ID A0A172TB30_9DEIO Unreviewed; 907 AA.
AC A0A172TB30;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00017172, ECO:0000256|PIRNR:PIRNR000156};
DE EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281, ECO:0000256|PIRNR:PIRNR000156};
GN ORFNames=SU48_10585 {ECO:0000313|EMBL:ANE44144.1};
OS Deinococcus puniceus.
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=1182568 {ECO:0000313|EMBL:ANE44144.1, ECO:0000313|Proteomes:UP000077363};
RN [1] {ECO:0000313|EMBL:ANE44144.1, ECO:0000313|Proteomes:UP000077363}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY1 {ECO:0000313|EMBL:ANE44144.1,
RC ECO:0000313|Proteomes:UP000077363};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Deinococcus puniceus/DY1/ whole genome sequencing.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex, that
CC catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
CC {ECO:0000256|PIRNR:PIRNR000156}.
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|ARBA:ARBA00043719,
CC ECO:0000256|PIRNR:PIRNR000156};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|PIRSR:PIRSR000156-1};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|PIRNR:PIRNR000156};
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DR EMBL; CP011387; ANE44144.1; -; Genomic_DNA.
DR RefSeq; WP_064015225.1; NZ_CP011387.1.
DR AlphaFoldDB; A0A172TB30; -.
DR STRING; 1182568.SU48_10585; -.
DR KEGG; dpu:SU48_10585; -.
DR PATRIC; fig|1182568.3.peg.2198; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000077363; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR CDD; cd02017; TPP_E1_EcPDC_like; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR035807; PDC_E1_N.
DR InterPro; IPR004660; PDH_E1.
DR InterPro; IPR041621; PDH_E1_M.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00759; aceE; 1.
DR PANTHER; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR PANTHER; PTHR43825:SF3; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR Pfam; PF17831; PDH_E1_M; 1.
DR Pfam; PF00456; Transketolase_N; 1.
DR PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 4: Predicted;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Magnesium {ECO:0000256|PIRSR:PIRSR000156-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR000156-1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR000156};
KW Pyruvate {ECO:0000256|PIRNR:PIRNR000156, ECO:0000313|EMBL:ANE44144.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000077363};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 93..309
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 496..709
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 274
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 276
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 907 AA; 100853 MW; 0C1EE516B6F32528 CRC64;
MTNVPPKGPP RAGLPPQERE QLNTVETQEW LDSLAYVLAD GGDDRAAQLL EDLDHYAYFH
GAPILFKQNT PYLNTIDVDK QPDYPGDIDM ERKIRNIIRW NAVAMVVKAN KKSDGIGGHL
STYASSAELL EVGFNHFFRG HGAGQDRDLV FFQGHASPGV YSRSFLEGRL DGGRLGRFRR
ELQAEPGLSS YPHPWLMPDY WEFPTVSMGL GPMQAIYQAR YIKYLENRGL KPAGDAKVWA
FLGDGEMDEP QSIGALRFAS YENLDNIVFV LNANLQRLDG PVRANSKVIQ EFEALFRGAG
WNVIKVVWDS KWDELLSKDY NGEIVKRFEL LVDGESQRYA AFGGKELREK FFNTPELKAL
IEGWSDADLE LLNRGGHDVR KIYAAYASAT KHKGSPTVII ARTIKGYGLG DTAQARNASH
QVKKLEFDAL KNLRDLLELP MTDEQVEHLE LYHPGPDSPE VKYTMERRAA LGGPVPARKV
EYPHPTVPTG EFYEEFAGGS KGRAVSTTMA AVQVISKLLR DKEIGKYIVP IVPDEARTFG
MDALVPRIGI YSPRGQTYTP VDSGSLMAYK ESKDGQMLEE GITEDGAMAS WIAAGTSYAN
HGVPTIPFFV FYSMFGMQRV GDLVWAAADQ RARGFLLGAT AGRTTLAGEG LQHQDGNSQL
QAYVVPNLKV YDPAFAYELA VIVEDGIQRM FVNDEDIFYY VTIDNENEVQ PAMPDDGRSH
DEIRQGIVKG LYRFQRSQSK GKLKAQILAG GPAMGAALEA AQKLEAYGVA ADIWSVTSYK
ELHQDALAVQ RHNMLHPTEA PRTSYVAQQL SKDNAPGVLI SVSDYVKLSA DGLNGHIDRK
IWTLGTDGFG RSEAREELRD FFEVDTKHVI LATLYALLRD GKIKGDVVQQ AITDLGIDPE
RQNPFLR
//
