ID Q8D003_YERPE Unreviewed; 426 AA.
AC Q8D003; Q74W79;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2003, sequence version 1.
DT 01-MAY-2013, entry version 77.
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 AltName: Full=7,8-diaminononanoate synthase;
DE AltName: Full=Diaminopelargonic acid synthase;
GN Name=bioA; OrderedLocusNames=y3032, YP_1010;
OS Yersinia pestis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM, and KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/JB.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C.,
RA Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V.,
RA Straley S.C., McDonough K.A., Nilles M.L., Matson J.S., Blattner F.R.,
RA Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001, and 91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z.,
RA Jin L., Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J.,
RA Yang H., Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=91001;
RX PubMed=15262951; DOI=10.1128/JB.186.15.5147-5152.2004;
RA Zhou D., Tong Z., Song Y., Han Y., Pei D., Pang X., Zhai J., Li M.,
RA Cui B., Qi Z., Jin L., Dai R., Du Z., Wang J., Guo Z., Wang J.,
RA Huang P., Yang R.;
RT "Genetics of metabolic variations between Yersinia pestis biovars and
RT the proposal of a new biovar, microtus.";
RL J. Bacteriol. 186:5147-5152(2004).
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.
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DR EMBL; AE009952; AAM86583.1; -; Genomic_DNA.
DR EMBL; AE017042; AAS61261.1; -; Genomic_DNA.
DR RefSeq; NP_670332.1; NC_004088.1.
DR RefSeq; NP_992384.1; NC_005810.1.
DR HSSP; P12995; 1QJ3.
DR STRING; 187410.y3032; -.
DR DNASU; 1147979; -.
DR EnsemblBacteria; AAM86583; AAM86583; y3032.
DR EnsemblBacteria; AAS61261; AAS61261; YP_1010.
DR GeneID; 1147979; -.
DR GeneID; 2764786; -.
DR KEGG; ypk:y3032; -.
DR KEGG; ypm:YP_1010; -.
DR PATRIC; 18620380; VBIYerPes99487_1140.
DR HOGENOM; HOG000020209; -.
DR KO; K00833; -.
DR ProtClustDB; PRK07986; -.
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 REGION 112 113 Pyridoxal phosphate binding (By
FT similarity).
FT REGION 308 309 Pyridoxal phosphate binding (By
FT similarity).
FT BINDING 52 52 Substrate (By similarity).
FT BINDING 144 144 Substrate (By similarity).
FT BINDING 245 245 Pyridoxal phosphate (By similarity).
FT BINDING 274 274 Substrate (By similarity).
FT BINDING 307 307 Substrate; via carbonyl oxygen (By
FT similarity).
FT BINDING 391 391 Substrate (By similarity).
FT SITE 17 17 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 274 274 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 426 AA; 46661 MW; 9ED36823944D7462 CRC64;
MTPSDLVFDQ QHIWHPYTSM TEPLPCYPVV GAEGVELQLA DGRRLIDGMS SWWAAIHGYN
HPVLNFAAHQ QLDKMSHVMF GGITHPPAVK LCRQLVAMTP PPLECVFLAD SGSVSVEVAL
KMALQYWQAK GERRQRILTL RHGYHGDTFG AMSVCDPQNS MHSLYQGYLA ENLFANAPQC
GFDDPWDPQD IANFVALITQ HANEIAAVIL EPVVQGAGGM RIYHPSYLRE VRALCDKHQI
LLIADEIATG FGRTGKLFAC EHAQIVPDIL CLGKALTGGY LTLSATLTTR AVAETISKGD
AGCFMHGPTF MANPLACAVA SANLSLLAEN SWQQQVSKIE DQLKRELLPL AQEDTVADVR
VLGAIGVVEM KKPVNVARLQ RSFVEQGVWI RPFGKLIYLM PPYIISQHAL TRLTAAVAAA
VVDRGS
//
