ID G9QMB2_9BACI Unreviewed; 325 AA.
AC G9QMB2;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 39.
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=HMPREF1015_00679 {ECO:0000313|EMBL:EHL77157.1};
OS Bacillus smithii 7_3_47FAA.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=665952 {ECO:0000313|EMBL:EHL77157.1, ECO:0000313|Proteomes:UP000011747};
RN [1] {ECO:0000313|EMBL:EHL77157.1, ECO:0000313|Proteomes:UP000011747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7_3_47FAA {ECO:0000313|EMBL:EHL77157.1,
RC ECO:0000313|Proteomes:UP000011747};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Goldberg J.,
RA Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Montmayeur A., Murphy C., Neiman D., Pearson M.,
RA Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Bacillus smithii 7_3_47FAA.";
RL Submitted (SEP-2011) 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:EHL77157.1}.
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DR EMBL; ACWF01000118; EHL77157.1; -; Genomic_DNA.
DR RefSeq; WP_003354409.1; NZ_JH414757.1.
DR AlphaFoldDB; G9QMB2; -.
DR PATRIC; fig|665952.3.peg.2225; -.
DR HOGENOM; CLU_012907_1_0_9; -.
DR Proteomes; UP000011747; 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 Pyruvate {ECO:0000313|EMBL:EHL77157.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000011747}.
FT DOMAIN 4..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 325 AA; 35599 MW; 8AA858B95394CB87 CRC64;
MPQMTMIQAI NDALRTELKN DENVLVFGED VGVNGGVFRA TEGLQKEFGE ERVFDTPLAE
SGIGGLSIGL ALQGFRPVPE IQFFGFVYEV MDSLSGQMAR YRYRSGGKFS MPITVRAPFG
GGVHTPELHA DSLEGLVAQQ PGLKVVIPST PYEAKGLLIS AIRDNDPVIF LEHMKLYRSF
RQEVPEGEYT IPLGKADVKR EGKDISIIAY GAMVHEALKA AEELEKEGYS AEVVDLRTVS
PLDVETIVAS VEKTNRAIVV QEAQKQAGIA ANVVAEINER AILSLEAPVL RVTAPDTVYP
FSQAESVWLP NFKDIVETAK KVLEF
//
