Annotations: 1ET0

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1et0a_	Multi-domain proteins (alpha and beta)	D-aminoacid aminotransferase-like PLP-dependent enzymes	D-aminoacid aminotransferase-like PLP-dependent enzymes	D-aminoacid aminotransferase-like PLP-dependent enzymes	Aminodeoxychorismate lyase	(Escherichia coli ) [TaxId: 562 ],	SCOPe (2.08)

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	8035892	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	PF01063	e1et0A2	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: PF01063	ECOD (1.6)
A	PF01063	e1et0A1	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: PF01063	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.30.470.10	Alpha Beta	2-Layer Sandwich	D-amino Acid Aminotransferase	Chain A, domain 1	CATH (4.3.0)
A	3.20.10.10	Alpha Beta	Alpha-Beta Barrel	D-amino Acid Aminotransferase	Chain A, domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	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	4-AMINO-4-DEOXYCHORISMATE LYASE	4-amino-4-deoxychorismate lyase activity oxo-acid-lyase activity lyase activity catalytic activity carbon-carbon lyase activity vitamin binding vitamin B6 binding pyridoxal phosphate binding ion binding binding organic cyclic compound binding anion binding heterocyclic compound binding small molecule binding	oxoacid metabolic process cellular biosynthetic process organonitrogen compound biosynthetic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process organic substance metabolic process para-aminobenzoic acid biosynthetic process organic substance biosynthetic process small molecule metabolic process organonitrogen compound metabolic process benzene-containing compound metabolic process aromatic amino acid metabolic process oxoacid metabolic process cellular biosynthetic process organonitrogen compound biosynthetic process amino acid metabolic process organic acid metabolic process organic acid biosynthetic process carboxylic acid biosynthetic process organic substance metabolic process para-aminobenzoic acid biosynthetic process organic substance biosynthetic process small molecule metabolic process organonitrogen compound metabolic process benzene-containing compound metabolic process aromatic amino acid metabolic process monocarboxylic acid biosynthetic process aromatic amino acid family biosynthetic process small molecule biosynthetic process cellular metabolic process carboxylic acid metabolic process primary metabolic process organic cyclic compound metabolic process amino acid biosynthetic process biosynthetic process para-aminobenzoic acid metabolic process organic cyclic compound biosynthetic process metabolic process cellular process monocarboxylic acid metabolic process vitamin 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 dicarboxylic acid metabolic process amide biosynthetic process cellular modified amino acid metabolic process vitamin metabolic process cellular modified amino acid biosynthetic process folic acid-containing compound metabolic process pteridine-containing compound biosynthetic process pteridine-containing compound metabolic process tetrahydrofolate biosynthetic process tetrahydrofolate metabolic process	intracellular anatomical structure cytoplasm cellular anatomical entity cytosol

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR043132	Branched-chain-amino-acid aminotransferase-like, C-terminal	Homologous Superfamily
A	IPR043131	Branched-chain-amino-acid aminotransferase-like, N-terminal	Homologous Superfamily
A	IPR001544	Aminotransferase class IV	Family
A	IPR017824	Aminodeoxychorismate lyase, class IV	Family
A	IPR036038	Aminotransferase-like, PLP-dependent enzymes	Homologous Superfamily
A	IPR018300	Aminotransferase, class IV, conserved site	Conserved Site

Structure Motif Annotation: Mechanism and Catalytic Site Atlas M-CSA Database Homepage

Chains	Enzyme Name	Description	Catalytic Residues
A	aminodeoxychorismate lyase (class IV) M-CSA #305	4-Amino-4-Deoxychorismate Lyase (ADCL), sourced from Escherichia coli is a member of the fold-type IV of PLP dependent enzymes. It converts 4-amino-4-deoxychorismate (ADC) to p-aminobenzoate and pyruvate during the process of tetrahydrofolate biosynthesis. P-aminobenzoate is a precursor of folic acid. ADCL is a homodimer and shows the re-face specific hydrogen transfer typical of a member of the fold-type IV family.	Defined by 3 residues: THR:A-28 [auth A-38]LYS:A-140 [auth A-159]GLU:A-173 [auth A-193] \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), 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 R01GM133198.