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Database: UniProt/TrEMBL
Entry: B6I653_ECOSE
LinkDB: B6I653_ECOSE
Original site: B6I653_ECOSE 
ID   B6I653_ECOSE            Unreviewed;       426 AA.
AC   B6I653;
DT   16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT   16-DEC-2008, sequence version 1.
DT   28-FEB-2018, entry version 52.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:BAG78439.1};
GN   OrderedLocusNames=ECSE_2915 {ECO:0000313|EMBL:BAG78439.1};
OS   Escherichia coli (strain SE11).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=409438 {ECO:0000313|EMBL:BAG78439.1, ECO:0000313|Proteomes:UP000008199};
RN   [1] {ECO:0000313|EMBL:BAG78439.1, ECO:0000313|Proteomes:UP000008199}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SE11 {ECO:0000313|EMBL:BAG78439.1,
RC   ECO:0000313|Proteomes:UP000008199};
RX   PubMed=18931093; DOI=10.1093/dnares/dsn026;
RA   Oshima K., Toh H., Ogura Y., Sasamoto H., Morita H., Park S.-H.,
RA   Ooka T., Iyoda S., Taylor T.D., Hayashi T., Itoh K., Hattori M.;
RT   "Complete genome sequence and comparative analysis of the wild-type
RT   commensal Escherichia coli strain SE11 isolated from a healthy
RT   adult.";
RL   DNA Res. 15:375-386(2008).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; AP009240; BAG78439.1; -; Genomic_DNA.
DR   RefSeq; WP_001087609.1; NC_011415.1.
DR   EnsemblBacteria; BAG78439; BAG78439; ECSE_2915.
DR   KEGG; ecy:ECSE_2915; -.
DR   HOGENOM; HOG000020206; -.
DR   KO; K07250; -.
DR   OMA; RVGNYLT; -.
DR   BioCyc; ECOL409438-HMP:GTSF-2966-MONOMER; -.
DR   Proteomes; UP000008199; Chromosome.
DR   GO; GO:0003867; F:4-aminobutyrate transaminase activity; IEA:InterPro.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 1.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 2.
DR   InterPro; IPR004632; 4NH2But_aminotransferase_bac.
DR   InterPro; IPR005814; Aminotrans_3.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_dom1.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00700; GABAtrnsam; 1.
DR   PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE   3: Inferred from homology;
KW   Aminotransferase {ECO:0000313|EMBL:BAG78439.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008199};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000313|EMBL:BAG78439.1}.
SQ   SEQUENCE   426 AA;  45759 MW;  D1F6FF048F726FB5 CRC64;
     MNSNKELMQR RSQAIPRGVG QIHPIFADRA ENCRVWDVEG REYLDFAGGI AVLNTGHLHP
     KVVAAVEAQL KKLSHTCFQV LAYEPYLELC EIMNQKVPGD FAKKTLLVTT GSEAVENAVK
     IARAATKRSG TIAFSGAYHG RTHYTLALTG KVNPYSAGMG LMPGHVYRAL YPCPLHGISE
     DDAIASIHRI FKNDAAPEDI AAIVIEPVQG EGGFYAASPA FMQRLRALCD EHGLMLIADE
     VQSGAGRTGT LFAMEQMGVA PDLTTFAKSI AGGFPLAGVT GRAEVMDAVA PGGLGGTYAG
     NPIACVAALE VLKVFEQENL LQKANDLGQK LKDGLLAIAE KHPEIGDVRG LGAMIAIELF
     EDGDHNKPDA KLTAEIVARA RDKGLILLSC GPYYNVLRIL VPLTIEDAQI RQGLEIISQC
     FDEAKQ
//
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