ID A0A158EUX3_9BURK Unreviewed; 899 AA.
AC A0A158EUX3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=AWB64_00385 {ECO:0000313|EMBL:SAL11351.1};
OS Caballeronia sordidicola.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=196367 {ECO:0000313|EMBL:SAL11351.1, ECO:0000313|Proteomes:UP000054893};
RN [1] {ECO:0000313|EMBL:SAL11351.1, ECO:0000313|Proteomes:UP000054893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 22029 {ECO:0000313|EMBL:SAL11351.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) 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|ARBA:ARBA00003157, 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; FCOC02000001; SAL11351.1; -; Genomic_DNA.
DR RefSeq; WP_060816914.1; NZ_FCOC02000001.1.
DR AlphaFoldDB; A0A158EUX3; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000054893; Unassembled WGS sequence.
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:SAL11351.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 142..303
FT /note="Transketolase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 493..707
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT BINDING 239
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 269
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 271
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 899 AA; 100648 MW; DC5CD33B871BD6F0 CRC64;
MSAVPDEVMK YVANAKDDED PQETAEWLEA LDGVISAEGP DRAHYLIEKQ IEFARVHGEH
LPFSANTPYI NTIPVAAQAK IPGDQDIEHK IRSYTRWNAI AMVLRAGKDT NVGGHIASFA
SAATLYDVGF NHFWHAPSPE HGGDLVFVQG HSSPGVYARA FLLGRLKESQ LDNFRQEVGG
EGISSYPHPW LMPDFWQFPT VSMGLGPIMA IYQARFMKYI DARGIAKAGD RKVWAFLGDG
ETDEPESLGA IGMAGRERLD NLVFVINCNL QRLDGPVRGN GKIIQELESE FRGAGWNVIK
VVWGSRWDSL FARDKTGALM RRMMEVVDGE YQTYKSESGA YVREHFFNTP ELKAMVAEWS
DEDIWNLNRG GHDPHKIYAA YTEASKTKGQ PTVILAKTIK GYGMGEAGQA MNITHQQKKL
HTDQLKKFRD QFKLPIPDDQ IADVPYLTFE EGSKELEYMR ARRQELGGYL PARRQKAESL
PVPDLSVFEP VLKGTGPGRE ISTTMAFVRI LNILLKDKAL GKRIVPIVPD ESRTFGMEGL
FRQIGIWNQD GQKYVPEDSD QLMFYRESET GQILQEGINE AGGMCDWIAA ATSYSTHNEI
MIPFYIFYSM FGFQRIGDLA WAAGDMRSRG FLLGGTAGRT TLNGEGLQHE DGHSLMWAAS
VPNCVSYDPT FGYELAVIMQ DGLRRMVAEQ EDVYYYVTVM NENYEHPAIP QSDSVASDIV
KGMYAFRKSD ADAKAPRVQL LGAGTIFNEV IAAADLLKND WNVAADLWSV PSFTELARNG
MDVERWNLLH PTEERRVAHV TNLLKDAKGP VVASTDYVRA LVDQIRGFVP NKFVVLGTDG
YGRSDTREKL RHFFEVDRYW VTVAALNALA DEGTIDRKVV AEAIKKYELD PAKPNPMTV
//
