ID   BIOA_CITFR              Reviewed;           5 AA.
AC   P13071;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=Diaminopelargonic acid synthase;
DE   Flags: Fragment;
GN   Name=bioA;
OS   Citrobacter freundii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Citrobacter; Citrobacter freundii complex.
OX   NCBI_TaxID=546;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2971595; DOI=10.1016/0378-1119(88)90397-6;
RA   Shiuan D., Campbell A.;
RT   "Transcriptional regulation and gene arrangement of Escherichia coli,
RT   Citrobacter freundii and Salmonella typhimurium biotin operons.";
RL   Gene 67:203-211(1988).
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 (By similarity). {ECO:0000250}.
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         Evidence={ECO:0000250};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
CC       diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. BioA subfamily. {ECO:0000305}.
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DR   EMBL; M21922; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; I40697; I40697.
DR   UniPathway; UPA00078; UER00160.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway.
PE   3: Inferred from homology;
KW   Aminotransferase; Biotin biosynthesis; Cytoplasm; Pyridoxal phosphate;
KW   S-adenosyl-L-methionine; Transferase.
FT   CHAIN           1..>5
FT                   /note="Adenosylmethionine-8-amino-7-oxononanoate
FT                   aminotransferase"
FT                   /id="PRO_0000120367"
FT   NON_TER         5
SQ   SEQUENCE   5 AA;  582 MW;  6AAAB1B1A6F00000 CRC64;
     MTTDD