ID   Q39AW5_BURL3            Unreviewed;       429 AA.
AC   Q39AW5;
DT   22-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2005, sequence version 1.
DT   02-SEP-2026, entry version 102.
DE   SubName: Full=4-aminobutyrate aminotransferase apoenzyme {ECO:0000313|EMBL:ABB10396.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:ABB10396.1};
GN   OrderedLocusNames=Bcep18194_B0280 {ECO:0000313|EMBL:ABB10396.1};
OS   Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 /
OS   R18194 / 383).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC   Burkholderiales; Burkholderiaceae; Burkholderia;
OC   Burkholderia cepacia complex.
OX   NCBI_TaxID=482957 {ECO:0000313|EMBL:ABB10396.1, ECO:0000313|Proteomes:UP000002705};
RN   [1] {ECO:0000313|EMBL:ABB10396.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=383 {ECO:0000313|EMBL:ABB10396.1};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA   Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 2 of Burkholderia sp. 383.";
RL   Submitted (OCT-2005) 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; CP000152; ABB10396.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q39AW5; -.
DR   KEGG; bur:Bcep18194_B0280; -.
DR   PATRIC; fig|482957.22.peg.3862; -.
DR   HOGENOM; CLU_016922_10_0_4; -.
DR   Proteomes; UP000002705; Chromosome 2.
DR   GO; GO:0034386; F:4-aminobutyrate:2-oxoglutarate transaminase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042802; F:identical protein binding; IEA:TreeGrafter.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   CDD; cd00610; OAT_like; 1.
DR   FunFam; 3.40.640.10:FF:000013; 4-aminobutyrate aminotransferase; 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; IPR050103; Class-III_PLP-dep_AT.
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   NCBIfam; NF005272; PRK06777.1; 1.
DR   PANTHER; PTHR11986; AMINOTRANSFERASE CLASS III; 1.
DR   Pfam; PF00202; Aminotran_3; 1.
DR   PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
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:ABB10396.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002705};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABB10396.1}.
SQ   SEQUENCE   429 AA;  45781 MW;  E76764FAFC6E04CA CRC64;
     MTVKNADLQA RKNAATPRGV GVMCDFYAAR AENAELWDVE GRRFIDFAAG IAVLNTGHRH
     PKIVKAISDQ LNNFTHTAYQ IVPYASYVEL AEKINARAPG DFPKKTAFFT TGAEAVENAI
     KIARAATGRP GVIAFSGGFH GRTMMGMALT GKVAPYKLNF GPFPGDVFHA PYPNAVHGVT
     TADSIKAIEM LFKADIDPKR VAAIIFEPVQ GEGGFYAAPA EFVRALRKIC NEHGILLIAD
     EVQTGFARTG KLFAMQHYDV LADLITMAKS LAGGMPLSGV VGRADVMDAA APGGLGGTYA
     GNPLAVASAH AVLEIIDEEK LCERATQFGD VLKAKLNALQ ADVPQIADVR GPGAMIAVEF
     LKPGSGEPDA EFTKRVQTRA LERGLLLLVC GVYSNVVRFL FPLTIPQAVF DEALVILEEV
     LKETVGVPA
//