ID   G9AGF9_RHIFH            Unreviewed;       422 AA.
AC   G9AGF9;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   SubName: Full=4-aminobutyrate aminotransferase {ECO:0000313|EMBL:CCF00141.1};
DE            EC=2.6.1.22 {ECO:0000313|EMBL:CCF00141.1};
GN   Name=gabT {ECO:0000313|EMBL:CCF00141.1};
GN   OrderedLocusNames=SFHH103_05678 {ECO:0000313|EMBL:CCF00141.1};
OS   Rhizobium fredii (strain HH103) (Sinorhizobium fredii).
OG   Plasmid pSfHH103e {ECO:0000313|EMBL:CCF00141.1,
OG   ECO:0000313|Proteomes:UP000007735}.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=1117943 {ECO:0000313|EMBL:CCF00141.1, ECO:0000313|Proteomes:UP000007735};
RN   [1] {ECO:0000313|EMBL:CCF00141.1, ECO:0000313|Proteomes:UP000007735}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HH103 {ECO:0000313|EMBL:CCF00141.1,
RC   ECO:0000313|Proteomes:UP000007735};
RC   PLASMID=pSfHH103e {ECO:0000313|Proteomes:UP000007735};
RX   PubMed=22374952; DOI=10.1128/JB.06729-11;
RA   Weidner S., Becker A., Bonilla I., Jaenicke S., Lloret J., Margaret I.,
RA   Puhler A., Ruiz-Sainz J.E., Schneiker-Bekel S., Szczepanowski R.,
RA   Vinardell J.M., Zehner S., Gottfert M.;
RT   "Genome sequence of the soybean symbiont Sinorhizobium fredii HH103.";
RL   J. Bacteriol. 194:1617-1618(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; HE616899; CCF00141.1; -; Genomic_DNA.
DR   RefSeq; WP_014331795.1; NC_016815.1.
DR   AlphaFoldDB; G9AGF9; -.
DR   KEGG; sfh:SFHH103_05678; -.
DR   PATRIC; fig|380.5.peg.5237; -.
DR   HOGENOM; CLU_016922_10_0_5; -.
DR   Proteomes; UP000007735; Plasmid pSfHH103e.
DR   GO; GO:0047298; F:(S)-3-amino-2-methylpropionate transaminase activity; IEA:UniProtKB-EC.
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:CCF00141.1}; Plasmid {ECO:0000313|EMBL:CCF00141.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:CCF00141.1}.
SQ   SEQUENCE   422 AA;  45079 MW;  3428396E14656F30 CRC64;
     MTSLTDRKNA AISRGVGMTT QIYADRAENA EIWDKEGNRY IDFAAGIAVV NTGHRHPKVI
     AAVKAQLDRF THTCHQVVPY ENYVHLAERL NALAPGKFAK KTIFVTTGAE AVENAVKIAR
     AATGRQAIIA FGGGFHGRTF MGMALTGKVV PYKVGFGAMP ADVFHAPFPI ELHGVSVEQS
     LAALKKLFAA DVDPGRVAAI ILEPVQGEGG FYPAPTAFMK ALREICDQHG ILLIADEVQT
     GFARTGKLFA MEHHDVAPDL MTMAKSLAGG FPLAAVTGRA EIMDAPGPGG LGGTYGGNPI
     GIAAAHAVLD VIEEEQLCER ADQLGNRLKQ RLAAIREKAP EITDIRGPGF MNAVEFNDVK
     TNLPSAEFAN KVRLIALEKG LILLTCGVHG NVIRFLAPIT IQDEVFAEAL DILEASILEA
     RG
//