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Database: UniProt
Entry: Q2FY53_STAA8
LinkDB: Q2FY53_STAA8
Original site: Q2FY53_STAA8 
ID   Q2FY53_STAA8            Unreviewed;       327 AA.
AC   Q2FY53;
DT   21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2006, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   SubName: Full=2-oxoisovalerate dehydrogenase, E1 component, beta subunit, putative {ECO:0000313|EMBL:ABD30691.1};
DE            EC=1.2.4.1 {ECO:0000313|EMBL:ABD30691.1};
GN   OrderedLocusNames=SAOUHSC_01612 {ECO:0000313|EMBL:ABD30691.1};
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061 {ECO:0000313|EMBL:ABD30691.1, ECO:0000313|Proteomes:UP000008816};
RN   [1] {ECO:0000313|Proteomes:UP000008816}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47 {ECO:0000313|Proteomes:UP000008816};
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington D.C
RL   (2006).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; CP000253; ABD30691.1; -; Genomic_DNA.
DR   RefSeq; WP_001096642.1; NZ_LS483365.1.
DR   RefSeq; YP_500127.1; NC_007795.1.
DR   AlphaFoldDB; Q2FY53; -.
DR   SMR; Q2FY53; -.
DR   STRING; 93061.SAOUHSC_01612; -.
DR   PaxDb; 1280-SAXN108_1540; -.
DR   GeneID; 3920028; -.
DR   KEGG; sao:SAOUHSC_01612; -.
DR   PATRIC; fig|93061.5.peg.1467; -.
DR   eggNOG; COG0022; Bacteria.
DR   HOGENOM; CLU_012907_1_0_9; -.
DR   OrthoDB; 9771835at2; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0009083; P:branched-chain amino acid catabolic process; IBA:GO_Central.
DR   GO; GO:0007584; P:response to nutrient; IBA:GO_Central.
DR   CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000313|EMBL:ABD30691.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008816}.
FT   DOMAIN          4..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   327 AA;  36061 MW;  05D8A4194F3B3D33 CRC64;
     MAKLSYLEAI RQAQDLALQQ NKDVFILGED VGRKGGVFGT TQGLQQKYGE DRVIDTPLAE
     SNIVGTAIGA AMVGKRPIAE IQFADFILPA TNQIISEAAK MRYRSNNDWQ CPLTIRAPFG
     GGVHGGLYHS QSIESIFASS PGLTIVIPST PYDAKGLLLS SIESNDPVLY FEHKKAYRFL
     KEEVPEEYYT VPLGKADVKR EGEDLTVFCY GLMVNYCLQA ADILAADGIN VEVVDLRTVY
     PLDKETIIDR AKHTGKVLLV TEDNLEGSIM SEVSAIIAEH CLFDLDAPIM RLAAPDVPSM
     PFSPVLENEI MMNPEKILNK MRELAEF
//
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