Annotations: 7KZ3

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
B	DegT_DnrJ_EryC1	e7kz3B3	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	e7kz3B2	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	e7kz3B1	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)
C	DegT_DnrJ_EryC1	e7kz3C3	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)
C	EUF08651	e7kz3C1	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)
C	Aminotran_5_N	e7kz3C2	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)
D	DegT_DnrJ_EryC1	e7kz3D2	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)
D	EUF08651	e7kz3D1	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)
D	Aminotran_5_N	e7kz3D3	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)
A	DegT_DnrJ_EryC1	e7kz3A3	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	e7kz3A1	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	e7kz3A2	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)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	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, C, D	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, C, D	Aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme	transferase activity, transferring nitrogenous groups transaminase activity transferase activity catalytic activity	-	-

InterPro: Protein Family Classification InterPro Database Homepage

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

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, B, C, D	LLP	Parent Component: LYS RESID: AA0119 PSI-MOD : N6-pyridoxal phosphate-L-lysine MOD:00128

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.