ID B1LM65_ECOSM Unreviewed; 450 AA.
AC B1LM65;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 29-MAY-2013, entry version 41.
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=EcSMS35_0797;
OS Escherichia coli (strain SMS-3-5 / SECEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=439855;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS-3-5 / SECEC;
RX PubMed=18708504; DOI=10.1128/JB.00661-08;
RA Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA Ravel J., Stepanauskas R.;
RT "Insights into the environmental resistance gene pool from the genome
RT sequence of the multidrug-resistant environmental isolate Escherichia
RT coli SMS-3-5.";
RL J. Bacteriol. 190:6779-6794(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.
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DR EMBL; CP000970; ACB15736.1; -; Genomic_DNA.
DR RefSeq; YP_001742877.1; NC_010498.1.
DR ProteinModelPortal; B1LM65; -.
DR SMR; B1LM65; 22-450.
DR STRING; 439855.EcSMS35_0797; -.
DR EnsemblBacteria; ACB15736; ACB15736; EcSMS35_0797.
DR GeneID; 6144408; -.
DR KEGG; ecm:EcSMS35_0797; -.
DR PATRIC; 18430431; VBIEscCol6161_0952.
DR eggNOG; COG0161; -.
DR HOGENOM; HOG000020209; -.
DR KO; K00833; -.
DR OMA; DRVFYAD; -.
DR ProtClustDB; PRK07986; -.
DR BioCyc; ECOL439855:GHHB-795-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 REGION 133 134 Pyridoxal phosphate binding (By
FT similarity).
FT REGION 329 330 Pyridoxal phosphate binding (By
FT similarity).
FT BINDING 73 73 Substrate (By similarity).
FT BINDING 165 165 Substrate (By similarity).
FT BINDING 266 266 Pyridoxal phosphate (By similarity).
FT BINDING 295 295 Substrate (By similarity).
FT BINDING 328 328 Substrate; via carbonyl oxygen (By
FT similarity).
FT BINDING 412 412 Substrate (By similarity).
FT SITE 38 38 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 295 295 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 450 AA; 49697 MW; C6B17F33C5DC7F30 CRC64;
MLLIRCRLVN LNLFNLVYKS IMTTDDLAFD QRHIWHPYTS MTSPLPVYPV ASAEGCELIL
SDGRRLVDGM SSWWAAIHGY NHPQLNAAMK SQIDAMSHVM FGGITHAPAI ELCRKLVAMT
PQPLECVFLA DSGSVAVEVA MKMALQYWQA KGEARQRFLT FRNGYHGDTF GAMSVCDPDN
SMHSLWKGYL PENLFAPAPQ SRLDGEWDER DMVGFARLMA AHRHEIAAVI IEPIVQGAGG
MRIYHPEWLK RIRKMCDREG ILLIADEIAT GFGRTGKLFA CEHAEIAPDI LCLGKALTGG
TMTLSATLTT REVAETISNG EAGCFMHGPT FMGNPLACAA ANASLAILES GDWQHQVAAI
EGQLREQLAP ACDAEMVADV RVLGAIGVVE TTRPVNMAAL QKFFVEQGVW IRPFGKLIYL
MPPYIILPQQ LQRLTAAVNR AVQDETFFCQ
//
