6Q1R

A hypothetical aminotransferase from Mycobacterium tuberculosis, PLP-bound form

External Resource: Annotation

Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
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	SCOP2B Superfamily	D-aminoacid aminotransferase-like PLP-dependent enzymes	8101677	3001836	SCOP2B (2022-06-29)
D	SCOP2B Superfamily	D-aminoacid aminotransferase-like PLP-dependent enzymes	8101677	3001836	SCOP2B (2022-06-29)
B	SCOP2B Superfamily	D-aminoacid aminotransferase-like PLP-dependent enzymes	8101677	3001836	SCOP2B (2022-06-29)
C	SCOP2B Superfamily	D-aminoacid aminotransferase-like PLP-dependent enzymes	8101677	3001836	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	Aminotran_4_N	e6q1rA1	A: a+b two layers	X: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	H: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	T: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes	F: Aminotran_4_N	ECOD (1.6)
A	Aminotran_4_C	e6q1rA2	A: a+b two layers	X: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	H: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	T: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes	F: Aminotran_4_C	ECOD (1.6)
D	Aminotran_4_N	e6q1rD1	A: a+b two layers	X: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	H: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	T: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes	F: Aminotran_4_N	ECOD (1.6)
D	Aminotran_4_C	e6q1rD2	A: a+b two layers	X: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	H: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	T: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes	F: Aminotran_4_C	ECOD (1.6)
B	Aminotran_4_N	e6q1rB2	A: a+b two layers	X: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	H: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	T: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes	F: Aminotran_4_N	ECOD (1.6)
B	Aminotran_4_C	e6q1rB1	A: a+b two layers	X: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	H: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	T: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes	F: Aminotran_4_C	ECOD (1.6)
C	Aminotran_4_N	e6q1rC2	A: a+b two layers	X: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	H: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	T: a+b domain in D-aminoacid aminotransferase-like PLP-dependent enzymes	F: Aminotran_4_N	ECOD (1.6)
C	Aminotran_4_C	e6q1rC1	A: a+b two layers	X: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	H: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes (From Topology)	T: barrel domain in D-aminoacid aminotransferase-like PLP-dependent enzymes	F: Aminotran_4_C	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C, D	PF01063	Amino-transferase class IV (Aminotran_4)	Amino-transferase class IV	The D-amino acid transferases (D-AAT) are required by bacteria to catalyse the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the diff ...	The D-amino acid transferases (D-AAT) are required by bacteria to catalyse the synthesis of D-glutamic acid and D-alanine, which are essential constituents of bacterial cell wall and are the building block for other D-amino acids. Despite the difference in the structure of the substrates, D-AATs and L-ATTs have strong similarity.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C, D	Probable amino acid aminotransferase	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 4-amino-4-deoxychorismate lyase activity 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 4-amino-4-deoxychorismate lyase activity oxo-acid-lyase activity lyase activity carbon-carbon lyase activity	developmental process regulation of biological process regulation of developmental process biological regulation regulation of cell shape cell morphogenesis regulation of cell morphogenesis anatomical structure morphogenesis anatomical structure development regulation of biological quality regulation of anatomical structure morphogenesis oxoacid metabolic process carboxylic acid metabolic process small molecule metabolic process developmental process regulation of biological process regulation of developmental process biological regulation regulation of cell shape cell morphogenesis regulation of cell morphogenesis anatomical structure morphogenesis anatomical structure development regulation of biological quality regulation of anatomical structure morphogenesis oxoacid metabolic process carboxylic acid metabolic process small molecule metabolic process metabolic process cellular process organic acid metabolic process modified amino acid biosynthetic process vitamin biosynthetic process organic acid biosynthetic process carboxylic acid biosynthetic process amide metabolic process water-soluble vitamin metabolic process folic acid metabolic process dicarboxylic acid biosynthetic process folic acid biosynthetic process folic acid-containing compound biosynthetic process water-soluble vitamin biosynthetic process small molecule biosynthetic process dicarboxylic acid metabolic process modified amino acid metabolic process amide biosynthetic process vitamin metabolic process biosynthetic process folic acid-containing compound metabolic process pteridine-containing compound biosynthetic process pteridine-containing compound metabolic process carbohydrate derivative biosynthetic process peptidoglycan-based cell wall biogenesis cell wall organization or biogenesis glycosaminoglycan metabolic process carbohydrate derivative metabolic process macromolecule biosynthetic process cellular component biogenesis peptidoglycan biosynthetic process cell wall biogenesis cell wall macromolecule biosynthetic process aminoglycan metabolic process peptidoglycan metabolic process aminoglycan biosynthetic process glycosaminoglycan biosynthetic process cellular component organization or biogenesis macromolecule metabolic process tetrahydrofolate biosynthetic process tetrahydrofolate metabolic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol cell periphery plasma membrane membrane

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C, D	IPR050571	Class-IV Pyridoxal-Phosphate-Dependent Aminotransferase	Family
A, B, C, D	IPR017824	Aminodeoxychorismate lyase, class IV	Family
A, B, C, D	IPR036038	Aminotransferase-like, PLP-dependent enzymes	Homologous Superfamily
A, B, C, D	IPR043132	Branched-chain-amino-acid aminotransferase-like, C-terminal	Homologous Superfamily
A, B, C, D	IPR043131	Branched-chain-amino-acid aminotransferase-like, N-terminal	Homologous Superfamily
A, B, C, D	IPR001544	Aminotransferase class IV	Family

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.