GenomeNet

Database: UniProt/TrEMBL
Entry: B1LM65_ECOSM
LinkDB: B1LM65_ECOSM
Original site: B1LM65_ECOSM 
ID   B1LM65_ECOSM            Unreviewed;       450 AA.
AC   B1LM65;
DT   29-APR-2008, integrated into UniProtKB/TrEMBL.
DT   29-APR-2008, sequence version 1.
DT   26-NOV-2014, entry version 50.
DE   RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
DE            EC=2.6.1.62 {ECO:0000256|HAMAP-Rule:MF_00834};
DE   AltName: Full=7,8-diamino-pelargonic acid aminotransferase {ECO:0000256|HAMAP-Rule:MF_00834};
DE   AltName: Full=7,8-diaminononanoate synthase {ECO:0000256|HAMAP-Rule:MF_00834};
DE   AltName: Full=Diaminopelargonic acid synthase {ECO:0000256|HAMAP-Rule:MF_00834};
GN   Name=bioA {ECO:0000256|HAMAP-Rule:MF_00834,
GN   ECO:0000313|EMBL:ACB15736.1};
GN   OrderedLocusNames=EcSMS35_0797 {ECO:0000313|EMBL:ACB15736.1};
OS   Escherichia coli (strain SMS-3-5 / SECEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=439855 {ECO:0000313|EMBL:ACB15736.1, ECO:0000313|Proteomes:UP000007011};
RN   [1] {ECO:0000313|EMBL:ACB15736.1, ECO:0000313|Proteomes:UP000007011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SMS-3-5 / SECEC {ECO:0000313|Proteomes:UP000007011};
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.
CC       {ECO:0000256|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:0000256|HAMAP-Rule:MF_00834}.
CC   -!- COFACTOR:
CC       Note=Pyridoxal phosphate. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00834}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00834}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834}.
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. BioA subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00834}.
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; CP000970; ACB15736.1; -; Genomic_DNA.
DR   RefSeq; WP_012311601.1; NC_010498.1.
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; PWQERRG; -.
DR   OrthoDB; EOG6QVRHN; -.
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: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 {ECO:0000256|HAMAP-Rule:MF_00834,
KW   ECO:0000313|EMBL:ACB15736.1};
KW   Biotin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Complete proteome {ECO:0000313|Proteomes:UP000007011};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_00834};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_00834};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00834,
KW   ECO:0000313|EMBL:ACB15736.1}.
FT   REGION      133    134       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   REGION      329    330       Pyridoxal phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   BINDING      73     73       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   BINDING     165    165       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   BINDING     266    266       Pyridoxal phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_00834}.
FT   BINDING     295    295       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   BINDING     328    328       Substrate; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   BINDING     412    412       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00834}.
FT   SITE         38     38       Participates in the substrate recognition
FT                                with KAPA and in a stacking interaction
FT                                with the adenine ring of SAM.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
FT   MOD_RES     295    295       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_00834}.
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
//
DBGET integrated database retrieval system