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Database: UniProt
Entry: A0A1B9YQH6_9BRAD
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ID   A0A1B9YQH6_9BRAD        Unreviewed;       361 AA.
AC   A0A1B9YQH6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit alpha {ECO:0000256|RuleBase:RU366007};
DE            EC=1.2.4.1 {ECO:0000256|RuleBase:RU366007};
GN   Name=pdhA {ECO:0000256|RuleBase:RU366007};
GN   ORFNames=LMTR3_13145 {ECO:0000313|EMBL:OCK57006.1};
OS   Bradyrhizobium sp. LMTR 3.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=189873 {ECO:0000313|EMBL:OCK57006.1, ECO:0000313|Proteomes:UP000093220};
RN   [1] {ECO:0000313|EMBL:OCK57006.1, ECO:0000313|Proteomes:UP000093220}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMTR 3 {ECO:0000313|EMBL:OCK57006.1,
RC   ECO:0000313|Proteomes:UP000093220};
RA   Ormeno-Orrillo E., Duran D., Rey L., Ruiz Argueso T., Imperial J.,
RA   Martinez E.;
RL   Submitted (JUL-2016) 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|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|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:OCK57006.1}.
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DR   EMBL; MAXC01000033; OCK57006.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1B9YQH6; -.
DR   STRING; 189873.LMTR3_13145; -.
DR   OrthoDB; 9766715at2; -.
DR   Proteomes; UP000093220; 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:OCK57006.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000093220};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU366007}.
FT   DOMAIN          44..324
FT                   /note="Dehydrogenase E1 component"
FT                   /evidence="ECO:0000259|Pfam:PF00676"
SQ   SEQUENCE   361 AA;  39676 MW;  19FB3EC9B3B8B991 CRC64;
     MSDGGLPVIA RFEVRHRNYL APDGSINRPL PAFASDANLL TALYRAMLLL RNFDRKAVAL
     QRTGRLGTYA VSLGQEAVSV GIASAMRAED VLLPSYRDNG ALIWRGVKLE EILLFWGGDE
     RGNQFSGPVQ DFPFCVPVGS QAPHAAGVAY AFKLRKQPRV AVCMFGDGAT SKGDVYEAMN
     FAGVHKLPVV FVATNNQWAI SVPLRLQTGC ETLAQKAIAA GFIGEQVDGS DVVAMRAAAE
     DAIATAREGQ GPRFIEAVTY RLGDHTTSDD ALRYRSADEV QARWKEEPIT RLRSYLVGQK
     MWSKAQEEQL AAECHERVEA AVERYLATEP RRPEIMFDHL YAELPETYAA QRRQLAGDGD
     A
//
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