(data stored in SCRATCH zone)

SWISSPROT: Q7WAB7_BORPA

ID   Q7WAB7_BORPA            Unreviewed;       901 AA.
AC   Q7WAB7;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   08-MAY-2019, entry version 103.
DE   RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|PIRNR:PIRNR000156};
DE            EC=1.2.4.1 {ECO:0000256|PIRNR:PIRNR000156};
GN   Name=aceE {ECO:0000313|EMBL:CAE36764.1};
GN   OrderedLocusNames=BPP1462 {ECO:0000313|EMBL:CAE36764.1};
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311 {ECO:0000313|Proteomes:UP000001421};
RN   [1] {ECO:0000313|Proteomes:UP000001421}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253
RC   {ECO:0000313|Proteomes:UP000001421};
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.,
RA   Harris D.E., Holden M.T., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.M., Temple L., James K., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J.,
RA   Feltwell T., Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Norberczak H., O'Neil S., Ormond D., Price C.,
RA   Rabbinowitsch E., Rutter S., Sanders M., Saunders D., Seeger K.,
RA   Sharp S., Simmonds M., Skelton J., Squares R., Squares S., Stevens K.,
RA   Unwin L., Whitehead S., Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- FUNCTION: Component of the pyruvate dehydrogenase (PDH) complex,
CC       that catalyzes the overall conversion of pyruvate to acetyl-CoA
CC       and CO(2). {ECO:0000256|PIRNR:PIRNR000156}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[dihydrolipoyllysine-residue acetyltransferase]-(R)-N(6)-
CC         lipoyl-L-lysine + H(+) + pyruvate = [dihydrolipoyllysine-residue
CC         acetyltransferase]-(R)-N(6)-(S(8)-acetyldihydrolipoyl)-L-lysine
CC         + CO2; Xref=Rhea:RHEA:19189, Rhea:RHEA-COMP:10480, Rhea:RHEA-
CC         COMP:10481, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:83099, ChEBI:CHEBI:83111;
CC         EC=1.2.4.1; Evidence={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|PIRNR:PIRNR000156,
CC         ECO:0000256|SAAS:SAAS01133295};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|SAAS:SAAS01133305}.
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DR   EMBL; BX640427; CAE36764.1; -; Genomic_DNA.
DR   RefSeq; WP_010928049.1; NC_002928.3.
DR   EnsemblBacteria; CAE36764; CAE36764; BPP1462.
DR   KEGG; bpa:BPP1462; -.
DR   HOGENOM; HOG000115215; -.
DR   KO; K00163; -.
DR   OMA; HEVAVIM; -.
DR   BioCyc; BPAR257311:G1GSY-1502-MONOMER; -.
DR   Proteomes; UP000001421; 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   CDD; cd02017; TPP_E1_EcPDC_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
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   PANTHER; PTHR43825:SF3; PTHR43825:SF3; 1.
DR   Pfam; PF17831; PDH_E1_M; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   PIRSF; PIRSF000156; Pyruvate_dh_E1; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00759; aceE; 1.
PE   4: Predicted;
DR   PRODOM; Q7WAB7.
DR   SWISS-2DPAGE; Q7WAB7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001421};
KW   Magnesium {ECO:0000256|PIRSR:PIRSR000156-1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR000156-1};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000156,
KW   ECO:0000313|EMBL:CAE36764.1};
KW   Pyruvate {ECO:0000256|PIRNR:PIRNR000156, ECO:0000313|EMBL:CAE36764.1};
KW   Thiamine pyrophosphate {ECO:0000256|PIRNR:PIRNR000156,
KW   ECO:0000256|SAAS:SAAS01133301}.
FT   DOMAIN      150    302       TRANSKETOLASE_1. {ECO:0000259|Pfam:
FT                                PF00456}.
FT   DOMAIN      498    711       PDH_E1_M. {ECO:0000259|Pfam:PF17831}.
FT   METAL       241    241       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR000156-1}.
FT   METAL       271    271       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR000156-1}.
FT   METAL       273    273       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000156-1}.
SQ   SEQUENCE   901 AA;  100848 MW;  977F138012051727 CRC64;
     MSSFAQAGAL AAANDEDTLE TQEWLEALAA VLDREGPQRA HYLLERLIDE ARRSGAHIPF
     SPNTAYVNTI PPGLEPAHPG NLELEARIRS YVRWNAMAMV VRANKHNPPD GGDLGGHIAS
     FASLATMIGC GQNHFWHGET EEHGGDLVYF QGHTSPGMYG RAYLEGRLTE DQLNHFRREV
     DGKGLSSYPH PKLMPDFWQF PTVSMGLGPL MAIYQARFLK YLHARGIADT SNRKVWVFCG
     DGEMDEPESL GAIALAAREK LDNLIFVINC NLQRLDGPVR GNGKIIQELE GDFRGSGWNV
     IKLIWGGYWD PLLAHDKEGI LRRIMEEAVD GEYQAYKAND GKYVREHFFG KHPKLLEMVA
     RMSDEDIWRL NRGGHDPHKV YAAFDAASKH AGQPTVILAK TIKGYGMGHV GQAKNPTHQQ
     KKLELDSIRE FRDRFGIPIP DDKLEELPYY KPAEDSPEMQ YLHERRKALG GYLPKRRAKA
     DEQLKAPALD AFKAVLEPTA EGREISTTQA FVRVLNQILR DKDLGPRVVP ILADESRTFG
     MEGLFRQIGI YAPEGQKYTP VDKDQVMYYK ESADGQLLQE GINEAGAMSS WMAAATSYST
     NNRIMVPFYI YYSMFGFQRV GDLAWAAGDM QARGFLLGGT AGRTTLNGEG LQHEDGHSHL
     LASTIPNCVS YDPTFAHELA VIIQHGLKRM VEDQENVYYY LTVMNENYPQ PGLTAGDEEG
     IIRGMYKLKS HGKGKQRVQL MGSGTILREV MAAQELLEAD WGVASDIWSV TSLTELRRDG
     LDAERHNLLH PEGKQQVPYV TTQLAKSEGP IIASTDYMKL FADQIRPFVP KDRTYKVLGT
     DGFGRSDFRY KLREHFEVDR HFVVLASLRA LADEGKIPAA KVAEAIKKYG INPNKANPHH
     A
//

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