3IWJ

Crystal structure of aminoaldehyde dehydrogenase 2 from Pisum sativum (PsAMADH2)

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
B	d3iwjb_	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	automated matches	automated matches	garden pea (Pisum sativum ) [TaxId: 3888 ],	SCOPe (2.08)
A	d3iwja_	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	automated matches	automated matches	garden pea (Pisum sativum ) [TaxId: 3888 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
B	SCOP2B Superfamily	ALDH-like	8065654	3001479	SCOP2B (2022-06-29)
A	SCOP2 Family	ALDH-like	8065653	4000806	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	ALDH-like	8065654	3001479	SCOP2 (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	Aldedh_2nd	e3iwjB2	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	e3iwjB1	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	Aldedh_2nd	e3iwjA2	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	e3iwjA1	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)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
B	3.40.605.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 1	CATH (4.3.0)
B	3.40.309.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 2	CATH (4.3.0)
A	3.40.605.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 1	CATH (4.3.0)
A	3.40.309.10	Alpha Beta	3-Layer(aba) Sandwich	Aldehyde Dehydrogenase	Chain A, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00171	Aldehyde dehydrogenase family (Aldedh)	Aldehyde dehydrogenase family	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Putative aminoaldehyde dehydrogenase	identical protein binding protein binding binding protein homodimerization activity protein dimerization activity oxidoreductase activity aldehyde dehydrogenase (NAD+) activity gamma-guanidinobutyraldehyde dehydrogenase (NAD+) activity oxidoreductase activity, acting on the aldehyde or oxo group of donors catalytic activity aldehyde dehydrogenase [NAD(P)+] activity oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor nucleoside phosphate binding organic cyclic compound binding identical protein binding protein binding binding protein homodimerization activity protein dimerization activity oxidoreductase activity aldehyde dehydrogenase (NAD+) activity gamma-guanidinobutyraldehyde dehydrogenase (NAD+) activity oxidoreductase activity, acting on the aldehyde or oxo group of donors catalytic activity aldehyde dehydrogenase [NAD(P)+] activity oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor nucleoside phosphate binding organic cyclic compound binding nucleotide binding heterocyclic compound binding small molecule binding cation binding ion binding alkali metal ion binding sodium ion binding metal ion binding aminobutyraldehyde dehydrogenase (NAD+) activity	cellular response to stimulus cellular detoxification response to stimulus detoxification response to oxygen-containing compound cellular response to oxygen-containing compound response to toxic substance cellular detoxification of aldehyde cellular response to chemical stimulus cellular response to aldehyde response to chemical cellular process cellular response to toxic substance amino-acid betaine biosynthetic process cellular response to stimulus cellular detoxification response to stimulus detoxification response to oxygen-containing compound cellular response to oxygen-containing compound response to toxic substance cellular detoxification of aldehyde cellular response to chemical stimulus cellular response to aldehyde response to chemical cellular process cellular response to toxic substance amino-acid betaine biosynthetic process modified amino acid biosynthetic process modified amino acid metabolic process amino-acid betaine metabolic process glycine betaine metabolic process glycine betaine biosynthetic process from choline ammonium ion metabolic process biosynthetic process choline metabolic process metabolic process glycine betaine biosynthetic process	membrane-bounded organelle intracellular organelle cellular anatomical structure intracellular anatomical structure organelle peroxisome microbody cytoplasm intracellular membrane-bounded organelle

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR015590	Aldehyde dehydrogenase domain	Domain
A, B	IPR016161	Aldehyde/histidinol dehydrogenase	Homologous Superfamily
A, B	IPR016162	Aldehyde dehydrogenase, N-terminal	Homologous Superfamily
A, B	IPR029510	Aldehyde dehydrogenase, glutamic acid active site	Conserved Site
A, B	IPR016163	Aldehyde dehydrogenase, C-terminal	Homologous Superfamily
A, B	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.