ID   E8T8G7_MESCW            Unreviewed;       332 AA.
AC   E8T8G7;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   OrderedLocusNames=Mesci_1464 {ECO:0000313|EMBL:ADV10623.1};
OS   Mesorhizobium ciceri biovar biserrulae (strain HAMBI 2942 / LMG 23838 /
OS   WSM1271).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=765698 {ECO:0000313|EMBL:ADV10623.1, ECO:0000313|Proteomes:UP000007471};
RN   [1] {ECO:0000313|Proteomes:UP000007471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAMBI 2942 / LMG 23838 / WSM1271
RC   {ECO:0000313|Proteomes:UP000007471};
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Teshima H., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Nandasena K., Reeve W.G., Howieson J.G., O'Hara G.,
RA   Tiwari R.P., Woyke T.;
RT   "Complete sequence of chromosome of Mesorhizobium ciceri bv. biserrulae
RT   WSM1271.";
RL   Submitted (JAN-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC       copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC       dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC       (E3). {ECO:0000256|ARBA:ARBA00025211}.
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC       {ECO:0000256|ARBA:ARBA00011870}.
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; CP002447; ADV10623.1; -; Genomic_DNA.
DR   RefSeq; WP_013529315.1; NC_014923.1.
DR   RefSeq; YP_004140673.1; NC_014923.1.
DR   AlphaFoldDB; E8T8G7; -.
DR   STRING; 765698.Mesci_1464; -.
DR   KEGG; mci:Mesci_1464; -.
DR   PATRIC; fig|765698.3.peg.1906; -.
DR   eggNOG; COG0022; Bacteria.
DR   HOGENOM; CLU_012907_1_1_5; -.
DR   OrthoDB; 9780894at2; -.
DR   Proteomes; UP000007471; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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; 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;
FT   DOMAIN          8..183
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   332 AA;  35678 MW;  8ACF6C867E7AEAA7 CRC64;
     MDAMVRELSY AQAIQEAMAI AMDMDERVFL MGEDIGVYGG AFQVTGDLVE RYGADRVIDT
     PISELGGAGV AVGAALTGMR PIFEFQFSDF ATLAMEQIVN QAAKMRFMLG GEVSVPVVMR
     FPAGSGTGAA AQHSQSLEAW LGHVPGLKVI QPATPYDAKG MLLAAVADPD PVMIFEHKLL
     YKMKGPVPEG YYTVPIGKAD IRREGRDLTI VATSIMVQKA LDAAAVLESE GIDVEVVDLR
     TIRPMDKQTV IDSVKKTSRL LCVYEAVKTL GIGAEVSAMI AESEAFDYLD APIVRLGGAE
     TPIPYNPELE KVTVPQIPDI ITAARDLVKG VR
//