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Database: UniProt/TrEMBL
Entry: A0A0H2Z228_ECOK1
LinkDB: A0A0H2Z228_ECOK1
Original site: A0A0H2Z228_ECOK1 
ID   A0A0H2Z228_ECOK1        Unreviewed;       428 AA.
AC   A0A0H2Z228;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   28-FEB-2018, entry version 11.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ABJ02097.1};
GN   Name=gabT {ECO:0000313|EMBL:ABJ02097.1};
GN   ORFNames=APECO1_3858 {ECO:0000313|EMBL:ABJ02097.1};
OS   Escherichia coli O1:K1 / APEC.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=405955 {ECO:0000313|EMBL:ABJ02097.1, ECO:0000313|Proteomes:UP000008216};
RN   [1] {ECO:0000313|EMBL:ABJ02097.1, ECO:0000313|Proteomes:UP000008216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APEC O1 {ECO:0000313|EMBL:ABJ02097.1};
RX   PubMed=17293413; DOI=10.1128/JB.01726-06;
RA   Johnson T.J., Kariyawasam S., Wannemuehler Y., Mangiamele P.,
RA   Johnson S.J., Doetkott C., Skyberg J.A., Lynne A.M., Johnson J.R.,
RA   Nolan L.K.;
RT   "The genome sequence of avian pathogenic Escherichia coli strain
RT   O1:K1:H7 shares strong similarities with human extraintestinal
RT   pathogenic E. coli genomes.";
RL   J. Bacteriol. 189:3228-3236(2007).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP000468; ABJ02097.1; -; Genomic_DNA.
DR   ProteinModelPortal; A0A0H2Z228; -.
DR   EnsemblBacteria; ABJ02097; ABJ02097; APECO1_3858.
DR   KEGG; ecv:APECO1_3858; -.
DR   KO; K07250; -.
DR   OMA; RVGNYLT; -.
DR   Proteomes; UP000008216; 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:ABJ02097.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008216};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Transferase {ECO:0000313|EMBL:ABJ02097.1}.
SQ   SEQUENCE   428 AA;  45917 MW;  EAAB37CE1D7D5E35 CRC64;
     MRMSSNKELM QRRSQAIPRG VGQIHPIFAD RAENCRVWDV EGREYLDFAG GIAVLNTGHL
     HPKVVAAVEA QLKKLSHTCF QVLAYEPYLE LCEIMNQKVP GDFAKKTLLV TTGSEAVENA
     VKIARAATKR SGTIAFSGAY HGRTHYTLAL TGKVNPYSAG MGLMPGHVYR ALYPCPLHGI
     SEDDAIASIH RIFKNDAAPE DIAAIVIEPV QGEGGFYAAT PAFMQRLRAL CDEHGIMLIA
     DEVQSGAGRT GTLFAMEQMG VAPDLTTFAK SIAGGFPLAG VTGRAEVMDA VAPGGLGGTY
     AGNPIACVAA LEVLKVFEQE NLLQKANDLG QKLKDGLLAI AEKHTEIGDV RGLGAMIAIE
     LFEDGDHSKP DAKLTAEIVA RARDKGLILL SCGPYNNVLR ILVPLTIEDA QIRQGLEIIS
     QCFAEAKQ
//
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