ID A0A1F6EWE7_9BACT Unreviewed; 343 AA.
AC A0A1F6EWE7;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=A3B35_02195 {ECO:0000313|EMBL:OGG77947.1};
OS Candidatus Kaiserbacteria bacterium RIFCSPLOWO2_01_FULL_54_24.
OC Bacteria; Candidatus Kaiserbacteria.
OX NCBI_TaxID=1798515 {ECO:0000313|EMBL:OGG77947.1, ECO:0000313|Proteomes:UP000177215};
RN [1] {ECO:0000313|EMBL:OGG77947.1, ECO:0000313|Proteomes:UP000177215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGG77947.1}.
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DR EMBL; MFMC01000002; OGG77947.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6EWE7; -.
DR STRING; 1798515.A3B35_02195; -.
DR Proteomes; UP000177215; 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;
FT DOMAIN 6..178
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 343 AA; 36799 MW; 3CB2F2D91ACC7556 CRC64;
MDDRILKTAD AIREATDQVM AVDPSVYVIG LGVPQGAGGT TNGLKQKYPE RIFDTPTSEA
ALTGMAVGSA IAGLHPIVHH DRVEFSLLAA DQIFTQAAKW NYMFGGGGPV PIIFRVVIGR
QWGNGPQHSQ ALYSLFGSVP GLKVVVPSSP TMAKGLLISA ARDKNPVVMM ESRWLYGIKE
EVPAEMYEVP LDKAHIVQKG TDITVVGYGD ALYTARQALT LLGEDAKHVE LIDLVSINPI
DHSTIHASIK KTGRLLTVDT TNGAFSVGSE IIAKAAQNRV GFIDAPRGLA APDVPCPTPP
SLSEFWYPTK VTIANAILEM LGKPPIDMQL SFEELHLPPT STL
//
