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 01-MAY-2013, entry version 32.
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; 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.,
RA 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
CC (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only
CC animotransferase known to utilize SAM as an amino donor (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 8-amino-7-
CC oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-
CC diaminononanoate.
CC -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
CC diaminononanoate from 8-amino-7-oxononanoate (SAM route): step
CC 1/1.
CC -!- SUBUNIT: Homodimer (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. BioA subfamily.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; CP000922; ACJ33447.1; -; Genomic_DNA.
DR RefSeq; YP_002315432.1; NC_011567.1.
DR ProteinModelPortal; B7GHM5; -.
DR STRING; 491915.Aflv_1071; -.
DR EnsemblBacteria; ACJ33447; ACJ33447; Aflv_1071.
DR GeneID; 7037328; -.
DR KEGG; afl:Aflv_1071; -.
DR PATRIC; 20953967; VBIAnoFla45531_1093.
DR eggNOG; COG0161; -.
DR HOGENOM; HOG000020209; -.
DR KO; K00833; -.
DR OMA; RENETIT; -.
DR ProtClustDB; PRK06916; -.
DR BioCyc; AFLA491915:GHEO-1146-MONOMER; -.
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:HAMAP.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:HAMAP.
DR GO; GO:0009102; P:biotin biosynthetic process; IEA:HAMAP.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 2.
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_sub1.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2.
DR PANTHER; PTHR11986; PTHR11986; 1.
DR PANTHER; PTHR11986:SF8; PTHR11986:SF8; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR SUPFAM; SSF53383; PyrdxlP-dep_Trfase_major; 1.
DR TIGRFAMs; TIGR00508; bioA; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase; Biotin biosynthesis; Complete proteome; Cytoplasm;
KW Pyridoxal phosphate; S-adenosyl-L-methionine; Transferase.
FT CHAIN 1 454 Adenosylmethionine-8-amino-7-oxononanoate
FT aminotransferase.
FT /FTId=PRO_0000411121.
FT REGION 119 120 Pyridoxal phosphate binding (By
FT similarity).
FT BINDING 152 152 Substrate (By similarity).
FT BINDING 257 257 Pyridoxal phosphate (By similarity).
FT BINDING 286 286 Substrate (By similarity).
FT BINDING 321 321 Substrate; via carbonyl oxygen (By
FT similarity).
FT BINDING 416 416 Substrate (By similarity).
FT SITE 23 23 Participates in the substrate recognition
FT with KAPA and in a stacking interaction
FT with the adenine ring of SAM (By
FT similarity).
FT MOD_RES 286 286 N6-(pyridoxal phosphate)lysine (By
FT similarity).
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
//
