ID   D4HXF1_ERWAC            Unreviewed;       420 AA.
AC   D4HXF1;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   SubName: Full=Putative 4-aminobutyrate aminotransferase {ECO:0000313|EMBL:CBA21637.1};
GN   Name=goaG {ECO:0000313|EMBL:CBA21637.1};
GN   OrderedLocusNames=EAMY_2391 {ECO:0000313|EMBL:CBA21637.1};
OS   Erwinia amylovora (strain CFBP1430).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=665029 {ECO:0000313|EMBL:CBA21637.1, ECO:0000313|Proteomes:UP000001841};
RN   [1] {ECO:0000313|EMBL:CBA21637.1, ECO:0000313|Proteomes:UP000001841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFBP1430 {ECO:0000313|Proteomes:UP000001841};
RX   PubMed=20192826; DOI=10.1094/MPMI-23-4-0384;
RA   Smits T.H., Rezzonico F., Kamber T., Blom J., Goesmann A., Frey J.E.,
RA   Duffy B.;
RT   "Complete genome sequence of the fire blight pathogen Erwinia amylovora
RT   CFBP 1430 and comparison to other Erwinia spp.";
RL   Mol. Plant Microbe Interact. 23:384-393(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; FN434113; CBA21637.1; -; Genomic_DNA.
DR   RefSeq; WP_004158639.1; NC_013961.1.
DR   AlphaFoldDB; D4HXF1; -.
DR   STRING; 665029.EAMY_2391; -.
DR   GeneID; 8911824; -.
DR   KEGG; eam:EAMY_2391; -.
DR   PATRIC; fig|665029.3.peg.2303; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_6; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000001841; Chromosome.
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:CBA21637.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:CBA21637.1}.
SQ   SEQUENCE   420 AA;  44686 MW;  C0A1A93EAAE7BDE2 CRC64;
     MNNRETDQRR LNATPRGVGV MCDFYVAKAE NATLWDEQGR EYTDFTAGIA VLNTGHRHPK
     VMAAVSAQLA CFTHTAYQVI PYENYIRLAE QLNQRVPIAG PCKTTFFSSG AEAVENAVKI
     ARAATGRPGV IAFSGAFHGR TLMTLGLTGK VTPYKTGFGP FPASVFHARY PNALHGFSVE
     DALESLQTLF KCDISPQQVA AIIYEPIQGE GGFNIAPDAF VSGLRKLCDQ HGIVMIADEI
     QTGFARSGKL FASEYYPDAQ PDLMTMAKSL GGGLPISAVS GRAELMDAPE PGGLGGTYAG
     NPLAIAAALA VLEVIEEEQL CARAQRLGAE LAEALNTSGC PALAEVRARG SMVAAEFNDP
     VSGKPSAAMA RSIQQRALEQ GLILLTCGVH GNVIRFLYPL TIPDAQFKAA LNLLASLLHG
//