ID Q2S151_SALRD Unreviewed; 327 AA. AC Q2S151; DT 24-JAN-2006, integrated into UniProtKB/TrEMBL. DT 24-JAN-2006, sequence version 1. DT 04-NOV-2026, entry version 114. DE SubName: Full=Pyruvate dehydrogenase E1 component, beta subunit {ECO:0000313|EMBL:ABC43655.1}; DE EC=1.2.4.1 {ECO:0000313|EMBL:ABC43655.1}; GN OrderedLocusNames=SRU_1970 {ECO:0000313|EMBL:ABC43655.1}; OS Salinibacter ruber (strain DSM 13855 / M31). OC Bacteria; Pseudomonadati; Rhodothermota; Rhodothermia; Rhodothermales; OC Salinibacteraceae; Salinibacter. OX NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC43655.1, ECO:0000313|Proteomes:UP000008674}; RN [1] {ECO:0000313|EMBL:ABC43655.1, ECO:0000313|Proteomes:UP000008674} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 13855 / CECT 5946 / M31 RC {ECO:0000313|Proteomes:UP000008674}; RX PubMed=16330755; DOI=10.1073/pnas.0509073102; RA Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H., RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K., RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L., RA Legault B., Rodriguez-Valera F.; RT "The genome of Salinibacter ruber: convergence and gene exchange among RT hyperhalophilic bacteria and archaea."; RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005). CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000256|ARBA:ARBA00001964}; 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; CP000159; ABC43655.1; -; Genomic_DNA. DR RefSeq; WP_011404705.1; NC_007677.1. DR AlphaFoldDB; Q2S151; -. DR STRING; 309807.SRU_1970; -. DR EnsemblBacteria; ABC43655; ABC43655; SRU_1970. DR KEGG; sru:SRU_1970; -. DR PATRIC; fig|309807.25.peg.2044; -. DR eggNOG; COG0022; Bacteria. DR HOGENOM; CLU_012907_1_1_10; -. DR OMA; AAHHSQC; -. DR OrthoDB; 9771835at2; -. DR Proteomes; UP000008674; Chromosome. DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC. DR CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1. DR FunFam; 3.40.50.920:FF:000001; Pyruvate dehydrogenase E1 beta subunit; 1. DR FunFam; 3.40.50.970:FF:000001; Pyruvate dehydrogenase E1 beta subunit; 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 NCBIfam; NF006667; PRK09212.1; 1. DR NCBIfam; NF008854; PRK11892.1; 1. DR PANTHER; PTHR43257; PYRUVATE DEHYDROGENASE E1 COMPONENT BETA SUBUNIT; 1. DR PANTHER; PTHR43257:SF2; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA; 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:0000256|ARBA:ARBA00023002, KW ECO:0000313|EMBL:ABC43655.1}; Pyruvate {ECO:0000313|EMBL:ABC43655.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000008674}; KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}. FT DOMAIN 4..179 FT /note="Transketolase-like pyrimidine-binding" FT /evidence="ECO:0000259|SMART:SM00861" SQ SEQUENCE 327 AA; 35869 MW; 71343D44C1D2202D CRC64; MATLEFRTAL REAMTEEMER DDDIFLIGEE VAEYDGAYKV SKGMLDHFGS DRVIDSPISE LGFAGLGIGA AMNGLRPIVE FMTFNFSFVA FDQVINNAPN MRYMSGGQFD VPIVFRGPNG AAGQLGATHS NSTEALYSNI PGLKVVSPSV PDDGKGLLKT AIRDDDPVVF LESELMYGMK REVSEESDYT IPIGSARVAR EGDDVTIVAH SKSYHIAMDA AETLEEQGYE AEVIDPRTIK PLDIETIVES VVKTNRLVVI DESTPFTSVA SEITHQVQDR AFDYLDAPIL RVTAPDTPAP YAPNLMDEYM PGADETVDKC LRVLYAE //