ID B3IWS8_9BACI Unreviewed; 360 AA.
AC B3IWS8;
DT 02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 02-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 32.
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 ECO:0000313|EMBL:BAG50248.1};
OS Amphibacillus xylanus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Amphibacillus.
OX NCBI_TaxID=1449 {ECO:0000313|EMBL:BAG50248.1};
RN [1] {ECO:0000313|EMBL:BAG50248.1}
RP NUCLEOTIDE SEQUENCE.
RA Arai T., Asano M., Takeda N., Tanaka R., Sato T., Sato J., Nakagawa J.,
RA Kawasaki S., Niimura Y.;
RT "Amphibacillus xylanus.";
RL Submitted (JAN-2008) 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, 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; AB374358; BAG50248.1; -; Genomic_DNA.
DR AlphaFoldDB; B3IWS8; -.
DR OMA; HGIVGGQ; -.
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 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:BAG50248.1};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU366007}.
FT DOMAIN 43..332
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 360 AA; 40446 MW; EE3F5ED3CB8A4D13 CRC64;
MKRINDAIEE QFQTFQILDE DGKVVNEEAM PELSDDELKE LMTRMVYTRI LDQRSIALNR
QGRLGFYAPT AGQEASQLGT QFALEKDDFI LPGYRDVPQL IWHGLPLYKA FLFSRGHYVG
NQMPEGVNAF SPQIIIGAQY VQAAGVALGM KKRNKNAVAI TYTGDGGTSQ GDFYEGINFA
GAYKAPAIFV VQNNRFAIST PVEKQTAAKT LAQKAVAAGI EGIQVDGMDV LAVYAATKEA
RERAVRGEGP TLIETLTYRY GPHTMAGDDP TRYRTKDLDS EWEKKDPLVR FRKFLEAKGL
WSEEEENKVI EQAKEDVKAA IKEADNVPKQ KVTDLISNMY EELPFNLKEQ YEEYKAKESK
//
