ID   A0A259F5S6_9PROT        Unreviewed;       327 AA.
AC   A0A259F5S6;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   ORFNames=B7X82_07665 {ECO:0000313|EMBL:OZA33790.1};
OS   Hydrogenophilales bacterium 17-64-65.
OC   Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales.
OX   NCBI_TaxID=1970528 {ECO:0000313|EMBL:OZA33790.1, ECO:0000313|Proteomes:UP000216509};
RN   [1] {ECO:0000313|EMBL:OZA33790.1, ECO:0000313|Proteomes:UP000216509}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=17-64-65 {ECO:0000313|EMBL:OZA33790.1};
RA   Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA   Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT   "Lifting the veil on microbial sulfur biogeochemistry in mining
RT   wastewaters.";
RL   Submitted (MAR-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:OZA33790.1}.
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DR   EMBL; NCIQ01000009; OZA33790.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A259F5S6; -.
DR   Proteomes; UP000216509; Unassembled WGS sequence.
DR   GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-UniRule.
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;
FT   DOMAIN          4..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   327 AA;  35501 MW;  D70EB12DF1E80432 CRC64;
     MAQIMLWEAI QRAHDEEMSR DPLVICMGED IGVAGGTYKA TKGLYEKYGP LRVMDTPISE
     GGFTGLAIGA SFLGVRPIVE IMSVNFAWLA MDQMFNSAAK IRYMSGGQLA APCVFRSAGG
     AAHQLGAQHS ARMEKVFMGI AGLRVVTPSN PKQAYGLLKS AIRCDDPVFI NEHELMYNMK
     GEVPDGEYFH PLEGSEVARA GTDVTLFGYN ISVHWCLKAA EILDKQYGIS AEVVDLYSLS
     PLDRAGIKAS VSKTHRVVIA EEDEAPVGVG SEVIAIINEE CFFELDAAPV RVHSALVPQP
     YNHTLEKAAI PDHEDVVKAV LKLFGKA
//