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

ChainsDomain InfoClassFoldSuperfamilyFamilyDomainSpeciesProvenance Source (Version)
Ad1al6a_ All alpha proteins Citrate synthase Citrate synthase Citrate synthase Citrate synthase (Gallus gallus ) [TaxId: 9031 ], SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

ChainsTypeFamily Name Domain Identifier Family IdentifierProvenance Source (Version)
ASCOP2B SuperfamilyCitrate synthase 8038420 3001050 SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

ChainsFamily NameDomain Identifier ArchitecturePossible HomologyHomologyTopologyFamilyProvenance Source (Version)
ACitrate_synte1al6A1 A: alpha complex topologyX: Citrate synthase-likeH: Citrate synthase (From Topology)T: Citrate synthaseF: Citrate_syntECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

ChainDomainClassArchitectureTopologyHomologyProvenance Source (Version)
A1.10.580.10 Mainly Alpha Orthogonal Bundle Citrate Synthase domain 1CATH (4.3.0)
A1.10.230.10 Mainly Alpha Orthogonal Bundle Cytochrome p450-Terp domain 2CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

ChainsAccessionNameDescriptionCommentsSource
PF00285Citrate synthase, C-terminal domain (Citrate_synt)Citrate synthase, C-terminal domainThis is the long, C-terminal part of the enzyme.Domain

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

ChainsEnzyme NameDescriptionCatalytic Residues
citrate (Si)-synthase  M-CSA #78

Citrate synthase catalyses the condensation between the carbonyl of oxaloacetate and the acetyl methyl group of acetyl CoA. A reaction considered to be the first step in the citric acid cycle (Krebs cycle) proper.

The product of this reaction, citryl-CoA, remains tightly bound to the enzyme and is hydrolysed to citrate and CoA in a separate chemical step that nevertheless uses the same catalytic residues. Conformational changes of the enzyme during the reaction are believed to be important in the catalytic mechanism.

Although most studies have been done on pig citrate synthase, but the structural equivalence of the amino acid residues implicated in catalysis for the Pyrococcus protein implies that the mechanism proceeds via the same acid/base catalytic process.

Defined by 5 residues: SER:A-244HIS:A-274HIS:A-320ARG:A-329ASP:A-375
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