ID A0A166TF29_9EURY Unreviewed; 339 AA.
AC A0A166TF29;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN ORFNames=A4G99_03505 {ECO:0000313|EMBL:KZN25549.1};
OS Haladaptatus sp. R4.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haladaptataceae; Haladaptatus.
OX NCBI_TaxID=1679489 {ECO:0000313|EMBL:KZN25549.1, ECO:0000313|Proteomes:UP000076599};
RN [1] {ECO:0000313|EMBL:KZN25549.1, ECO:0000313|Proteomes:UP000076599}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R4 {ECO:0000313|EMBL:KZN25549.1,
RC ECO:0000313|Proteomes:UP000076599};
RA Mukhopadhyay S.K.;
RT "Genome sequence of halophilic archaea.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:KZN25549.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LWHG01000011; KZN25549.1; -; Genomic_DNA.
DR RefSeq; WP_066141263.1; NZ_LWHG01000011.1.
DR AlphaFoldDB; A0A166TF29; -.
DR STRING; 1679489.A4G99_03505; -.
DR OrthoDB; 6779at2157; -.
DR Proteomes; UP000076599; 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 Pyruvate {ECO:0000313|EMBL:KZN25549.1}.
FT DOMAIN 9..184
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 339 AA; 36794 MW; C3D8098F0C546387 CRC64;
MAESDGKELT MSRAMVDAIA HEMRESDDVF VMGEDIADYG GIFDSTQGLL DEFDHDRIMD
VPISETAFIG AAVGAAQQGM RPIAELMFVD FFGVAMDQIY NQMAKNTYMS GGSVTVPMVL
MTAVGGTYND AAQHSQTLYG TFAHLPGMKV VVPSTAYDAK GLMHAAIRDD DPVVFMFHKR
LMGIGWMPAP EGPKTPVPDE DYTIEFGEAD VKREGDDVTV VTLGLHVHRA MEAAKELADE
GEVDAEVIDL RTLVPLDTET IVESVAKTGR LVVVDEDYHS FGVSGEIIAR AAENGLSDLD
AVERVTMPDV PIPYARPLEQ EVNPGTEDIA DAIRSVNDE
//
