6QCL

Citryl-CoA lyase core module of Chlorobium limicola ATP citrate lyase in complex with acetyl-CoA and L-malate

External Resource: Annotation

Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	Citrate_synt	e6qclB1	A: alpha complex topology	X: Citrate synthase-like	H: Citrate synthase (From Topology)	T: Citrate synthase	F: Citrate_synt	ECOD (1.6)
C	Citrate_synt	e6qclC1	A: alpha complex topology	X: Citrate synthase-like	H: Citrate synthase (From Topology)	T: Citrate synthase	F: Citrate_synt	ECOD (1.6)
D	Citrate_synt	e6qclD1	A: alpha complex topology	X: Citrate synthase-like	H: Citrate synthase (From Topology)	T: Citrate synthase	F: Citrate_synt	ECOD (1.6)
E	Citrate_synt	e6qclE1	A: alpha complex topology	X: Citrate synthase-like	H: Citrate synthase (From Topology)	T: Citrate synthase	F: Citrate_synt	ECOD (1.6)
A	Citrate_synt	e6qclA1	A: alpha complex topology	X: Citrate synthase-like	H: Citrate synthase (From Topology)	T: Citrate synthase	F: Citrate_synt	ECOD (1.6)
F	Citrate_synt	e6qclF1	A: alpha complex topology	X: Citrate synthase-like	H: Citrate synthase (From Topology)	T: Citrate synthase	F: Citrate_synt	ECOD (1.6)
G	Citrate_synt	e6qclG1	A: alpha complex topology	X: Citrate synthase-like	H: Citrate synthase (From Topology)	T: Citrate synthase	F: Citrate_synt	ECOD (1.6)
H	Citrate_synt	e6qclH1	A: alpha complex topology	X: Citrate synthase-like	H: Citrate synthase (From Topology)	T: Citrate synthase	F: Citrate_synt	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D, E A, B, C, D, E, F, G, H	PF00285	Citrate synthase, C-terminal domain (Citrate_synt)	Citrate synthase, C-terminal domain	This is the long, C-terminal part of the enzyme.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D, E A, B, C, D, E, F, G, H	ATP-citrate lyase alpha-subunit	binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding binding adenyl ribonucleotide binding nucleotide binding purine ribonucleotide binding purine ribonucleoside triphosphate binding nucleoside phosphate binding ion binding purine nucleotide binding organic cyclic compound binding anion binding adenyl nucleotide binding ATP binding heterocyclic compound binding carbohydrate derivative binding ribonucleotide binding small molecule binding ATP citrate synthase activity acyltransferase activity acyltransferase activity, acyl groups converted into alkyl on transfer transferase activity catalytic activity lyase activity cation binding metal ion binding	aerobic respiration cellular respiration tricarboxylic acid cycle energy derivation by oxidation of organic compounds metabolic process cellular process primary metabolic process generation of precursor metabolites and energy fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process carboxylic acid metabolic process lipid biosynthetic process aerobic respiration cellular respiration tricarboxylic acid cycle energy derivation by oxidation of organic compounds metabolic process cellular process primary metabolic process generation of precursor metabolites and energy fatty acid metabolic process monocarboxylic acid biosynthetic process small molecule biosynthetic process oxoacid metabolic process carboxylic acid metabolic process lipid biosynthetic process organic acid biosynthetic process organic acid metabolic process fatty acid biosynthetic process carboxylic acid biosynthetic process biosynthetic process small molecule metabolic process monocarboxylic acid metabolic process lipid metabolic process thioester biosynthetic process acetyl-CoA metabolic process nucleobase-containing compound metabolic process acyl-CoA metabolic process nucleobase-containing small molecule metabolic process purine-containing compound biosynthetic process acyl-CoA biosynthetic process phosphate-containing compound metabolic process sulfur compound metabolic process amide metabolic process thioester metabolic process phosphorus metabolic process nucleoside phosphate metabolic process amide biosynthetic process nucleobase-containing compound biosynthetic process purine-containing compound metabolic process acetyl-CoA biosynthetic process sulfur compound biosynthetic process organophosphate metabolic process organophosphate biosynthetic process nucleoside phosphate biosynthetic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D, E A, B, C, D, E, F, G, H	IPR016102	Succinyl-CoA synthetase-like	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR016143	Citrate synthase-like, small alpha subdomain	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR003781	CoA-binding	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR036969	Citrate synthase superfamily	Homologous Superfamily
A, B, C, D, E A, B, C, D, E, F, G, H	IPR005811	ATP-citrate synthase/succinyl-CoA ligase, C-terminal domain	Domain
A, B, C, D, E A, B, C, D, E, F, G, H	IPR002020	Citrate synthase	Family
A, B, C, D, E A, B, C, D, E, F, G, H	IPR016142	Citrate synthase-like, large alpha subdomain	Homologous Superfamily

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM157729.