1c3cb_ All alpha proteins L-aspartase-like L-aspartase-like L-aspartase/fumarase Adenylosuccinate lyase (Thermotoga maritima ) [TaxId: 2336 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2 FamilyL-aspartase/fumarase8026461 4001433 SCOP2 (2022-06-29)
ASCOP2 SuperfamilyL-aspartase-like8038840 3001572 SCOP2 (2022-06-29)
BSCOP2B SuperfamilyL-aspartase-like8038840 3001572 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
AAdenylsuccinate_lyase_1e1c3cA3 A: alpha arraysX: L-aspartase N-terminal domain-like (From Topology)H: L-aspartase N-terminal domain-like (From Topology)T: L-aspartase N-terminal domain-likeF: Adenylsuccinate_lyase_1ECOD (1.6)
AADSL_Ce1c3cA2 A: alpha arraysX: L-aspartase C-terminal domain-like (From Homology)H: L-aspartase C-terminal domain-likeT: L-aspartase C-terminal domain-likeF: ADSL_CECOD (1.6)
ALyase_1_Ce1c3cA1 A: alpha arraysX: L-aspartase middle domain-likeH: L-aspartase middle domain-like (From Topology)T: L-aspartase middle domain-likeF: Lyase_1_CECOD (1.6)
BAdenylsuccinate_lyase_1e1c3cB3 A: alpha arraysX: L-aspartase N-terminal domain-like (From Topology)H: L-aspartase N-terminal domain-like (From Topology)T: L-aspartase N-terminal domain-likeF: Adenylsuccinate_lyase_1ECOD (1.6)
BADSL_Ce1c3cB2 A: alpha arraysX: L-aspartase C-terminal domain-like (From Homology)H: L-aspartase C-terminal domain-likeT: L-aspartase C-terminal domain-likeF: ADSL_CECOD (1.6)
BLyase_1_Ce1c3cB1 A: alpha arraysX: L-aspartase middle domain-likeH: L-aspartase middle domain-like (From Topology)T: L-aspartase middle domain-likeF: Lyase_1_CECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
A, B
PF00206Lyase (Lyase_1)Lyase- Domain
A, B
PF10397Adenylosuccinate lyase C-terminus (ADSL_C)Adenylosuccinate lyase C-terminusThis 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 [1], Adenylosuccinate lyase cata ...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 [1], Adenylosuccinate lyase catalyses 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 [2].
Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

ChainsPolymerMolecular FunctionBiological ProcessCellular Component
A, B
PROTEIN (ADENYLOSUCCINATE LYASE)

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

ChainsEnzyme NameDescriptionCatalytic Residues
A, B
adenylosuccinate lyase  M-CSA #80

Adenylosuccinate lyase catalyses two similar but separate reactions in the de novo purine synthesis pathway. In the first reaction is converts 5-aminoimidazole-(N-succinylcarboxyamide) ribotide into 5-aminoimidazole-4-carboxyamide ribotide in the ninth step of the synthesis of inosine monophosphate. In the second reaction the enzyme converts adenylosuccinate into adenosine monophospate which occurs four steps after the first reaction. Adenylosuccinate lyase helps provide the majority of purine nucleotides required for DNA replication as well as playing a role in cellular metabolism as an enzyme in the purine nucleotide cycle. The purine nucleotide cycle controls both the amounts of available citric acid intermediates and the amount of free AMP. Mutations in the enzyme leads to severe clinical consequences including mental retardation with autistic features.

Defined by 6 residues: HIS:A_2-67 [auth A_2-68]THR:A-139 [auth A-140]HIS:A-140 [auth A-141]SER:B-262 [auth B-263]LYS:B-267 [auth B-268]GLU:B-274 [auth B-275]
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