ID G9A1F1_RHIFH Unreviewed; 460 AA.
AC G9A1F1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Aminotransferase, class III {ECO:0000313|EMBL:CCE97531.1};
DE EC=2.6.1.19 {ECO:0000313|EMBL:CCE97531.1};
GN OrderedLocusNames=SFHH103_03039 {ECO:0000313|EMBL:CCE97531.1};
OS Rhizobium fredii (strain HH103) (Sinorhizobium fredii).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=1117943 {ECO:0000313|EMBL:CCE97531.1, ECO:0000313|Proteomes:UP000007735};
RN [1] {ECO:0000313|EMBL:CCE97531.1, ECO:0000313|Proteomes:UP000007735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HH103 {ECO:0000313|EMBL:CCE97531.1,
RC 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 -!- 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; HE616890; CCE97531.1; -; Genomic_DNA.
DR AlphaFoldDB; G9A1F1; -.
DR STRING; 1117943.SFHH103_03039; -.
DR KEGG; sfh:SFHH103_03039; -.
DR PATRIC; fig|380.5.peg.3226; -.
DR eggNOG; COG0160; Bacteria.
DR HOGENOM; CLU_016922_8_0_5; -.
DR Proteomes; UP000007735; 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 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; 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 PANTHER; PTHR45688; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45688:SF3; ALANINE--GLYOXYLATE AMINOTRANSFERASE 2, MITOCHONDRIAL; 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:CCE97531.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|RuleBase:RU003560}; Transferase {ECO:0000313|EMBL:CCE97531.1}.
SQ SEQUENCE 460 AA; 49859 MW; F26425DC31F7C46C CRC64;
MGTAGKNIAR YMHVRFYGRN TPHPQALVSE GREMSGTQEI LARREKLLGS NVSTFYEKPV
HLVKGEGVWL WDADGRRYLD CYNNVPHVGH CHPRVVEAIA RQASTLNTHT RYLHEGILDY
VERLTGTFDR HLDTAILTCT GSEANDIALR MAQAVTGNTG VIATNHTYHG NTAAVSQLST
RMPPVGGYGG HVRHVPAPDS YRPLGGAPGS AFTDAWAAAL EEAIGSLQES PFGFSALIID
PFFANEGFPE LPDELLARVS AVVRKAGGLL ICDEVQPGFG RTGTHMWGHQ RAGIVPDIVT
LGKPMGNGHP IGGVVANADT LNAFRKAFRY FNTFGGNPVS CAAAMAVLDV LEDENLMENA
RTVGAHARFG LERLAERHGL IGDVRGSGLF FGCELVLDRP EKTPASHLAT RVVNEMRERG
VLMGKLGIHQ NATKIRPPMP FSRDNADLML STLDDVLTGL
//
