Annotations: 1BS0

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

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1bs0a_	Alpha and beta proteins (a/b)	PLP-dependent transferase-like	PLP-dependent transferases	GABA-aminotransferase-like	PLP-dependent acyl-CoA synthase (8-amino-7-oxonanoate synthase, AONS)	(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	SCOP2 Family	GABA-aminotransferase-like	8020028	4000675	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	PLP-dependent transferases	8032408	3000954	SCOP2 (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_1_2_C_10	e1bs0A1	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_10	ECOD (1.6)
A	Aminotran_5_N	e1bs0A2	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	3.90.1150.10	Alpha Beta	Alpha-Beta Complex	Aspartate Aminotransferase, domain 1	Aspartate Aminotransferase, domain 1	CATH (4.3.0)
A	3.40.640.10	Alpha Beta	3-Layer(aba) Sandwich	Aspartate Aminotransferase	domain 2	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
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	PROTEIN (8-AMINO-7-OXONANOATE SYNTHASE)	identical protein binding protein binding binding protein homodimerization activity protein dimerization activity vitamin binding vitamin B6 binding pyridoxal phosphate binding ion binding organic cyclic compound binding anion binding heterocyclic compound binding small molecule binding acyltransferase activity identical protein binding protein binding binding protein homodimerization activity protein dimerization activity vitamin binding vitamin B6 binding pyridoxal phosphate binding ion binding organic cyclic compound binding anion binding heterocyclic compound binding small molecule binding acyltransferase activity 8-amino-7-oxononanoate synthase activity acyltransferase activity, transferring groups other than amino-acyl groups transferase activity catalytic activity	biotin metabolic process oxoacid metabolic process cellular biosynthetic process vitamin biosynthetic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process small molecule metabolic process sulfur compound metabolic process amide metabolic process water-soluble vitamin metabolic process water-soluble vitamin biosynthetic process monocarboxylic acid biosynthetic process small molecule biosynthetic process biotin metabolic process oxoacid metabolic process cellular biosynthetic process vitamin biosynthetic process organic acid biosynthetic process organic acid metabolic process carboxylic acid biosynthetic process small molecule metabolic process sulfur compound metabolic process amide metabolic process water-soluble vitamin metabolic process water-soluble vitamin biosynthetic process monocarboxylic acid biosynthetic process small molecule biosynthetic process cellular metabolic process carboxylic acid metabolic process amide biosynthetic process biotin biosynthetic process vitamin metabolic process sulfur compound biosynthetic process biosynthetic process metabolic process cellular process monocarboxylic acid metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR015424	Pyridoxal phosphate-dependent transferase	Homologous Superfamily
A	IPR001917	Aminotransferase, class-II, pyridoxal-phosphate binding site	Binding Site
A	IPR015421	Pyridoxal phosphate-dependent transferase, major domain	Homologous Superfamily
A	IPR015422	Pyridoxal phosphate-dependent transferase, small domain	Homologous Superfamily
A	IPR022834	8-amino-7-oxononanoate synthase, Proteobacteria	Family
A	IPR004839	Aminotransferase, class I/classII, large domain	Domain
A	IPR050087	8-amino-7-oxononanoate synthase class-II	Family
A	IPR004723	8-amino-7-oxononanoate synthase, Archaea/Proteobacteria type	Family

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

Chains	Enzyme Name	Description	Catalytic Residues
A	8-amino-7-oxononanoate synthase M-CSA #430	8-Amino-7-oxononanoate synthase (AONS) is a pyridoxal 5′-phosphate-dependent enzyme that catalyzes the decarboxylative condensation of L-alanine with pimeloyl-CoA in a stereospecific manner to form 8(S)-amino-7-oxononanoate, coenzyme A, and carbon dioxide in the first committed step of biotin biosynthesis. AONS also performs the carboxylation of acetyl-CoA to give malonyl-CoA, which is the first step in fatty acid biosynthesis. Biotin is an essential enzyme cofactor for carboxylase and transcarboxlase reactions. Fatty acid synthesis is essential for the growth and development of most organisms. Plants, microorganisms, and some fungi bio-synthesize their own biotin, whilst animals require trace amounts in their diet, thus, inhibition of the enzymes involved in the biotin biosynthesis pathway can cause irreparable damage to plants but can be non-toxic to mammals; for this reason, such enzymes can be useful targets for the rational design of inhibitors in the hopes of finding new herbicides and antibiotics.	Defined by 7 residues: ASN:A-47HIS:A-133GLU:A-175SER:A-179ASP:A-204HIS:A-207LYS:A-236 \| Explore in 3D: M-CSA Motif Definition Search M-CSA Motif EC: 2.3.1.47 (PDB Primary Data) Search M-CSA Motif + EC 2.3.1.47

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.