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Database: UniProt/TrEMBL
Entry: E1SHY1_PANVC
LinkDB: E1SHY1_PANVC
Original site: E1SHY1_PANVC 
ID   E1SHY1_PANVC            Unreviewed;       438 AA.
AC   E1SHY1;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-SEP-2017, entry version 43.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:ADO10062.1};
DE            EC=2.6.1.22 {ECO:0000313|EMBL:ADO10062.1};
GN   Name=gabT {ECO:0000313|EMBL:ADO10062.1};
GN   OrderedLocusNames=Pvag_1877 {ECO:0000313|EMBL:ADO10062.1};
OS   Pantoea vagans (strain C9-1) (Pantoea agglomerans (strain C9-1)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=712898 {ECO:0000313|EMBL:ADO10062.1, ECO:0000313|Proteomes:UP000006631};
RN   [1] {ECO:0000313|EMBL:ADO10062.1, ECO:0000313|Proteomes:UP000006631}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C9-1 {ECO:0000313|EMBL:ADO10062.1,
RC   ECO:0000313|Proteomes:UP000006631};
RX   PubMed=20952567; DOI=10.1128/JB.01122-10;
RA   Smits T.H., Rezzonico F., Kamber T., Goesmann A., Ishimaru C.A.,
RA   Stockwell V.O., Frey J.E., Duffy B.;
RT   "The genome sequence of the biocontrol agent Pantoea vagans strain C9-
RT   1.";
RL   J. Bacteriol. 192:6486-6487(2010).
CC   -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC       aminotransferase family. {ECO:0000256|RuleBase:RU003560}.
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DR   EMBL; CP002206; ADO10062.1; -; Genomic_DNA.
DR   RefSeq; WP_013358365.1; NC_014562.1.
DR   ProteinModelPortal; E1SHY1; -.
DR   STRING; 712898.Pvag_1877; -.
DR   EnsemblBacteria; ADO10062; ADO10062; Pvag_1877.
DR   KEGG; pva:Pvag_1877; -.
DR   eggNOG; ENOG4108JPW; Bacteria.
DR   eggNOG; COG0160; LUCA.
DR   HOGENOM; HOG000020206; -.
DR   KO; K07250; -.
DR   OMA; TGMSQPY; -.
DR   OrthoDB; POG091H0APS; -.
DR   Proteomes; UP000006631; Chromosome.
DR   GO; GO:0047298; F:(S)-3-amino-2-methylpropionate transaminase activity; IEA:UniProtKB-EC.
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:ADO10062.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006631};
KW   Pyridoxal phosphate {ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006631};
KW   Transferase {ECO:0000313|EMBL:ADO10062.1}.
SQ   SEQUENCE   438 AA;  46814 MW;  0B66D044FB660D18 CRC64;
     MQNVMAEQQA YSDNSLLLDA REQNVPRGVV TAHPLVIERA RGSEVWDVEG NRYLDFVGGI
     GVLNVGHNHP AVVNAVTRQL GLVSHACFQV VAYPGYIELA QRLNKLVGGD EAYKSVFFTS
     GAEAVENAVK IARSHTQRPG IIAFDGAFHG RTLLGITLTG MSAPYKQNFG PFPGDIYRLP
     FPNPLHGVTE ADCLKALDQL FAVQILPERV AAIIIEPVQG DGGFLPAGPA FMQALHRITS
     QHGILLICDE VQSGFGRTGT MFAFQQLGIK PDLITLAKSL GGGLPISGVV GRAAIMDAPT
     PGGLGGTYGG NALGCAAALA VLDLFEQENL LQRSCQLGEQ LNARLRQLAD KYACIGDVRG
     VGFMQAVEIL DFETGRPDAA LTQKILDSAC QEGLLLIKCG LHRNTIRFLA PLVTTDSQLE
     EALHIFDIAL ARATGRLG
//
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