ID   A3P279_BURP0            Unreviewed;       427 AA.
AC   A3P279;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=4-aminobutyrate transaminase {ECO:0000313|EMBL:ABN92795.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:ABN92795.1};
GN   Name=gabT {ECO:0000313|EMBL:ABN92795.1};
GN   OrderedLocusNames=BURPS1106A_A0396 {ECO:0000313|EMBL:ABN92795.1};
OS   Burkholderia pseudomallei (strain 1106a).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=357348 {ECO:0000313|EMBL:ABN92795.1, ECO:0000313|Proteomes:UP000006738};
RN   [1] {ECO:0000313|Proteomes:UP000006738}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1106a {ECO:0000313|Proteomes:UP000006738};
RA   DeShazer D., Woods D.E., Nierman W.C.;
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000573; ABN92795.1; -; Genomic_DNA.
DR   RefSeq; WP_004529824.1; NC_009078.1.
DR   AlphaFoldDB; A3P279; -.
DR   GeneID; 56531262; -.
DR   KEGG; bpl:BURPS1106A_A0396; -.
DR   HOGENOM; CLU_016922_10_0_4; -.
DR   Proteomes; UP000006738; Chromosome II.
DR   GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
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:SF79; ACETYLORNITHINE AMINOTRANSFERASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 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:ABN92795.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:ABN92795.1}.
SQ   SEQUENCE   427 AA;  45151 MW;  370984C50CF7A603 CRC64;
     MNNADLHARK NAATPRGVGV MCDFYAARAE NAELWDVEGR RFIDFAAGIA VLNTGHRHPR
     IVKAIADQLG QFTHTAYQIV PYASYVELAE KINARAPIAQ PKKTAFFTTG AEAVENAVKI
     ARAYTGRPGM IAFAGGFHGR TMMGMALTGK VAPYKIGFGP FPGDVFHAPY PNALHGVTSA
     DSIAAVETLF KADIDPKRVA AIIFEPVQGE GGFNPAPAEF VRALRKLCDA HGILLIADEV
     QTGFARTGKL FAMEHYDVSA DLMTIAKSLA GGMPLSGVVG RADVMDAAAP GGLGGTYAGN
     PLAVAAAHAV LDVIDEEKLA ERATVLGDKL KAKLAALRAE LPQIVDVRGP GAMVAAEFVD
     PHTRASDAAF TKRVQTLALE RGLLLLICGV DANVIRFLFP LTIEDAVFDE ALGILESVLR
     EAVGVPA
//