2HJ0

Crystal Structure of the Putative Alfa Subunit of Citrate Lyase in Complex with Citrate from Streptococcus mutans, Northeast Structural Genomics Target SmR12 .

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
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	CitF	e2hj0B2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NagB/RpiA/CoA transferase-like	F: CitF	ECOD (1.6)
A	CitF	e2hj0A2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NagB/RpiA/CoA transferase-like	F: CitF	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.1080.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaconate Coenzyme A-transferase	Glutaconate Coenzyme A-transferase	CATH (4.3.0)
A	3.40.1080.10	Alpha Beta	3-Layer(aba) Sandwich	Glutaconate Coenzyme A-transferase	Glutaconate Coenzyme A-transferase	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF04223	Citrate lyase, alpha subunit (CitF) (CitF)	Citrate lyase, alpha subunit (CitF)	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Putative citrate lyase, alfa subunit	oxo-acid-lyase activity lyase activity catalytic activity citrate (pro-3S)-lyase activity carbon-carbon lyase activity citrate CoA-transferase activity transferase activity, transferring sulphur-containing groups transferase activity CoA-transferase activity	ribose phosphate metabolic process nucleoside bisphosphate metabolic process purine nucleoside bisphosphate metabolic process ribonucleoside bisphosphate metabolic process carbohydrate derivative metabolic process acetyl-CoA metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process organic substance metabolic process acyl-CoA metabolic process ribonucleotide metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process small molecule metabolic process ribose phosphate metabolic process nucleoside bisphosphate metabolic process purine nucleoside bisphosphate metabolic process ribonucleoside bisphosphate metabolic process carbohydrate derivative metabolic process acetyl-CoA metabolic process nucleobase-containing compound metabolic process purine nucleotide metabolic process organic substance metabolic process acyl-CoA metabolic process ribonucleotide metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process small molecule metabolic process sulfur compound metabolic process amide metabolic process thioester metabolic process phosphorus metabolic process nucleoside phosphate metabolic process organonitrogen compound metabolic process cellular metabolic process primary metabolic process nucleotide metabolic process purine-containing compound metabolic process organic cyclic compound metabolic process organophosphate metabolic process metabolic process cellular process purine ribonucleotide metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity protein-containing complex catalytic complex ATP-independent citrate lyase complex intracellular protein-containing complex

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR006472	Citrate lyase, alpha subunit	Family
A, B	IPR037171	NagB/RpiA transferase-like	Homologous Superfamily

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.