4H6Q

Structure of oxidized Deinococcus radiodurans proline dehydrogenase complexed with L-tetrahydrofuroic acid

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 [auth C]	Pro_dh	e4h6qC2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Pro_dh	ECOD (1.6)
A	Pro_dh	e4h6qA1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Pro_dh	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B [auth C]	3.20.20.220	Alpha Beta	Alpha-Beta Barrel	TIM Barrel		CATH (4.3.0)
A	3.20.20.220	Alpha Beta	Alpha-Beta Barrel	TIM Barrel		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B [auth C]	PF01619	Proline dehydrogenase (Pro_dh)	Proline dehydrogenase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B [auth C]	Proline dehydrogenase	oxidoreductase activity oxidoreductase activity, acting on the CH-NH group of donors proline dehydrogenase activity catalytic activity oxidoreductase activity, acting on the CH-NH group of donors, quinone or similar compound as acceptor FAD binding flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding oxidoreductase activity oxidoreductase activity, acting on the CH-NH group of donors proline dehydrogenase activity catalytic activity oxidoreductase activity, acting on the CH-NH group of donors, quinone or similar compound as acceptor FAD binding flavin adenine dinucleotide binding binding nucleoside phosphate binding ion binding organic cyclic compound binding anion binding nucleotide binding heterocyclic compound binding small molecule binding	catabolic process oxoacid metabolic process glutamine family amino acid catabolic process amino acid metabolic process organic acid metabolic process organic acid catabolic process proline catabolic process alpha-amino acid metabolic process glutamine family amino acid metabolic process cellular catabolic process proline metabolic process carboxylic acid catabolic process glutamate metabolic process small molecule metabolic process catabolic process oxoacid metabolic process glutamine family amino acid catabolic process amino acid metabolic process organic acid metabolic process organic acid catabolic process proline catabolic process alpha-amino acid metabolic process glutamine family amino acid metabolic process cellular catabolic process proline metabolic process carboxylic acid catabolic process glutamate metabolic process small molecule metabolic process amino acid catabolic process proline catabolic process to glutamate dicarboxylic acid metabolic process carboxylic acid metabolic process L-amino acid catabolic process primary metabolic process L-amino acid metabolic process proteinogenic amino acid metabolic process alpha-amino acid catabolic process proteinogenic amino acid catabolic process metabolic process cellular process small molecule catabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B [auth C]	IPR002872	Proline dehydrogenase domain	Domain
A, B [auth C]	IPR029041	FAD-linked oxidoreductase-like	Homologous Superfamily
A, B [auth C]	IPR015659	Proline oxidase family	Family
A, B [auth C]	IPR008219	Proline dehydrogenase, bacteria and archaea	Family

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.