ID L9WDG6_9EURY Unreviewed; 337 AA.
AC L9WDG6;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=C495_04497 {ECO:0000313|EMBL:ELY47489.1};
OS Natronorubrum sulfidifaciens JCM 14089.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natronorubrum.
OX NCBI_TaxID=1230460 {ECO:0000313|EMBL:ELY47489.1, ECO:0000313|Proteomes:UP000011661};
RN [1] {ECO:0000313|EMBL:ELY47489.1, ECO:0000313|Proteomes:UP000011661}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 14089 {ECO:0000313|EMBL:ELY47489.1,
RC ECO:0000313|Proteomes:UP000011661};
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:ELY47489.1}.
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DR EMBL; AOHX01000026; ELY47489.1; -; Genomic_DNA.
DR RefSeq; WP_008160399.1; NZ_AOHX01000026.1.
DR AlphaFoldDB; L9WDG6; -.
DR STRING; 1230460.C495_04497; -.
DR PATRIC; fig|1230460.4.peg.904; -.
DR eggNOG; arCOG01052; Archaea.
DR OrthoDB; 6779at2157; -.
DR Proteomes; UP000011661; 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 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:UP000011661}.
FT DOMAIN 9..184
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 337 AA; 36662 MW; 1DBCA4073848B654 CRC64;
MSDDEGRQAT MSTAMVEAIA TEMRDNDEVF YMGEDVADYG GIFDSTDGLL EEFGHDRIMD
VPISETAYIG AAVGAAQAGM RPIAELMFVD FFGVCMDQLY NQMAKNTYMS GANVNVPMVL
TTAVGGTYSD AAQHSQTLYG TFAHLPGMKV VVPSTAYDAK GLMHNAIRDD DPVVYMFHKR
LMGIGWMPAP DGPKTAVPEE PYTIPFGQAD IKREGADVTV VTLGLHVHRA LEAAAKLADD
GIDVEVIDLR TLVPLDEATI LESVQKTGRL VVVDEDYRSF GLTGEVISRV VEAEPDALEA
VERLAIPDVP LPYARPLENR VIPDSDDIED AIRKTQP
//
