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Database: UniProt
Entry: A0A261VJ94_9BORD
LinkDB: A0A261VJ94_9BORD
Original site: A0A261VJ94_9BORD 
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
//
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