ID   A0A1Y6G2A3_9BACI        Unreviewed;       456 AA.
AC   A0A1Y6G2A3;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=4-aminobutyrate aminotransferase apoenzyme {ECO:0000313|EMBL:SMQ83725.1};
GN   ORFNames=SAMN05444673_5535 {ECO:0000313|EMBL:SMQ83725.1};
OS   Bacillus sp. OV166.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1882763 {ECO:0000313|EMBL:SMQ83725.1, ECO:0000313|Proteomes:UP000194454};
RN   [1] {ECO:0000313|EMBL:SMQ83725.1, ECO:0000313|Proteomes:UP000194454}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV166 {ECO:0000313|EMBL:SMQ83725.1};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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}.
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; FXWM01000001; SMQ83725.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y6G2A3; -.
DR   OrthoDB; 9807885at2; -.
DR   Proteomes; UP000194454; Unassembled WGS sequence.
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; AMINOTRANSFERASE CLASS III; 1.
DR   PANTHER; PTHR11986:SF58; LEUCINE_METHIONINE RACEMASE; 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:0000313|EMBL:SMQ83725.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:SMQ83725.1}.
SQ   SEQUENCE   456 AA;  50141 MW;  113440A4C6F67C16 CRC64;
     MEKKYVKLQT EIPGPKSKEI LEQRNKYVPK GISNNCQAFV KKAQGALVED VDGNCYIDFA
     GAIGTINVGH SHPRVVRALQ EQASQFIHTG FNVMMYESYI TLAERLCILA PGEFDKQAAF
     FNSGAEAVEN AVKIARKYTK RQGIISFTRG FHGRTLMTMT MTSKVKPYKF GFGPFAPEVY
     KAPYPYVYRR PEGTNEQQYS AMIIEQFEQF LLAEVAPETI AAVVMEPVQG EGGFIVPDTA
     FVKRVREICT QYGILFIADE IQTGFARTGK YFAIDHFEVV PDLITISKSM GAGVPISGVI
     GRAEIMSTPE VGEIGGTYAG SPLGCRAALT VLDIIESEQL NDRARKIGDR VIEKMQLLAD
     RFEGIGDVRG LGAMCAMEIV QDRQSKTPDK DATGKIVKAA GERGLMLLSA GLYSNVIRLL
     MPITITDDQL EEGLQILEEA MEAVYHNDPA LSVGGE
//