ID   A0A292Z0T1_9PSEU        Unreviewed;       326 AA.
AC   A0A292Z0T1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   ORFNames=TOK_4099 {ECO:0000313|EMBL:GAY09746.1};
OS   Pseudonocardia sp. N23.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Pseudonocardia.
OX   NCBI_TaxID=1987376 {ECO:0000313|EMBL:GAY09746.1, ECO:0000313|Proteomes:UP000222857};
RN   [1] {ECO:0000313|EMBL:GAY09746.1, ECO:0000313|Proteomes:UP000222857}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N23 {ECO:0000313|EMBL:GAY09746.1,
RC   ECO:0000313|Proteomes:UP000222857};
RA   Yamamoto N., Saito Y., Inoue D., Sei K., Ike M.;
RT   "Characterization of newly isolated Pseudonocardia sp. N23 with high 1,4-
RT   dioxane-degrading ability.";
RL   Submitted (AUG-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   -!- 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:GAY09746.1}.
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DR   EMBL; BEGX01000052; GAY09746.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A292Z0T1; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000222857; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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   Oxidoreductase {ECO:0000313|EMBL:GAY09746.1}.
FT   DOMAIN          4..177
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   326 AA;  34358 MW;  70E5BF2D2C3F961D CRC64;
     MARTRLITAV NEALVAEMER DPTLIVFGED VELAIMGDTR GLVERFGRDR IRNSPICEQT
     LTGMAVGLAS AGFRVVLHLM FNNFIYTGMD AIGNQMAKLR LMTGGQMELP ITVIAGYGGG
     NGNAAQHSDT AYPALMNLGG IQVAVPTSSA DAKGLFTTAV RGRTPTFFLE PAGRGGDMGE
     VPDGEHLVPF GKANVLRTGT DVTLVAIGTM VRPTLTAATA LAGEGVSAEV IDPRTLVPFD
     EDTVLASVAR TGRLVVVDEA RDRCSAASQI AAVVADRGFA TLRAPVRRVT VPDVALPYAR
     NAEAVLIPGP ERIAAAVRSV MERQLA
//