BIOA_ANOFW
ID BIOA_ANOFW Reviewed; 454 AA.
AC B7GHM5;
DT 27-JUL-2011, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000255|HAMAP-Rule:MF_00834};
DE EC=2.6.1.62 {ECO:0000255|HAMAP-Rule:MF_00834};
DE AltName: Full=7,8-diamino-pelargonic acid aminotransferase {ECO:0000255|HAMAP-Rule:MF_00834};
DE Short=DAPA AT {ECO:0000255|HAMAP-Rule:MF_00834};
DE Short=DAPA aminotransferase {ECO:0000255|HAMAP-Rule:MF_00834};
DE AltName: Full=7,8-diaminononanoate synthase {ECO:0000255|HAMAP-Rule:MF_00834};
DE Short=DANS {ECO:0000255|HAMAP-Rule:MF_00834};
DE AltName: Full=Diaminopelargonic acid synthase {ECO:0000255|HAMAP-Rule:MF_00834};
GN Name=bioA {ECO:0000255|HAMAP-Rule:MF_00834}; OrderedLocusNames=Aflv_1071;
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1;
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(2008).
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. {ECO:0000255|HAMAP-
CC Rule:MF_00834}.
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; Evidence={ECO:0000255|HAMAP-Rule:MF_00834};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00834};
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
CC diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00834}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00834}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00834}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. BioA subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00834}.
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DR EMBL; CP000922; ACJ33447.1; -; Genomic_DNA.
DR RefSeq; WP_012574710.1; NC_011567.1.
DR AlphaFoldDB; B7GHM5; -.
DR SMR; B7GHM5; -.
DR STRING; 491915.Aflv_1071; -.
DR EnsemblBacteria; ACJ33447; ACJ33447; Aflv_1071.
DR KEGG; afl:Aflv_1071; -.
DR PATRIC; fig|491915.6.peg.1093; -.
DR eggNOG; COG0161; Bacteria.
DR HOGENOM; CLU_016922_4_3_9; -.
DR OMA; VAVKMCL; -.
DR OrthoDB; 478143at2; -.
DR UniPathway; UPA00078; UER00160.
DR Proteomes; UP000000742; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR HAMAP; MF_00834; BioA; 1.
DR InterPro; IPR005814; Aminotrans_3.
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 Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR TIGRFAMs; TIGR00508; bioA; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Biotin biosynthesis; Cytoplasm; Pyridoxal phosphate;
KW Reference proteome; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1..454
FT /note="Adenosylmethionine-8-amino-7-oxononanoate
FT aminotransferase"
FT /id="PRO_0000411121"
FT BINDING 119..120
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 152
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 257
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 321
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT BINDING 416
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT SITE 23
FT /note="Participates in the substrate recognition with KAPA
FT and in a stacking interaction with the adenine ring of SAM"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
FT MOD_RES 286
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00834"
SQ SEQUENCE 454 AA; 51193 MW; 407ED6A6C90F4781 CRC64;
MEKGMVAMNE WIEKSKTYLW LPFTQMKDYE QHPLVIESGE GIFLTDVNGK TYYDGYSSLW
LNVHGHRKKE IDDAIRAQLE RIAHSTLLGA ANIPAIALAE KLIEWTPSHL TRVFYSDSGA
EAVEIALKIA FQYWRNIGEN KKQKFVTLAN GYHGDTVGAI SVGAIDIFHT VYEPLMFTSY
KAPFPLVYRH PSNDPNVVRD EALGALEALF AEHHEEIAAM IVEGMIQGAG GMHVMPKGYL
KGVEQLCRQY NILFIVDEVA TGFGRTGKRF AIEHEDVQPD IMTVAKGITG GYLPIAATLT
TEAIYEAFYG DYTEFKTFFH GHSYTGNQLG CAAALANIQI FERERLIEQI QQKATFVAEQ
LASFNELNHV GDVRQLGLMC GIELVRDRRT HEPYPWTERM GYRTTLTMRE KGMLTRPLGD
VIVFMPPLAS TFEQLEAMIA MMKEAIIETT EKRG
