ID   E3HG15_ACHXA            Unreviewed;       421 AA.
AC   E3HG15;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=4-aminobutyrate transaminase 2 {ECO:0000313|EMBL:ADP17788.1};
DE            EC=2.6.1.19 {ECO:0000313|EMBL:ADP17788.1};
GN   Name=gabT2 {ECO:0000313|EMBL:ADP17788.1};
GN   OrderedLocusNames=AXYL_04469 {ECO:0000313|EMBL:ADP17788.1};
OS   Achromobacter xylosoxidans (strain A8).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP17788.1, ECO:0000313|Proteomes:UP000006876};
RN   [1] {ECO:0000313|EMBL:ADP17788.1, ECO:0000313|Proteomes:UP000006876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A8 {ECO:0000313|EMBL:ADP17788.1,
RC   ECO:0000313|Proteomes:UP000006876};
RX   PubMed=21097610; DOI=10.1128/JB.01299-10;
RA   Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT   "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT   Achromobacter xylosoxidans A8.";
RL   J. Bacteriol. 193:791-792(2011).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002287; ADP17788.1; -; Genomic_DNA.
DR   RefSeq; WP_013395096.1; NC_014640.1.
DR   AlphaFoldDB; E3HG15; -.
DR   STRING; 762376.AXYL_04469; -.
DR   KEGG; axy:AXYL_04469; -.
DR   PATRIC; fig|762376.5.peg.4481; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_4; -.
DR   OrthoDB; 3398487at2; -.
DR   Proteomes; UP000006876; Chromosome.
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; 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:ADP17788.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:ADP17788.1}.
SQ   SEQUENCE   421 AA;  44469 MW;  CA49FDD3B05BA704 CRC64;
     MKNQDLNTRR SLATPRGVGV MCDFYAVRAE NATLWDANGK EYIDFAGGIA VLNTGHLHPK
     IKAAVAAQLD NFTHTAYQIV PYEGYVSLAE RINRLAPIDG LKKSAFFTTG VEAVENAVKI
     ARSATGRSGV IAFSGSFHGR TMLGMALTGK VAPYKLSFGP MPGDIYHVPF PNATQSISVA
     DSLKALDLLF KCDIDPKRVA AIIIEPVQGE GGFNITPPEL MTALRKVCDE HGILLIADEV
     QTGFGRTGKL FAMEHHSVQA DLITMAKSLG GGFPISGVVG RADVMDAPAA GGLGGTYAGN
     PLAVAAAHAV LDVIAEEKLC ERADALGDKL RAHLEGLRAK VPGIADVRGL GSMVALELND
     PATGKPDAEA VKRVQARAIE KGLILLSCGV YGNVLRFLYP LTIPDAQFDR ALAILSEALA
     A
//