ID Q8FPR9_COREF Unreviewed; 380 AA.
AC Q8FPR9;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE SubName: Full=Adenosylmethionine--8-amino-7-oxononanoate transaminase {ECO:0000313|EMBL:BAC18231.1};
DE EC=2.6.1.62 {ECO:0000313|EMBL:BAC18231.1};
GN Name=bioA {ECO:0000313|EMBL:BAC18231.1};
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=196164 {ECO:0000313|EMBL:BAC18231.1, ECO:0000313|Proteomes:UP000001409};
RN [1] {ECO:0000313|EMBL:BAC18231.1, ECO:0000313|Proteomes:UP000001409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395
RC {ECO:0000313|Proteomes:UP000001409};
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(2003).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004746}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR EMBL; BA000035; BAC18231.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8FPR9; -.
DR STRING; 196164.gene:10741835; -.
DR KEGG; cef:CE1421; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_3_11; -.
DR UniPathway; UPA00078; -.
DR Proteomes; UP000001409; Chromosome.
DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR005815; BioA.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00508; bioA; 1.
DR PANTHER; PTHR42684; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR PANTHER; PTHR42684:SF21; ADENOSYLMETHIONINE-8-AMINO-7-OXONONANOATE AMINOTRANSFERASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:BAC18231.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560};
KW Reference proteome {ECO:0000313|Proteomes:UP000001409};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAC18231.1}.
SQ SEQUENCE 380 AA; 40011 MW; 64F85FB3DA205A02 CRC64;
MSSWWSAVHG HGHPRLVAAA TAQAHRMSHV MFGGLTHEPA ARLTRALLEL VDAPLDTVFY
SDSGSVAVEV AVKMALQYSR GIGHPERTRL LTWRSGYHGD TFAAMSVCDP DGGMHSLWSG
VLAQQLFAPA PPVRGSDPQE LERYLDELES LVDDTVAAII IEPVVQGAGG MRFHDHRLVA
GVREICNRRG ILMIADEIAT GFGRTGSLFA TSAAGVTPDI LCVGKALTGG FMTLAATLCT
TAVADAITSP RGGGALMHGP TFMANPLACA VAAESLAIIA EGGWRSAVLG IDTELRAGLD
PLRREPGVAD VRVLGAIGVV EMTTPVDMIN ATRAAIAEGV WLRPFGRLIY VMPPYVCTTE
DIATICRGVA AAVRAAGSRP
//
