3P2Y

Crystal structure of alanine dehydrogenase/pyridine nucleotide transhydrogenase from Mycobacterium smegmatis

External Resource: Annotation

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: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	L-alanine dehydrogenase-like	8085300	4000097	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	D-2-hydroxyacid dehydrogenase-like	8085301	3000044	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)
A	AlaDh_PNT_C	e3p2yA1	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: NAD(P)-binding Rossmann-fold domains	F: AlaDh_PNT_C	ECOD (1.6)
A	AlaDh_PNT_N	e3p2yA2	A: a/b three-layered sandwiches	X: Rossmann-like	H: Rossmann-related	T: Formate/glycerate dehydrogenase catalytic domain-like	F: AlaDh_PNT_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.720	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	NAD(P)-binding Rossmann-like Domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF05222	Alanine dehydrogenase/PNT, N-terminal domain (AlaDh_PNT_N)	Alanine dehydrogenase/PNT, N-terminal domain	This family now also contains the lysine 2-oxoglutarate reductases.	Domain
A	PF01262	Alanine dehydrogenase/PNT, C-terminal domain (AlaDh_PNT_C)	Alanine dehydrogenase/PNT, C-terminal domain	This family now also contains the lysine 2-oxoglutarate reductases.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Alanine dehydrogenase/pyridine nucleotide transhydrogenase	binding nucleoside phosphate binding purine nucleotide binding organic cyclic compound binding adenyl nucleotide binding nucleotide binding heterocyclic compound binding NADP binding small molecule binding cation binding ion binding metal ion binding	nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process primary metabolic process generation of precursor metabolites and energy nucleotide metabolic process purine-containing compound metabolic process NADP metabolic process nucleobase-containing compound metabolic process NADPH regeneration purine nucleotide metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process pyridine-containing compound metabolic process nucleoside phosphate metabolic process nicotinamide nucleotide metabolic process primary metabolic process generation of precursor metabolites and energy nucleotide metabolic process purine-containing compound metabolic process NADP metabolic process nucleobase-containing compound metabolic process NADPH regeneration purine nucleotide metabolic process organophosphate metabolic process nucleobase-containing small molecule metabolic process phosphate-containing compound metabolic process pyridine-containing compound metabolic process metabolic process cellular process small molecule metabolic process phosphorus metabolic process pyridine nucleotide metabolic process	cell periphery cellular anatomical structure plasma membrane membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR007886	Alanine dehydrogenase/pyridine nucleotide transhydrogenase, N-terminal	Domain
A	IPR036291	NAD(P)-binding domain superfamily	Homologous Superfamily
A	IPR007698	Alanine dehydrogenase/pyridine nucleotide transhydrogenase, NAD(H)-binding domain	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.