ID   B2VIX6_ERWT9            Unreviewed;       420 AA.
AC   B2VIX6;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:CAO96236.1};
GN   Name=goaG {ECO:0000313|EMBL:CAO96236.1};
GN   OrderedLocusNames=ETA_11900 {ECO:0000313|EMBL:CAO96236.1};
OS   Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB
OS   4357 / Et1/99).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=465817 {ECO:0000313|EMBL:CAO96236.1, ECO:0000313|Proteomes:UP000001726};
RN   [1] {ECO:0000313|EMBL:CAO96236.1, ECO:0000313|Proteomes:UP000001726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99
RC   {ECO:0000313|Proteomes:UP000001726};
RX   PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x;
RA   Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R.,
RA   Geider K.;
RT   "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic
RT   bacterium in the genus Erwinia.";
RL   Environ. Microbiol. 10:2211-2222(2008).
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; CU468135; CAO96236.1; -; Genomic_DNA.
DR   RefSeq; WP_012440933.1; NC_010694.1.
DR   AlphaFoldDB; B2VIX6; -.
DR   STRING; 465817.ETA_11900; -.
DR   KEGG; eta:ETA_11900; -.
DR   eggNOG; COG0160; Bacteria.
DR   HOGENOM; CLU_016922_10_0_6; -.
DR   OrthoDB; 9801052at2; -.
DR   Proteomes; UP000001726; 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:CAO96236.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001726};
KW   Transferase {ECO:0000256|ARBA:ARBA00022576, ECO:0000313|EMBL:CAO96236.1}.
SQ   SEQUENCE   420 AA;  45221 MW;  B48546BE8AB9B456 CRC64;
     MNNRETERRR LDATPRGVGV MCDFYAVKAE NATLWDEQGR EYTDFTAGIA VLNTGHRHPK
     VMAAVHAQLE CFTHTAYQVI PYENYIRLAE RLNHQVPIDG PCKTTFFSSG AEAVENAVKI
     ARAATGRPGV IAFSGAFHGR TLLTMGLTGK VTPYKTGFGP FPASVFHARY PNALHGYSVE
     DALESLETLF KCDISPQQVA AIIYEPIQGE GGFNIAPEAF VSALRKLCDQ HGILLIADEI
     QTGFARSGKL FASEYYPDAR PDLMTMAKSL GGGLPISAVS GRAELMDAPE PGGLGGTYAG
     NPLAIAAALA VLEVIEEEQL CTRALRLGAE LVEALNSSGC AALAEVRARG SMVAAEFNDP
     IDGRPSSAIA RRIQQRALEQ GLILLTCGVH GNVIRFLYPL TIPDAQFKTA LKLIASLLRD
//