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Database: UniProt
Entry: V6Q7A5_9ENTE
LinkDB: V6Q7A5_9ENTE
Original site: V6Q7A5_9ENTE 
ID   V6Q7A5_9ENTE            Unreviewed;       325 AA.
AC   V6Q7A5;
DT   19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT   19-FEB-2014, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=T233_00279 {ECO:0000313|EMBL:EST90535.1};
OS   Vagococcus lutrae LBD1.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX   NCBI_TaxID=1408226 {ECO:0000313|EMBL:EST90535.1, ECO:0000313|Proteomes:UP000018126};
RN   [1] {ECO:0000313|EMBL:EST90535.1, ECO:0000313|Proteomes:UP000018126}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LBD1 {ECO:0000313|EMBL:EST90535.1,
RC   ECO:0000313|Proteomes:UP000018126};
RX   PubMed=24371201;
RA   Lebreton F., Valentino M.D., Duncan L.B., Zeng Q., Manson McGuire A.,
RA   Earl A.M., Gilmore M.S.;
RT   "High-Quality Draft Genome Sequence of Vagococcus lutrae Strain LBD1,
RT   Isolated from the Largemouth Bass Micropterus salmoides.";
RL   Genome Announc. 1:e01087-13(2013).
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EST90535.1}.
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DR   EMBL; AYSH01000004; EST90535.1; -; Genomic_DNA.
DR   RefSeq; WP_023605636.1; NZ_AYSH01000004.1.
DR   AlphaFoldDB; V6Q7A5; -.
DR   STRING; 1408226.T233_00279; -.
DR   PATRIC; fig|1408226.3.peg.280; -.
DR   eggNOG; COG0022; Bacteria.
DR   Proteomes; UP000018126; Unassembled WGS sequence.
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   Pyruvate {ECO:0000313|EMBL:EST90535.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018126}.
FT   DOMAIN          4..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   325 AA;  35600 MW;  2EADD068AD51AB41 CRC64;
     MAQKTMIQAI TDALDLELGK DENVLIFGED VGNNGGVFRA TEGLQEKHGK ERVFDTPLAE
     SGIGGLAFGL ALEGFRPVPE IQFFGFVFEV FDEIVGQMAR TRYRMGGTRN LPITIRAPFG
     GGVHTPEMHA DNLEGLIAQS PGIRVVIPSN PYDAKGLLIS AIRDNDPVVF LEHMKLYRSF
     REEVPEGEYT VPLDKAAITR EGSDITVITY GAMVREAIKV ADKLEKENIS VEIVDLRTVA
     PLDVETIIDS VEKTGRVVVV QEAQKQAGVG AQVASEISER AILSLEAPIG RVSAPDTVYP
     FGQAENSWLP NANDIEEKVR EIYEF
//
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