Annotations: 3HAZ

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Pro_dh	e3hazA9	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Pro_dh	ECOD (1.6)
A	Aldedh_2nd	e3hazA5	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_2nd	ECOD (1.6)
A	Aldedh_1st_1	e3hazA4	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_1st_1	ECOD (1.6)
A	Pro_dh-DNA_bdg	e3hazA1	A: extended segments	X: N-terminal domain of bifunctional PutA protein (From Topology)	H: N-terminal domain of bifunctional PutA protein (From Topology)	T: N-terminal domain of bifunctional PutA protein	F: Pro_dh-DNA_bdg	ECOD (1.6)
B	Pro_dh	e3hazB3	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Pro_dh	ECOD (1.6)
B	Aldedh_2nd	e3hazB4	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_2nd	ECOD (1.6)
B	Aldedh_1st_1	e3hazB5	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: Aldedh_1st_1	ECOD (1.6)
B	Pro_dh-DNA_bdg	e3hazB1	A: extended segments	X: N-terminal domain of bifunctional PutA protein (From Topology)	H: N-terminal domain of bifunctional PutA protein (From Topology)	T: N-terminal domain of bifunctional PutA protein	F: Pro_dh-DNA_bdg	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00171	Aldehyde dehydrogenase family (Aldedh)	Aldehyde dehydrogenase family	-	Family
A, B	PF01619	Proline dehydrogenase (Pro_dh)	Proline dehydrogenase	-	Family
A, B	PF14850	DNA-binding domain of Proline dehydrogenase (Pro_dh-DNA_bdg)	DNA-binding domain of Proline dehydrogenase	This domain lies at the N-terminus of bifunctional proline-dehydrogenases and is found to bind DNA.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Proline dehydrogenase	DNA binding binding organic cyclic compound binding nucleic acid binding 1-pyrroline-5-carboxylate dehydrogenase activity oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors catalytic activity oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor nucleoside phosphate binding nucleotide binding heterocyclic compound binding small molecule binding oxidoreductase activity, acting on the CH-NH group of donors DNA binding binding organic cyclic compound binding nucleic acid binding 1-pyrroline-5-carboxylate dehydrogenase activity oxidoreductase activity oxidoreductase activity, acting on the aldehyde or oxo group of donors catalytic activity oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor nucleoside phosphate binding nucleotide binding heterocyclic compound binding small molecule binding oxidoreductase activity, acting on the CH-NH group of donors proline dehydrogenase activity oxidoreductase activity, acting on the CH-NH group of donors, quinone or similar compound as acceptor transcription regulator activity DNA-binding transcription factor activity identical protein binding protein 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 glutamine family amino acid biosynthetic process organic acid biosynthetic process carboxylic acid biosynthetic process proline biosynthetic process small molecule biosynthetic process L-amino acid biosynthetic process amino acid biosynthetic process biosynthetic process proteinogenic amino acid biosynthetic process alpha-amino acid biosynthetic process	cell periphery cellular anatomical structure cytoplasmic side of plasma membrane cytoplasmic side of membrane membrane plasma membrane side of membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR002872	Proline dehydrogenase domain	Domain
A, B	IPR015590	Aldehyde dehydrogenase domain	Domain
A, B	IPR016161	Aldehyde/histidinol dehydrogenase	Homologous Superfamily
A, B	IPR029041	FAD-linked oxidoreductase-like	Homologous Superfamily
A, B	IPR016162	Aldehyde dehydrogenase, N-terminal	Homologous Superfamily
A, B	IPR050485	Proline metabolism enzyme	Family
A, B	IPR025703	Bifunctional protein PutA	Family
A, B	IPR024089	Proline dehydrogenase PutA, domain I/II	Homologous Superfamily
A, B	IPR016163	Aldehyde dehydrogenase, C-terminal	Homologous Superfamily
A, B	IPR016160	Aldehyde dehydrogenase, cysteine active site	Conserved Site
A, B	IPR005933	Bifunctional protein PutA, C-terminal domain	Domain
A, B	IPR024082	Proline dehydrogenase PutA, domain II	Domain

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.