4K2M

Crystal structure of ntda from bacillus subtilis in complex with the plp external aldimine adduct with kanosamine-6-phosphate

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	GABA-aminotransferase-like	8098089	4000675	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	PLP-dependent transferases	8098090	3000954	SCOP2 (2022-06-29)
B	SCOP2B Superfamily	PLP-dependent transferases	8098090	3000954	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	DegT_DnrJ_EryC1	e4k2mA2	A: a+b two layers	X: C-terminal domain in some PLP-dependent transferases (From Topology)	H: C-terminal domain in some PLP-dependent transferases (From Topology)	T: C-terminal domain in some PLP-dependent transferases	F: DegT_DnrJ_EryC1	ECOD (1.6)
A	EUF08651	e4k2mA3	A: a/b three-layered sandwiches	X: N-terminal domain in NTD biosynthesis operon protein NtdA (From Topology)	H: N-terminal domain in NTD biosynthesis operon protein NtdA (From Topology)	T: N-terminal domain in NTD biosynthesis operon protein NtdA	F: EUF08651	ECOD (1.6)
A	Aminotran_5_N	e4k2mA1	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_5_N	ECOD (1.6)
B	DegT_DnrJ_EryC1	e4k2mB3	A: a+b two layers	X: C-terminal domain in some PLP-dependent transferases (From Topology)	H: C-terminal domain in some PLP-dependent transferases (From Topology)	T: C-terminal domain in some PLP-dependent transferases	F: DegT_DnrJ_EryC1	ECOD (1.6)
B	EUF08651	e4k2mB2	A: a/b three-layered sandwiches	X: N-terminal domain in NTD biosynthesis operon protein NtdA (From Topology)	H: N-terminal domain in NTD biosynthesis operon protein NtdA (From Topology)	T: N-terminal domain in NTD biosynthesis operon protein NtdA	F: EUF08651	ECOD (1.6)
B	Aminotran_5_N	e4k2mB1	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_5_N	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.640.10	Alpha Beta	3-Layer(aba) Sandwich	Aspartate Aminotransferase	domain 2	CATH (4.3.0)
A	3.90.1150.10	Alpha Beta	Alpha-Beta Complex	Aspartate Aminotransferase, domain 1	Aspartate Aminotransferase, domain 1	CATH (4.3.0)
B	3.40.640.10	Alpha Beta	3-Layer(aba) Sandwich	Aspartate Aminotransferase	domain 2	CATH (4.3.0)
B	3.90.1150.10	Alpha Beta	Alpha-Beta Complex	Aspartate Aminotransferase, domain 1	Aspartate Aminotransferase, domain 1	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B	PF01041	DegT/DnrJ/EryC1/StrS aminotransferase family (DegT_DnrJ_EryC1)	DegT/DnrJ/EryC1/StrS aminotransferase family	The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA Swiss:P72454, StsC Swiss:P77952 and StsS [1]. The aminotransferase activity was demons ...	The members of this family are probably all pyridoxal-phosphate-dependent aminotransferase enzymes with a variety of molecular functions. The family includes StsA Swiss:P72454, StsC Swiss:P77952 and StsS [1]. The aminotransferase activity was demonstrated for purified StsC protein as the L-glutamine:scyllo-inosose aminotransferase EC:2.6.1.50, which catalyses the first amino transfer in the biosynthesis of the streptidine subunit of streptomycin [1].	Domain
A, B	PF22127	NTD biosynthesis operon protein NtdA, N-terminal domain (NtdA_N)	NTD biosynthesis operon protein NtdA, N-terminal domain	This entry represents the N-terminal domain of NtdA, which is not found in other aminotransferases and consists of two-stranded parallel beta-sheet flanked by two alpha-helices [1]. This domain may be involved in protein-protein interactions. NtdA is ...	This entry represents the N-terminal domain of NtdA, which is not found in other aminotransferases and consists of two-stranded parallel beta-sheet flanked by two alpha-helices [1]. This domain may be involved in protein-protein interactions. NtdA is a sugar aminotransferase involved in the biosynthesis of kanosamine.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B	NTD biosynthesis operon protein NtdA	transferase activity, transferring nitrogenous groups transaminase activity transferase activity catalytic activity vitamin binding vitamin B6 binding pyridoxal phosphate binding ion binding binding organic cyclic compound binding anion binding heterocyclic compound binding small molecule binding	carbohydrate metabolic process polysaccharide biosynthetic process cellular biosynthetic process carbohydrate biosynthetic process cellular metabolic process primary metabolic process macromolecule biosynthetic process polysaccharide metabolic process biosynthetic process metabolic process cellular process macromolecule metabolic process antibiotic metabolic process antibiotic biosynthetic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B	IPR015424	Pyridoxal phosphate-dependent transferase	Homologous Superfamily
A, B	IPR000653	DegT/DnrJ/EryC1/StrS aminotransferase	Family
A, B	IPR054367	Oxo-glucose-6-phosphate:glutamate aminotransferase, N-terminal domain	Domain
A, B	IPR015421	Pyridoxal phosphate-dependent transferase, major domain	Homologous Superfamily
A, B	IPR015422	Pyridoxal phosphate-dependent transferase, small domain	Homologous Superfamily

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.