6ZUP

Psychrophilic aromatic amino acids aminotransferase from Psychrobacter sp. B6 cocrystalized with substrate analog - L-(-)-3-phenyllactic acid

External Resource: Annotation

Domain Annotation: SCOP/SCOPe Classification
Domain Annotation: SCOP2 Classification
Domain Annotation: ECOD Classification
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A [auth B]	d6zupb_	Alpha and beta proteins (a/b)	PLP-dependent transferase-like	PLP-dependent transferases	automated matches	automated matches	(Psychrobacter sp. B6 ) [TaxId: 408968 ],	SCOPe (2.08)
B [auth A]	d6zupa_	Alpha and beta proteins (a/b)	PLP-dependent transferase-like	PLP-dependent transferases	automated matches	automated matches	(Psychrobacter sp. B6 ) [TaxId: 408968 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A [auth B]	SCOP2B Superfamily	PLP-dependent transferases	8069121	3000954	SCOP2B (2022-06-29)
B [auth A]	SCOP2B Superfamily	PLP-dependent transferases	8069121	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 [auth B]	Aminotran_1_2_C_7	e6zupB2	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: Aminotran_1_2_C_7	ECOD (1.6)
A [auth B]	Aminotran_1_2_N	e6zupB1	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_1_2_N	ECOD (1.6)
B [auth A]	Aminotran_1_2_C_7	e6zupA2	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: Aminotran_1_2_C_7	ECOD (1.6)
B [auth A]	Aminotran_1_2_N	e6zupA1	A: a/b three-layered sandwiches	X: PLP-dependent transferases (From Topology)	H: PLP-dependent transferases (From Topology)	T: PLP-dependent transferases	F: Aminotran_1_2_N	ECOD (1.6)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A [auth B], B [auth A]	PF00155	Aminotransferase class I and II (Aminotran_1_2)	Aminotransferase class I and II	-	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A [auth B], B [auth A]	Aminotransferase	transferase activity, transferring nitrogenous groups aromatic-amino-acid transaminase activity transaminase activity L-tyrosine-2-oxoglutarate 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 transferase activity, transferring nitrogenous groups aromatic-amino-acid transaminase activity transaminase activity L-tyrosine-2-oxoglutarate 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 cation binding metal ion binding identical protein binding protein binding	oxoacid metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process L-phenylalanine biosynthetic process from chorismate via phenylpyruvate alpha-amino acid metabolic process carboxylic acid biosynthetic process chorismate metabolic process small molecule metabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process L-phenylalanine biosynthetic process aromatic amino acid family biosynthetic process aromatic amino acid metabolic process small molecule biosynthetic process oxoacid metabolic process amino acid metabolic process organic acid biosynthetic process organic acid metabolic process L-phenylalanine biosynthetic process from chorismate via phenylpyruvate alpha-amino acid metabolic process carboxylic acid biosynthetic process chorismate metabolic process small molecule metabolic process erythrose 4-phosphate/phosphoenolpyruvate family amino acid metabolic process L-phenylalanine biosynthetic process aromatic amino acid family biosynthetic process aromatic amino acid metabolic process small molecule biosynthetic process dicarboxylic acid metabolic process carboxylic acid metabolic process primary metabolic process L-amino acid biosynthetic process L-amino acid metabolic process L-phenylalanine metabolic process aromatic amino acid family biosynthetic process, prephenate pathway proteinogenic amino acid metabolic process amino acid biosynthetic process biosynthetic process proteinogenic amino acid biosynthetic process metabolic process cellular process erythrose 4-phosphate/phosphoenolpyruvate family amino acid biosynthetic process alpha-amino acid biosynthetic process	cellular anatomical structure intracellular anatomical structure cytoplasm cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A [auth B], B [auth A]	IPR015424	Pyridoxal phosphate-dependent transferase	Homologous Superfamily
A [auth B], B [auth A]	IPR004838	Aminotransferases, class-I, pyridoxal-phosphate-binding site	Binding Site
A [auth B], B [auth A]	IPR015421	Pyridoxal phosphate-dependent transferase, major domain	Homologous Superfamily
A [auth B], B [auth A]	IPR015422	Pyridoxal phosphate-dependent transferase, small domain	Homologous Superfamily
A [auth B], B [auth A]	IPR000796	Aspartate/other aminotransferase	Family
A [auth B], B [auth A]	IPR004839	Aminotransferase, class I/classII, large 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.