ID A0A135L3D7_9BACI Unreviewed; 326 AA.
AC A0A135L3D7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
DE EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281};
GN ORFNames=U473_05580 {ECO:0000313|EMBL:KXG43544.1};
OS Tepidibacillus decaturensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Tepidibacillus.
OX NCBI_TaxID=1413211 {ECO:0000313|EMBL:KXG43544.1, ECO:0000313|Proteomes:UP000070352};
RN [1] {ECO:0000313|EMBL:KXG43544.1, ECO:0000313|Proteomes:UP000070352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Z9 {ECO:0000313|EMBL:KXG43544.1,
RC ECO:0000313|Proteomes:UP000070352};
RA Dong Y., Chang J.Y., Sanford R., Fouke B.W.;
RT "Draft Genome for Tepidibacillus decaturensis nov. sp. Strain Z9, an
RT Anaerobic, Moderately Thermophilic and Heterotrophic Bacterium from Deep
RT Subsurface of the Illinois Basin, USA.";
RL Submitted (FEB-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 -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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:KXG43544.1}.
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DR EMBL; LSKU01000001; KXG43544.1; -; Genomic_DNA.
DR RefSeq; WP_068724175.1; NZ_LSKU01000001.1.
DR AlphaFoldDB; A0A135L3D7; -.
DR STRING; 1413211.U473_05580; -.
DR OrthoDB; 9771835at2; -.
DR Proteomes; UP000070352; 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:UP000070352}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 326 AA; 36073 MW; 3115C3ED0E9E107B CRC64;
MPQMTMIQAI TDAMRVELAR DTNVLLFGED VGKYGGVFRA TAGLQDEFGE DRVFDTPLSE
SGIAGLAIGL GLMGYRPIAE IQFIGFIFEA MDSICAQAPR IRYRTNGRFH SPITFRAPFG
GGVKTPELHA DSLEGYLMQT PGLKVVIPSN PYDAKGLLIS AIRDNDPVFF MEHMKLYRSF
RQEVPEGEYT VPIGKANIVR EGTDITIITY GAMVHTSLKA AEEIEKKRGV KVEVIDLRTI
NPIDTETVLK SVEKTNRAIV VQEAQRTSGA AAEIIAQITE KGILYLEAPV LRVTSPDTVY
PFGMIEDEWL PDPTRVIEGI EQVLDF
//
