ID   K0DU22_9BURK            Unreviewed;       429 AA.
AC   K0DU22;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:AFT88192.1};
GN   ORFNames=BUPH_00733 {ECO:0000313|EMBL:AFT88192.1};
OS   Paraburkholderia phenoliruptrix BR3459a.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1229205 {ECO:0000313|EMBL:AFT88192.1, ECO:0000313|Proteomes:UP000010105};
RN   [1] {ECO:0000313|EMBL:AFT88192.1, ECO:0000313|Proteomes:UP000010105}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BR3459a {ECO:0000313|EMBL:AFT88192.1,
RC   ECO:0000313|Proteomes:UP000010105};
RX   PubMed=23144415; DOI=10.1128/JB.01821-12;
RA   de Oliveira Cunha C., Goda Zuleta L.F., Paula de Almeida L.G.,
RA   Prioli Ciapina L., Lustrino Borges W., Pitard R.M., Baldani J.I.,
RA   Straliotto R., de Faria S.M., Hungria M., Sousa Cavada B., Mercante F.M.,
RA   Ribeiro de Vasconcelos A.T.;
RT   "Complete Genome Sequence of Burkholderia phenoliruptrix BR3459a (CLA1), a
RT   Heat-Tolerant, Nitrogen-Fixing Symbiont of Mimosa flocculosa.";
RL   J. Bacteriol. 194:6675-6676(2012).
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; CP003864; AFT88192.1; -; Genomic_DNA.
DR   RefSeq; WP_013590659.1; NC_018672.1.
DR   AlphaFoldDB; K0DU22; -.
DR   STRING; 1229205.BUPH_00733; -.
DR   GeneID; 27799465; -.
DR   KEGG; bpx:BUPH_00733; -.
DR   PATRIC; fig|1229205.11.peg.4618; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_4; -.
DR   Proteomes; UP000010105; Chromosome 2.
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: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:AFT88192.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:AFT88192.1}.
SQ   SEQUENCE   429 AA;  46016 MW;  E66946D5FB765405 CRC64;
     MNLKNADLKS RKDAATPRGV GVMCDFYAER AENAELWDVE GRRFIDFAAG IAVCNTGHRH
     PKIVAALRDQ LDHFTHTAYQ IVPYASYVEL AEKLNQRAPG DHPKKTAFFT TGAEAVENAI
     KIARAATGRP GVIAFTGGFH GRTLMGMALT GKVAPYKLGF GPFPSDVFHA PFPNPLHGVS
     TADSLKAIEF LFKADIDPKR VAAIIFEPVQ GEGGFYPAPV EFVRALRKLC NEHGILLIAD
     EVQTGFARTG KLFAMHHYDV VPDLMTVAKS LAGGMPLSGV IGRAEVMDAA APGGLGGTYA
     GNPLALAAAH AVLDIIDEEK LCERAVVLGE RVKTKLIALQ KDAPQIADVR GPGAMVAVEF
     CKPGSTEPDA DFTKRVQARA LERGLLLLVC GVYSNVVRFL FPLTIQDTVF DEALAILEDV
     IKDSVAVAA
//