1KAE

L-HISTIDINOL DEHYDROGENASE (HISD) STRUCTURE COMPLEXED WITH L-HISTIDINOL (SUBSTRATE), ZINC AND NAD (COFACTOR)

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
Structure Motif: Primary M-CSA Annotation

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1kaea_	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	L-histidinol dehydrogenase HisD	L-histidinol dehydrogenase HisD	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)
B	d1kaeb_	Alpha and beta proteins (a/b)	ALDH-like	ALDH-like	L-histidinol dehydrogenase HisD	L-histidinol dehydrogenase HisD	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	ALDH-like	8037854	3001479	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	ALDH-like	8037854	3001479	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF00815	e1kaeA1	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: PF00815	ECOD (1.6)
B	PF00815	e1kaeB1	A: a/b three-layered sandwiches	X: ALDH-like (From Topology)	H: ALDH-like (From Topology)	T: ALDH-like	F: PF00815	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1980	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Nitrogenase molybdenum iron protein domain	CATH (4.3.0)
A	1.20.5.1300	Mainly Alpha	Up-down Bundle	Single alpha-helices involved in coiled-coils or other helix-helix interfaces		CATH (4.3.0)
B	3.40.50.1980	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Nitrogenase molybdenum iron protein domain	CATH (4.3.0)
B	1.20.5.1300	Mainly Alpha	Up-down Bundle	Single alpha-helices involved in coiled-coils or other helix-helix interfaces		CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF00815	Histidinol dehydrogenase (Histidinol_dh)	Histidinol dehydrogenase	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	Histidinol dehydrogenase	cation binding manganese ion binding transition metal ion binding ion binding binding metal ion binding small molecule binding NAD binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding cation binding manganese ion binding transition metal ion binding ion binding binding metal ion binding small molecule binding NAD binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding zinc ion binding histidinol dehydrogenase activity oxidoreductase activity oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor oxidoreductase activity, acting on CH-OH group of donors catalytic activity	organonitrogen compound metabolic process small molecule biosynthetic process oxoacid metabolic process cellular biosynthetic process cellular metabolic process organonitrogen compound biosynthetic process carboxylic acid metabolic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process organic substance metabolic process biosynthetic process organic substance biosynthetic process small molecule metabolic process organonitrogen compound metabolic process small molecule biosynthetic process oxoacid metabolic process cellular biosynthetic process cellular metabolic process organonitrogen compound biosynthetic process carboxylic acid metabolic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process organic substance metabolic process biosynthetic process organic substance biosynthetic process small molecule metabolic process metabolic process cellular process histidine metabolic process histidine biosynthetic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR022695	Histidinol dehydrogenase, monofunctional	Family
A, B	IPR016161	Aldehyde/histidinol dehydrogenase	Homologous Superfamily
A, B	IPR001692	Histidinol dehydrogenase, conserved site	Conserved Site
A, B	IPR012131	Histidinol dehydrogenase	Family

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A, B	histidinol dehydrogenase M-CSA #741	L-histidinol dehydrogenase, sourced from Escherichia coli, catalyses the last two steps of histidine biosynthesis: NAD dependent oxidation of L-histidinol to L-histinaldehyde and then to L-histidine. L-histidinol dehydrogenase is a homodimeric zinc metalloenzyme with one binding site per monomer. Each monomer contains four domains- the intertwined dimer possibly results from domain swapping. Two domains display a similar incomplete Rossmann fold, suggesting an ancient event of gene duplication.	Defined by 6 residues: GLN:A-259HIS:A-262GLU:A-326HIS:A-327ASP:A-360HIS:B-419 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 1.1.1.23 (PDB Primary Data) Search M-CSA Motif + EC 1.1.1.23

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.