ID A0A261VJ94_9BORD Unreviewed; 885 AA.
AC A0A261VJ94;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=CAL22_06800 {ECO:0000313|EMBL:OZI74204.1};
OS Bordetella genomosp. 12.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=463035 {ECO:0000313|EMBL:OZI74204.1, ECO:0000313|Proteomes:UP000216429};
RN [1] {ECO:0000313|EMBL:OZI74204.1, ECO:0000313|Proteomes:UP000216429}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU6712 {ECO:0000313|EMBL:OZI74204.1,
RC ECO:0000313|Proteomes:UP000216429};
RA Spilker T., LiPuma J.;
RT "Complete and WGS of Bordetella genogroups.";
RL Submitted (MAY-2017) 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:ARBA00033635,
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};
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:OZI74204.1}.
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DR EMBL; NEVU01000002; OZI74204.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261VJ94; -.
DR OrthoDB; 9759664at2; -.
DR Proteomes; UP000216429; 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; IPR017600; Alpha-ketoglut_DH.
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 NCBIfam; TIGR03186; AKGDH_not_PDH; 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:OZI74204.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|PIRNR:PIRNR000156}.
FT DOMAIN 137..314
FT /note="Transketolase signature 1"
FT /evidence="ECO:0000259|Pfam:PF00456"
FT DOMAIN 488..703
FT /note="Pyruvate dehydrogenase E1 component middle"
FT /evidence="ECO:0000259|Pfam:PF17831"
FT BINDING 236
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 266
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
FT BINDING 268
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000156-1"
SQ SEQUENCE 885 AA; 97552 MW; FDF230EBA367DB71 CRC64;
MSARPAAVDS DAAETAEWRD ALSSLLHAEG SERAAYVLGC LIEHAGKLGL KLPHHANTPY
LNTIARAEEP AFPGDLELEA RLASINRWNA LAMVVRANQA HGELGGHIAS YASAADLFEV
GFNHFFRAGS AQQGADLIYM QPHSAPGIYA RAFLEGFLEE ADLALFRQEI TAREQGRRGL
SSYPHPWLMP DFWQFPTGSM GIGPINAIYQ ARYMRYLEHR GLAAASERRV WGIFGDGEMD
EPESIAALTL AAREKLDNLV FVINCNLQRL DGPVRGNGRI IDELETLYAG AGWNVIKLLW
GGDWDALLAA DDDAALARAF SHTVDGQFQT FAAKDGAYNR EHFFGQDPAL AALICGLDDD
AIDRLRRGGH DMVKIHAAYH RAVRHRGQPT VILAQTKKGF GMGEAGQGRM TTHQQKKLDD
QALLAFRDRF ALPLSDDDCL NLRFYRPAAD SRELRHLHAR RQALGGYIPR RSRGARSLAT
PPAVEFAPFA LQAQGKEMSS TMAVVRMLTQ LLKQPELGPR VVPIVADEAR TFGMANLFRQ
IGIYSAQGQL YEPEDIGSVL SYREARDGQI LEEGITEAGA ISSWTAAGTS YSTHDLPTLP
FYIYYSMFGF QRVGDLIWAA ADQRCRGFLI GATSGRSTLG GEGLQHQDGA SHLIASTVPN
CRAYDPAYAY EVAVIVEAGM RRMLGEQRDE FYYLTVTNEN LPQPDMPPDS TAGILRGMHC
VRQATAPRLR LLGAGPMLPE AQAAAALLEQ RYGVAAEVWS VTSFSELARD GRRAERDSAL
GLPGEPAWIQ QCLPSALPTI AVSDYVRAVP DQIRAWVPGR FRSLGTDGFG RSDTRARLRD
FFEIGAEWIA LHALDLLAEQ DADWRQARDA QRSRLSQRPR APWLE
//