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Database: UniProt
Entry: A0A429X9X9_9BACI
LinkDB: A0A429X9X9_9BACI
Original site: A0A429X9X9_9BACI 
ID   A0A429X9X9_9BACI        Unreviewed;       359 AA.
AC   A0A429X9X9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
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:RST59923.1};
GN   ORFNames=D5F11_009415 {ECO:0000313|EMBL:RST59923.1};
OS   Siminovitchia terrae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Siminovitchia.
OX   NCBI_TaxID=1914933 {ECO:0000313|EMBL:RST59923.1, ECO:0000313|Proteomes:UP000287296};
RN   [1] {ECO:0000313|EMBL:RST59923.1, ECO:0000313|Proteomes:UP000287296}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29736 {ECO:0000313|EMBL:RST59923.1,
RC   ECO:0000313|Proteomes:UP000287296};
RA   Sun L., Chen Z.;
RL   Submitted (DEC-2018) 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}.
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:RST59923.1}.
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DR   EMBL; QYTW02000007; RST59923.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A429X9X9; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000287296; Unassembled WGS sequence.
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:RST59923.1};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU366007}.
FT   DOMAIN          42..331
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   359 AA;  40541 MW;  C571DB5ED4D47B21 CRC64;
     MNNLLHEINE FETFQLLNEN GEVVHNDLLP ELSDKELQLL MERMIYTRTI DQRCISLSRQ
     GRLGFYAPVA GQEASMIGTQ FVLEKEDWIL PGYRDLPQML FQGVPLSQLF QWSRGHHKGG
     RMPEGVNVTP PQIIIGAQIV QAAGVGLGLK KRGKKNVAIT YTGDGGSSQG DFYEGINFAG
     VFNAQTIFVV QNNQFAISTP FEKQTAAKSI AHKSVAAGIK GVRVDGMDIL ATYVVTKEAR
     ERAINSNGPT LIETVTYRYG PHSTSGDDPT LYRNEQLEKE WAQKDPITRF RLFLEKQDLW
     TEEQEFQIIE QAKKDVKNAI KQAESESKTK VSNLIENMYE ELPFNLREQL NQVKEKENG
//
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