AC MF_00834; DC Protein; auto TR HAMAP; MF_00834; -; 1; level=0 XX Names: BioA XX ID BIOA DE RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase; DE EC=2.6.1.62; DE AltName: Full=7,8-diamino-pelargonic acid aminotransferase; DE Short=DAPA AT; DE Short=DAPA aminotransferase; DE AltName: Full=7,8-diaminononanoate synthase; DE Short=DANS; DE AltName: Full=Diaminopelargonic acid synthase; GN Name=bioA; XX CC -!- FUNCTION: Catalyzes the transfer of the alpha-amino group from S- CC adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to CC form 7,8-diaminopelargonic acid (DAPA). It is the only aminotransferase CC known to utilize SAM as an amino donor. CC -!- CATALYTIC ACTIVITY: CC Reaction=(8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine = CC (7R,8S)-7,8-diammoniononanoate + S-adenosyl-4-methylsulfanyl-2- CC oxobutanoate; Xref=Rhea:RHEA:16861, ChEBI:CHEBI:16490, CC ChEBI:CHEBI:59789, ChEBI:CHEBI:149468, ChEBI:CHEBI:149469; CC EC=2.6.1.62; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8- CC diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1. CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. BioA subfamily. XX DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1; trigger=no DR Pfam; PF00202; Aminotran_3; 1; trigger=no DR NCBIfam; TIGR00508; BioA; 1; trigger=no XX KW Aminotransferase KW Biotin biosynthesis KW Cytoplasm KW Pyridoxal phosphate KW S-adenosyl-L-methionine KW Transferase XX GO GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity GO GO:0030170; F:pyridoxal phosphate binding GO GO:0009102; P:biotin biosynthetic process GO GO:0005737; C:cytoplasm XX FT From: BIOA_ECOLI (P12995) FT BINDING 112..113 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT Condition: G-[SA] FT BINDING 308..309 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT Condition: [PHNS]-[TS] FT BINDING 52 FT /ligand="substrate" FT Condition: W FT BINDING 144 FT /ligand="substrate" FT Condition: Y FT BINDING 245 FT /ligand="pyridoxal 5'-phosphate" FT /ligand_id="ChEBI:CHEBI:597326" FT Condition: D FT BINDING 274 FT /ligand="substrate" FT Condition: K FT BINDING 307 FT /ligand="substrate" FT Condition: [GS] FT BINDING 391 FT /ligand="substrate" FT Condition: R FT MOD_RES 274 FT /note="N6-(pyridoxal phosphate)lysine" FT Condition: K FT SITE 17 FT /note="Participates in the substrate recognition with KAPA FT and in a stacking interaction with the adenine ring of SAM" XX Size: 400-560; Related: None; Template: P12995; P9WQ81; P53555; P22805; Scope: Bacteria Archaea Fusion: Nter: MF_01694 (BioB) Cter: None Duplicate: None Plasmid: None Comments: B.subtilis DAPA aminotransferase does not utilize SAM, but instead utilizes L-lysine as the amino donor (PMID:15880481). Bacteroides encode a fusion between BioA and BioB (Biotin synthase). XX # Revision 1.15 2023/06/01 //