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-MAR-2024, entry version 59.
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; Pseudomonadota; 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 C9-1.";
RL J. Bacteriol. 192:6486-6487(2010).
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933};
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000256|ARBA:ARBA00008954,
CC ECO:0000256|RuleBase:RU003560}.
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DR EMBL; CP002206; ADO10062.1; -; Genomic_DNA.
DR RefSeq; WP_013358365.1; NC_014562.1.
DR AlphaFoldDB; E1SHY1; -.
DR KEGG; pva:Pvag_1877; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_10_0_6; -.
DR OrthoDB; 9801052at2; -.
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; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR InterPro; IPR004632; 4NH2But_aminotransferase_bac.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR049704; Aminotrans_3_PPA_site.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR NCBIfam; TIGR00700; GABAtrnsam; 1.
DR PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 1.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 2.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 3: Inferred from homology;
KW Aminotransferase {ECO:0000256|ARBA:ARBA00022576,
KW ECO:0000313|EMBL:ADO10062.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; 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
//
