GenomeNet

Database: UniProt
Entry: A0A2D1SQ05_9BACL
LinkDB: A0A2D1SQ05_9BACL
Original site: A0A2D1SQ05_9BACL 
ID   A0A2D1SQ05_9BACL        Unreviewed;       325 AA.
AC   A0A2D1SQ05;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
DE            EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281};
GN   ORFNames=CSE16_03660 {ECO:0000313|EMBL:ATP39200.1};
OS   Solibacillus sp. R5-41.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Solibacillus.
OX   NCBI_TaxID=2048654 {ECO:0000313|EMBL:ATP39200.1, ECO:0000313|Proteomes:UP000222866};
RN   [1] {ECO:0000313|EMBL:ATP39200.1, ECO:0000313|Proteomes:UP000222866}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R5-41 {ECO:0000313|EMBL:ATP39200.1,
RC   ECO:0000313|Proteomes:UP000222866};
RA   Guo Y., Chen Z., Wang H.;
RT   "Complete genome sequence of Solibacillus sp. R5-41.";
RL   Submitted (OCT-2017) 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   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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; CP024123; ATP39200.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D1SQ05; -.
DR   KEGG; sob:CSE16_03660; -.
DR   OrthoDB; 9771835at2; -.
DR   Proteomes; UP000222866; 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;
KW   Reference proteome {ECO:0000313|Proteomes:UP000222866}.
FT   DOMAIN          4..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   325 AA;  35584 MW;  31126AA3C4FBDF9D CRC64;
     MAQMTMIQAI TDALRCEMKN DENVLVFGED VGVNGGVFRA TEGLQKEFGV ERVFDTPLAE
     SGIGGLAIGL ALTGYRPVPE IQFFGFVYEV MDSISGQLAR MRYRSGGTYN APVTIRSPFG
     GGVHTPEMHS DSLEGLMAQQ PGLKVVIPST PYDAKGLLIA SIRDNDPVIF LEHLKLYRSF
     REEVPEEAYT VEIGKADVKR EGKDLSIIAY GLMVHESLKA AEELEKEGYS VEVVDLRTIQ
     PLDIETIIAS VEKTGRAIVV QEAQKQAGIA ANVVSEITER AILSLEAPVL RVAAPDTIYP
     FPQAEGVWLP TYKDVMETAK KVLTF
//
DBGET integrated database retrieval system