ID B1HPR9_LYSSC Unreviewed; 371 AA.
AC B1HPR9;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha {ECO:0000256|ARBA:ARBA00014159, ECO:0000256|RuleBase:RU366007};
DE EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281, ECO:0000256|RuleBase:RU366007};
GN Name=pdhA {ECO:0000256|RuleBase:RU366007};
GN OrderedLocusNames=Bsph_1363 {ECO:0000313|EMBL:ACA38971.1};
OS Lysinibacillus sphaericus (strain C3-41).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=444177 {ECO:0000313|EMBL:ACA38971.1, ECO:0000313|Proteomes:UP000002164};
RN [1] {ECO:0000313|EMBL:ACA38971.1, ECO:0000313|Proteomes:UP000002164}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C3-41 {ECO:0000313|EMBL:ACA38971.1,
RC ECO:0000313|Proteomes:UP000002164};
RX PubMed=18296527; DOI=10.1128/JB.01652-07;
RA Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA Berry C., Yuan Z.;
RT "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT sphaericus C3-41 and comparison with those of closely related Bacillus
RT species.";
RL J. Bacteriol. 190:2892-2902(2008).
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, ECO:0000256|RuleBase:RU366007}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase] + pyruvate = CO2 + N(6)-[(R)-S(8)-
CC acetyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC acetyltransferase]; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480,
CC Rhea:RHEA-COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111; EC=1.2.4.1;
CC Evidence={ECO:0000256|RuleBase:RU366007};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|RuleBase:RU366007};
CC -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|ARBA:ARBA00011870, ECO:0000256|RuleBase:RU366007}.
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DR EMBL; CP000817; ACA38971.1; -; Genomic_DNA.
DR RefSeq; WP_012293093.1; NC_010382.1.
DR AlphaFoldDB; B1HPR9; -.
DR EnsemblBacteria; ACA38971; ACA38971; Bsph_1363.
DR KEGG; lsp:Bsph_1363; -.
DR HOGENOM; CLU_029393_1_0_9; -.
DR Proteomes; UP000002164; Chromosome.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR InterPro; IPR001017; DH_E1.
DR InterPro; IPR017596; PdhA/BkdA.
DR InterPro; IPR029061; THDP-binding.
DR NCBIfam; TIGR03181; PDH_E1_alph_x; 1.
DR PANTHER; PTHR43380; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43380:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT ALPHA, MITOCHONDRIAL; 1.
DR Pfam; PF00676; E1_dh; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Glycolysis {ECO:0000256|RuleBase:RU366007};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU366007};
KW Pyruvate {ECO:0000256|RuleBase:RU366007, ECO:0000313|EMBL:ACA38971.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU366007}.
FT DOMAIN 53..342
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT COILED 313..340
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 371 AA; 41603 MW; B4722AE6D3D69A66 CRC64;
MSKKNNNIFD AKQTLTEIED KFEMFQILNE EGEIINNEAD PKLSDEELVE LMTRMVYTRI
LDQRSISLNR QGRLGFYAPT AGQEASQLAS HFALEQEDWI LPGYRDVPQI VWHGLPLDKA
FLFSRGHFMG NQVPEGVNVL APQIIIGAQY IQAAGVALGI QKRGKKAVAV TYTGDGGSSQ
GDFYEGINFA GAFKSPAIFI VQNNQYAIST PRELQTAAKT IAQKGVAAGL PSILVDGMDA
LAVYVATRDA RERAINGEGP TLIETMCYRY GPHTMAGDDP TRYRTSDTDN EWAQKDPLVR
FRKYLEAKGL WDEKKEEAVI ERAKEEIKEA IKKADAAPKQ KVTELMENMY KGEMPSNLKE
QYEIYKEKES K
//
