ID F8GT33_CUPNN Unreviewed; 361 AA.
AC F8GT33;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=bkdA1 {ECO:0000313|EMBL:AEI81160.1};
GN Synonyms=pdhA {ECO:0000256|RuleBase:RU366007};
GN OrderedLocusNames=CNE_2c22110 {ECO:0000313|EMBL:AEI81160.1};
OS Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453
OS / N-1) (Ralstonia eutropha).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1042878 {ECO:0000313|EMBL:AEI81160.1, ECO:0000313|Proteomes:UP000006798};
RN [1] {ECO:0000313|EMBL:AEI81160.1, ECO:0000313|Proteomes:UP000006798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1
RC {ECO:0000313|Proteomes:UP000006798};
RX PubMed=21742890; DOI=10.1128/JB.05660-11;
RA Poehlein A., Kusian B., Friedrich B., Daniel R., Bowien B.;
RT "Complete genome sequence of the type strain Cupriavidus necator N-1.";
RL J. Bacteriol. 193:5017-5017(2011).
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}.
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DR EMBL; CP002878; AEI81160.1; -; Genomic_DNA.
DR RefSeq; WP_013953834.1; NC_015723.1.
DR AlphaFoldDB; F8GT33; -.
DR KEGG; cnc:CNE_2c22110; -.
DR HOGENOM; CLU_029393_1_0_4; -.
DR Proteomes; UP000006798; Chromosome 2.
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}; Pyruvate {ECO:0000256|RuleBase:RU366007};
KW Thiamine pyrophosphate {ECO:0000256|RuleBase:RU366007}.
FT DOMAIN 43..328
FT /note="Dehydrogenase E1 component"
FT /evidence="ECO:0000259|Pfam:PF00676"
SQ SEQUENCE 361 AA; 38485 MW; 46B81DEC767732C6 CRC64;
MSTVASFEIG YTRYLAPPGD TSSPTSPPPP LASNPDALLP LYQAMVLTRQ FDLKAIALQR
TGKIGTFASA LGQEAIGVGV AFAMRPEDVL VPSYRDHAAQ FVRGVTMTES LLYWGGDERG
SGFAAAPHDF ANCVPIGTQV CHAAGAAYAF QLRGEPRVAV CLLGDGGTSK GDFYEGMNMA
GAWHAPLVIV INNNQWAISM PRSGQTAAQT LAQKAIAAGI PGEQVDGNDV VAVRHRVGEA
IARARDGGGP ALIEAITYRL GDHTTADDAS RYRDEASVKA HWQEEPLLRL RTHLLALHAW
DAAREEALVK ACSQQVAQAV ETYLAMPPPD PAAMFDCLYA AMPAELQAQL EIARRFPAPH
G
//
