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Database: UniProt/TrEMBL
Entry: A0A0E0V8C0_ECOLX
LinkDB: A0A0E0V8C0_ECOLX
Original site: A0A0E0V8C0_ECOLX 
ID   A0A0E0V8C0_ECOLX        Unreviewed;       426 AA.
AC   A0A0E0V8C0;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   07-JUN-2017, entry version 12.
DE   SubName: Full=4-aminobutyrate aminotransferase, PLP-dependent {ECO:0000313|EMBL:AEQ13822.1};
GN   Name=gabT {ECO:0000313|EMBL:AEQ13822.1};
GN   ORFNames=CE10_3080 {ECO:0000313|EMBL:AEQ13822.1};
OS   Escherichia coli O7:K1 str. CE10.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=1072459 {ECO:0000313|EMBL:AEQ13822.1, ECO:0000313|Proteomes:UP000002657};
RN   [1] {ECO:0000313|EMBL:AEQ13822.1, ECO:0000313|Proteomes:UP000002657}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CE10 {ECO:0000313|EMBL:AEQ13822.1};
RX   PubMed=22123760; DOI=10.1128/JB.06284-11;
RA   Lu S., Zhang X., Zhu Y., Kim K.S., Yang J., Jin Q.;
RT   "Complete Genome Sequence of the Neonatal-Meningitis-Associated
RT   Escherichia coli Strain CE10.";
RL   J. Bacteriol. 193:7005-7005(2011).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP003034; AEQ13822.1; -; Genomic_DNA.
DR   RefSeq; WP_000097669.1; NC_017646.1.
DR   ProteinModelPortal; A0A0E0V8C0; -.
DR   EnsemblBacteria; AEQ13822; AEQ13822; CE10_3080.
DR   KEGG; eoc:CE10_3080; -.
DR   PATRIC; fig|1072459.4.peg.3120; -.
DR   KO; K07250; -.
DR   Proteomes; UP000002657; 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; IPR015421; PyrdxlP-dep_Trfase_major_sub1.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_sub2.
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:AEQ13822.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002657};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000313|EMBL:AEQ13822.1}.
SQ   SEQUENCE   426 AA;  45575 MW;  3D5A4F8533AA45C4 CRC64;
     MSSNKELMQR RSQAVPRGVG QIHPIFADRA ENCRVWDVEG REYLDFAGGI AVLNTGHLHP
     KVVAAVEAQL KKLSHTCFQV LAYEPYLELC EIMNQKVPGD FAKKTLLVTT GSEAVENAVK
     IARAATKRSG TIAFSGAYHG RTHYTLALTG KVNPYSAGMG LMPGHVYRAL YPCPLHGISE
     DDAIASIHRI FKNDAAPEDI AAIVIEPVQG EGGFYAATPA FMLRLRALCD EHGIMLIADE
     VQSGAGRTGT LFAMEQMGVA PDLTTFAKSI AGGFPLAGVT GRAEVMDAVA PGGLGGTYAG
     NPIACVAALE VLKVFEQENL LQKANVLGQK LKDGLLAIAE KHPEIGDVRG LGAMIAIELF
     EDGDPSKPDA KLTAEIVARA RDKGLILLSC GPYYNVLRIL VPLTIEDAQI RQGLEIISQC
     FAEAKL
//
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