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Database: UniProt
Entry: B7GHM5
LinkDB: B7GHM5
Original site: B7GHM5 
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-OCT-2014, entry version 39.
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};
GN   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.
CC       {ECO:0000255|HAMAP-Rule:MF_00834}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 8-amino-7-
CC       oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-
CC       diaminononanoate. {ECO:0000255|HAMAP-Rule:MF_00834}.
CC   -!- COFACTOR: Pyridoxal phosphate. {ECO:0000255|HAMAP-Rule:MF_00834}.
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-
CC       diaminononanoate from 8-amino-7-oxononanoate (SAM route): step
CC       1/1. {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   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; LVQSKET; -.
DR   OrthoDB; EOG6QVRHN; -.
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:UniProtKB-HAMAP.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-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   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 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; Complete proteome; Cytoplasm;
KW   Pyridoxal phosphate; Reference proteome; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN         1    454       Adenosylmethionine-8-amino-7-oxononanoate
FT                                aminotransferase.
FT                                /FTId=PRO_0000411121.
FT   REGION      119    120       Pyridoxal phosphate binding.
FT                                {ECO:0000255|HAMAP-Rule:MF_00834}.
FT   BINDING     152    152       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00834}.
FT   BINDING     257    257       Pyridoxal phosphate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00834}.
FT   BINDING     286    286       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00834}.
FT   BINDING     321    321       Substrate; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00834}.
FT   BINDING     416    416       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_00834}.
FT   SITE         23     23       Participates in the substrate recognition
FT                                with KAPA and in a stacking interaction
FT                                with the adenine ring of SAM.
FT                                {ECO:0000255|HAMAP-Rule:MF_00834}.
FT   MOD_RES     286    286       N6-(pyridoxal phosphate)lysine.
FT                                {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
//
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