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Database: UniProt
Entry: D3FD88_CONWI
LinkDB: D3FD88_CONWI
Original site: D3FD88_CONWI 
ID   D3FD88_CONWI            Unreviewed;       325 AA.
AC   D3FD88;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   OrderedLocusNames=Cwoe_5071 {ECO:0000313|EMBL:ADB53480.1};
OS   Conexibacter woesei (strain DSM 14684 / CIP 108061 / JCM 11494 / NBRC
OS   100937 / ID131577).
OC   Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC   Conexibacteraceae; Conexibacter.
OX   NCBI_TaxID=469383 {ECO:0000313|EMBL:ADB53480.1, ECO:0000313|Proteomes:UP000008229};
RN   [1] {ECO:0000313|EMBL:ADB53480.1, ECO:0000313|Proteomes:UP000008229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14684 / CIP 108061 / JCM 11494 / NBRC 100937 / ID131577
RC   {ECO:0000313|Proteomes:UP000008229};
RX   PubMed=21304704;
RA   Pukall R., Lapidus A., Glavina Del Rio T., Copeland A., Tice H.,
RA   Cheng J.-F., Lucas S., Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S.,
RA   Mavromatis K., Ivanova N., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.-J., Jeffries C.D., Chain P.,
RA   Meincke L., Sims D., Brettin T., Detter J.C., Rohde M., Goeker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Kyrpides N.C., Klenk H.-P.,
RA   Hugenholtz P.;
RT   "Complete genome sequence of Conexibacter woesei type strain (ID131577).";
RL   Stand. Genomic Sci. 2:212-219(2010).
RN   [2] {ECO:0000313|Proteomes:UP000008229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14684 / CIP 108061 / JCM 11494 / NBRC 100937 / ID131577
RC   {ECO:0000313|Proteomes:UP000008229};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA   Mikhailova N., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F.,
RA   Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA   Wu D., Pukall R., Steenblock K., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Conexibacter woesei DSM 14684.";
RL   Submitted (JAN-2010) 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}.
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DR   EMBL; CP001854; ADB53480.1; -; Genomic_DNA.
DR   RefSeq; WP_012936531.1; NC_013739.1.
DR   AlphaFoldDB; D3FD88; -.
DR   STRING; 469383.Cwoe_5071; -.
DR   KEGG; cwo:Cwoe_5071; -.
DR   eggNOG; COG0022; Bacteria.
DR   HOGENOM; CLU_012907_1_0_11; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000008229; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000008229}.
FT   DOMAIN          4..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   325 AA;  34441 MW;  1512F2E5A8EF6DE7 CRC64;
     MSQVTYKEAI RRAQEDALAE NDRVVLLGED IAAAGGAFKV TDRLFERFGP ERVLDTPISE
     QAIVGAAIGA ALKGRRPVAE LMFADFAAVC FDQIANQLAK YRYMTGGQVT LPVTLRLSNG
     AGGGFASQHS QTVENWFLNC PGLKVVVPGS PADAYGLFMA AVRDEDPVLF FEHKGMYNVK
     GELGPAGEAI EIGRAGVIRS GTSATVVATQ LMRQRAERVA EELAAEGIEL ELIDPRTVLP
     LDLDTIGASV DKTGRLVVVQ ESPLGGSWGA TVVAGVVAER FESLDAAPVL VSGPDTPVPY
     AGPLEDAWLP SERHIAGEIR SLLGA
//
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