ID M0NCS6_9EURY Unreviewed; 333 AA.
AC M0NCS6;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=C451_04863 {ECO:0000313|EMBL:EMA55782.1};
OS Halococcus thailandensis JCM 13552.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halococcaceae; Halococcus.
OX NCBI_TaxID=1227457 {ECO:0000313|EMBL:EMA55782.1, ECO:0000313|Proteomes:UP000011680};
RN [1] {ECO:0000313|EMBL:EMA55782.1, ECO:0000313|Proteomes:UP000011680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 13552 {ECO:0000313|EMBL:EMA55782.1,
RC ECO:0000313|Proteomes:UP000011680};
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
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:EMA55782.1}.
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DR EMBL; AOMF01000103; EMA55782.1; -; Genomic_DNA.
DR AlphaFoldDB; M0NCS6; -.
DR STRING; 1227457.C451_04863; -.
DR PATRIC; fig|1227457.3.peg.876; -.
DR eggNOG; arCOG01052; Archaea.
DR OrthoDB; 6779at2157; -.
DR Proteomes; UP000011680; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0006082; P:organic acid metabolic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
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 14..189
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 333 AA; 35877 MW; 9737410B228B97C4 CRC64;
MASAELESQE TETMTIREAI RETMREELNR DDDVFLIGED IGVMEGVLDV TGDLYHDFGP
ERVRDTPISE AGIIGAATGA AATGSRPVAE LMFSDFIGVA MEQTMNQMAK MRYMFGGKIE
MPVTVRATEG GGMGAASQHS GTVHTMIAHF PGLMAVAPGT PEAAKGLLRS AIRSDDPVFF
FENKMIYEQS GEVPVDEDFT IPLGEANVER EGDDVTVVAT QRLVGESLTV ADELDGDIDV
EVIDLRSLYP LDTDTIVESL DKTGRMVVAG ESPLSYGAQA EVVSRAVENA FYSLDAPIQR
VGVPDTHIPF GPSLESEVLP DADDVRNAIE RIA
//
