ID A0A0S6VSL5_9BACT Unreviewed; 327 AA.
AC A0A0S6VSL5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=U14_01689 {ECO:0000313|EMBL:GAK50458.1};
OS Candidatus Moduliflexus flocculans.
OC Bacteria; Candidatus Moduliflexota; Candidatus Moduliflexia;
OC Candidatus Moduliflexales; Candidatus Moduliflexaceae.
OX NCBI_TaxID=1499966 {ECO:0000313|EMBL:GAK50458.1};
RN [1] {ECO:0000313|EMBL:GAK50458.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Sekiguchi Y., Ohashi A., Parks D.H., Yamauchi T., Tyson G.W.,
RA Hugenholtz P.;
RT "First genomic representation of candidate bacterial phylum KSB3 points to
RT enhanced environmental sensing as a trigger of wastewater bulking.";
RL PeerJ 3:e740-e740(2015).
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}.
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DR EMBL; DF820456; GAK50458.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S6VSL5; -.
DR STRING; 1499966.U14_01689; -.
DR HOGENOM; CLU_012907_1_0_0; -.
DR Proteomes; UP000030700; 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 Reference proteome {ECO:0000313|Proteomes:UP000030700}.
FT DOMAIN 4..180
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 327 AA; 36052 MW; 2FA7EAA127953BA5 CRC64;
MRTMMYSDAL REAMREEMRK DARVILIGED VGQGYAGAFG VSKGLFEEFG AKQILDTPIC
ESTIIGCALG AAMVGMKPIA EIMFEDFIAM GFDQIVNQAA KLKFMSGEQY HANLVIRTPG
GSGGGTGPHH SQCWEALFMH IPGLIIAMPS NAYDAKGLLK TAINTSEPVI FFEHKRLYKT
KGEVPEEEYT VPFGKGRIAR EGKDLTVIAI SYMVNVAEEA AEELKKQHQF ELEIIDPRTI
VPLDLALIGE SIKKTNKAVV IEEGVLRGGV GSEIAAQIHE HFFDELDFPV TRIASRNLPI
PMTPLMEKSV IPTKERIIQD IRTLVGL
//