ID A0A1F2RJU5_9BACT Unreviewed; 335 AA.
AC A0A1F2RJU5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=A3H95_07785 {ECO:0000313|EMBL:OFV93962.1};
OS Acidobacteria bacterium RIFCSPLOWO2_02_FULL_64_15.
OC Bacteria; Acidobacteriota.
OX NCBI_TaxID=1797181 {ECO:0000313|EMBL:OFV93962.1, ECO:0000313|Proteomes:UP000179236};
RN [1] {ECO:0000313|EMBL:OFV93962.1, ECO:0000313|Proteomes:UP000179236}
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:OFV93962.1}.
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DR EMBL; MEKS01000007; OFV93962.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F2RJU5; -.
DR STRING; 1797181.A3H95_07785; -.
DR Proteomes; UP000179236; 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:OFV93962.1}.
FT DOMAIN 13..188
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 335 AA; 36085 MW; 42DF158786FFF0BE CRC64;
MLDTVTTTAV RELTFGEAIR EALAEELRRD PRVCLLGEDV AEAGTAFKVL KGLVDEFGKN
RIIDTPISEA GFTGLGVGAA MTGLRPVVDI MFGDFLTLIM DQLVNQAAKI HYMSGGAWKV
PLVLRTTMGA TRRSGAQHSQ SLHAWPAHIP GLKVVVPSTP ADAKGLLKSA IRDDNPVVFF
EDKISYAKVK GPVPSHDYTI PLGVADVKRE GTDITLVGTS SMVQVALGAA TMLEQVGISA
EVVDPRTLWP LDEKTLVESV KKTSRCIVID EGYARYGVTG ELASVIAEGA FYDLDGPVRR
MGARHVPIPF APPLEDATVP TEQQVVELAR QMCHK
//
