5UR2

Crystal structure of proline utilization A (PutA) from Bdellovibrio bacteriovorus inactivated by N-propargylglycine

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)
A	Pro_dh	e5ur2A2	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	e5ur2A3	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	e5ur2A4	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	EUF08776	e5ur2A1	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: EUF08776	ECOD (1.6)
B	Pro_dh	e5ur2B4	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	e5ur2B2	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	e5ur2B3	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	EUF08776	e5ur2B1	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: EUF08776	ECOD (1.6)
C	Pro_dh	e5ur2C2	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Pro_dh	ECOD (1.6)
C	Aldedh_2nd	e5ur2C3	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)
C	Aldedh_1st_1	e5ur2C4	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)
C	EUF08776	e5ur2C1	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: EUF08776	ECOD (1.6)
D	Pro_dh	e5ur2D1	A: a/b barrels	X: TIM beta/alpha-barrel	H: TIM barrels (From Topology)	T: TIM barrels	F: Pro_dh	ECOD (1.6)
D	Aldedh_2nd	e5ur2D2	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)
D	Aldedh_1st_1	e5ur2D3	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)
D	EUF08776	e5ur2D4	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: EUF08776	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF00171	Aldehyde dehydrogenase family (Aldedh)	Aldehyde dehydrogenase family	-	Family
A, B, C, D	PF01619	Proline dehydrogenase (Pro_dh)	Proline dehydrogenase	-	Family
A, B, C, D	PF18083	Proline utilization A N-terminal domain (PutA_N)	Proline utilization A N-terminal domain	This domain is found in Proline utilization A (PutA) proteins present in Geobacter sulfurreducens. PutA are bifunctional peripheral membrane flavoenzymes that catalyze the oxidation of l-proline to l-glutamate and couple the oxidation of imported pro ...	This domain is found in Proline utilization A (PutA) proteins present in Geobacter sulfurreducens. PutA are bifunctional peripheral membrane flavoenzymes that catalyze the oxidation of l-proline to l-glutamate and couple the oxidation of imported proline imported to the reduction of membrane-associated quinones. This domain is located at the N-terminus and is referred to as the alpha domain. The hydrocarbon tail of Zwittergent 3-12 binds to an exposed hydrophobic patch of the alpha domain which contains aromatic and nonpolar residues. The domain may be involved in membrane association [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Bifunctional protein PutA	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 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	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	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, C, D	IPR002872	Proline dehydrogenase domain	Domain
A, B, C, D	IPR015590	Aldehyde dehydrogenase domain	Domain
A, B, C, D	IPR016161	Aldehyde/histidinol dehydrogenase	Homologous Superfamily
A, B, C, D	IPR029041	FAD-linked oxidoreductase-like	Homologous Superfamily
A, B, C, D	IPR016162	Aldehyde dehydrogenase, N-terminal	Homologous Superfamily
A, B, C, D	IPR050485	Proline metabolism enzyme	Family
A, B, C, D	IPR025703	Bifunctional protein PutA	Family
A, B, C, D	IPR005932	1-pyrroline-5-carboxylate dehydrogenase	Family
A, B, C, D	IPR029510	Aldehyde dehydrogenase, glutamic acid active site	Conserved Site
A, B, C, D	IPR041514	Proline utilization A, N-terminal	Domain
A, B, C, D	IPR016163	Aldehyde dehydrogenase, C-terminal	Homologous Superfamily
A, B, C, D	IPR016160	Aldehyde dehydrogenase, cysteine active site	Conserved Site

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.