ID A0A2N7VX47_9BURK Unreviewed; 362 AA.
AC A0A2N7VX47;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 19.
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 ECO:0000313|EMBL:PMS21724.1};
GN ORFNames=C0Z18_07710 {ECO:0000313|EMBL:PMS21724.1};
OS Trinickia dabaoshanensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Trinickia.
OX NCBI_TaxID=564714 {ECO:0000313|EMBL:PMS21724.1, ECO:0000313|Proteomes:UP000235616};
RN [1] {ECO:0000313|EMBL:PMS21724.1, ECO:0000313|Proteomes:UP000235616}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GIMN1.004 {ECO:0000313|EMBL:PMS21724.1,
RC ECO:0000313|Proteomes:UP000235616};
RA Estrada-de los Santos P., Palmer M., Chavez-Ramirez B., Beukes C.,
RA Steenkamp E.T., Hirsch A.M., Manyaka P., Maluk M., Lafos M., Crook M.,
RA Gross E., Simon M.F., Bueno dos Reis Junior F., Poole P.S., Venter S.N.,
RA James E.K.;
RT "Whole genome analyses suggest that Burkholderia sensu lato contains two
RT further novel genera in the rhizoxinica-symbiotica group Mycetohabitans
RT gen. nov., and Trinickia gen. nov.: implications for the evolution of
RT diazotrophy and nodulation in the Burkholderiaceae.";
RL Submitted (JAN-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|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:PMS21724.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PNYA01000005; PMS21724.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2N7VX47; -.
DR OrthoDB; 9766715at2; -.
DR Proteomes; UP000235616; 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:PMS21724.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000235616};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU366007}.
FT DOMAIN 39..318
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 362 AA; 39151 MW; 0E9DC3E859ABA001 CRC64;
MTTVASFHIE YTRFLDADGV PAQPLPEFAR NPATLQTFYR AMVLTRAFDM KAVALQRTGK
LGTFASSVGQ EAIGVGLASA MRPEDALFPS YRDHAAQLLR GVTMTESLLY WGGDERGSAF
AAAPHDFPNC VPIATQVAHA AGAAYAFRLR QEPRVAVAIV GDGGTSKGDF YEAMNMAGVW
QAPLVIVIND NQWAISMPRA AQTATQTLAQ KAIAAGIEGR QVDGNDVIAV HDAACVALAK
ARRGEGPTLI EALSYRLGDH TTADDATRYR DPELVNQAWR AEPIARLRKY LVSLNVWDKA
REDELNRDCG QQVDAAVQAY LAVAPPGPAA MFEHLYASLP QALNDQLASA LQWASRTERD
HG
//
