ID A0A1F8R7B4_9CHLR Unreviewed; 336 AA.
AC A0A1F8R7B4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 11.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
DE Flags: Fragment;
GN ORFNames=A2137_03105 {ECO:0000313|EMBL:OGO43580.1};
OS Chloroflexi bacterium RBG_16_58_8.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797655 {ECO:0000313|EMBL:OGO43580.1, ECO:0000313|Proteomes:UP000180317};
RN [1] {ECO:0000313|EMBL:OGO43580.1, ECO:0000313|Proteomes:UP000180317}
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:OGO43580.1}.
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DR EMBL; MGNW01000056; OGO43580.1; -; Genomic_DNA.
DR Proteomes; UP000180317; 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 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT NON_TER 336
FT /evidence="ECO:0000313|EMBL:OGO43580.1"
SQ SEQUENCE 336 AA; 36225 MW; 6C9EFD646E5A8846 CRC64;
MRSITYRQAI NEALAQEMAR DASVFVYGIG VPDHKGIFGS TSGLAERFGP ERCFDTPLAE
DSLTGFGLGA AINGLRPVHV HMRADFLLLA MNQLANMVSS YTYGSGGKLS VPLVIRAVIG
RGWGQGFQHS KSIYSVYAHI PGLKVVLPAT PRDAKGLLIS AIRDDNPVIC LEHRLLYDVS
GEVPEEPYTI PIGQAHTLGE GRDVTVVAVS WMAVEAVKAA EIMQKRGVSV EVIDPRTITP
LDADTIVKSV KKTGRCIVAD NDWVQCGFSA EVAAVIGAXX LRELKSPVAR LGFSPTPCPC
TRPLETCFYP NAVDIIRTIE EMLGLAAADL SGEDFY
//
