ID   A0A139D958_9FIRM        Unreviewed;       324 AA.
AC   A0A139D958;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   ORFNames=AWL62_622 {ECO:0000313|EMBL:KXS49881.1};
OS   Halanaerobium sp. T82-1.
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halanaerobiaceae;
OC   Halanaerobium.
OX   NCBI_TaxID=1794808 {ECO:0000313|EMBL:KXS49881.1, ECO:0000313|Proteomes:UP000070487};
RN   [1] {ECO:0000313|EMBL:KXS49881.1, ECO:0000313|Proteomes:UP000070487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=T82-1 {ECO:0000313|EMBL:KXS49881.1};
RA   Wolfe R., Daly R., Wrighton K.;
RT   "Halanaerobium-1 T82 Annotated.";
RL   Submitted (JAN-2016) 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   -!- 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:KXS49881.1}.
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DR   EMBL; LSBN01000017; KXS49881.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A139D958; -.
DR   PATRIC; fig|1794808.3.peg.252; -.
DR   Proteomes; UP000070487; 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:KXS49881.1}.
FT   DOMAIN          4..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   324 AA;  34976 MW;  C4960F038936AA38 CRC64;
     MKKLSYAEAL RLAMEEEMNR DSSVFVMGED VGVFGGCFGV TGDLVEKFGE DRVRDTPITE
     TAIVGSAVGA AMTGSRPVAE IMFAGFLGVA MDEIFNQAAK MCYMTGGQAH VPMVLRIPDG
     AGIGAAAQHS ERTEAWVTHV PGLKVVYPSN PADAKGLLKA AIRDEDPVMF FEHKILYNHV
     GDVPEEDDYI VPLGKGEIKR EGSDVTIVAT GIEVSHALEA AEQLAEEGID VEVIDPRTLV
     PLDIDMIMKS VEKTGKLLIA SEETKRGSFA SEIAAEVAEE GLFYLEQPIK RVCAPDAPVP
     FSSVLEQAYL PNPKKIADAV REMF
//