ID Q5L137_GEOKA Unreviewed; 369 AA.
AC Q5L137;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 27-MAR-2024, entry version 104.
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=GK1058 {ECO:0000313|EMBL:BAD75343.1};
OS Geobacillus kaustophilus (strain HTA426).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC Geobacillus thermoleovorans group.
OX NCBI_TaxID=235909 {ECO:0000313|EMBL:BAD75343.1, ECO:0000313|Proteomes:UP000001172};
RN [1] {ECO:0000313|EMBL:BAD75343.1, ECO:0000313|Proteomes:UP000001172}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTA426 {ECO:0000313|EMBL:BAD75343.1,
RC ECO:0000313|Proteomes:UP000001172};
RX PubMed=15576355; DOI=10.1093/nar/gkh970;
RA Takami H., Takaki Y., Chee G.J., Nishi S., Shimamura S., Suzuki H.,
RA Matsui S., Uchiyama I.;
RT "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT Geobacillus kaustophilus.";
RL Nucleic Acids Res. 32:6292-6303(2004).
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; BA000043; BAD75343.1; -; Genomic_DNA.
DR RefSeq; WP_011230558.1; NC_006510.1.
DR AlphaFoldDB; Q5L137; -.
DR STRING; 235909.GK1058; -.
DR KEGG; gka:GK1058; -.
DR PATRIC; fig|235909.7.peg.1154; -.
DR eggNOG; COG1071; Bacteria.
DR HOGENOM; CLU_029393_1_0_9; -.
DR Proteomes; UP000001172; 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}; Pyruvate {ECO:0000256|RuleBase:RU366007};
KW Reference proteome {ECO:0000313|Proteomes:UP000001172};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU366007}.
FT DOMAIN 51..341
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
FT COILED 312..339
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 369 AA; 41418 MW; 9166078E5E080499 CRC64;
MGVKTSQFRF AEQLEKVAEQ FPTFQILNEE GEIVNEEAMP ELSDEQLKEL MRRMVYTRIL
DQRSISLNRQ GRLGFYAPTA GQEASQIASH FALEKEDFIL PGYRDVPQII WHGLPLYQAF
LFSRGHFHGN QIPEGVNVLP PQIIIGAQYI QAAGVALGLK MRGKKAVAIT YTGDGGTSQG
DFYEGINFAG AFKAPAIFVV QNNRFAISTP VEKQTIAKTL AQKAVAAGIP GIQVDGMDPL
AVYAAVKAAR ERAINGEGPA LIETLCFRYG PHTMSGDDPT RYRSKELENE WAKKDPLVRF
RKFLEAKGLW SEEEENRVIE QAKEDIKEAI KKADETPKQK VTDLISIMFE ELPANLKEQY
EIYKEKESK
//
