(data stored in ACNUC7421 zone)

SWISSPROT: Q3KJ49_PSEPF

ID   Q3KJ49_PSEPF            Unreviewed;       881 AA.
AC   Q3KJ49;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   08-MAY-2019, entry version 109.
DE   RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|PIRNR:PIRNR000156};
DE            EC=1.2.4.1 {ECO:0000256|PIRNR:PIRNR000156};
GN   OrderedLocusNames=Pfl01_0463 {ECO:0000313|EMBL:ABA72207.1};
OS   Pseudomonas fluorescens (strain Pf0-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=205922 {ECO:0000313|EMBL:ABA72207.1, ECO:0000313|Proteomes:UP000002704};
RN   [1] {ECO:0000313|EMBL:ABA72207.1, ECO:0000313|Proteomes:UP000002704}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pf0-1 {ECO:0000313|EMBL:ABA72207.1,
RC   ECO:0000313|Proteomes:UP000002704};
RX   PubMed=19432983; DOI=10.1186/gb-2009-10-5-r51;
RA   Silby M.W., Cerdeno-Tarraga A.M., Vernikos G.S., Giddens S.R.,
RA   Jackson R.W., Preston G.M., Zhang X.X., Moon C.D., Gehrig S.M.,
RA   Godfrey S.A., Knight C.G., Malone J.G., Robinson Z., Spiers A.J.,
RA   Harris S., Challis G.L., Yaxley A.M., Harris D., Seeger K., Murphy L.,
RA   Rutter S., Squares R., Quail M.A., Saunders E., Mavromatis K.,
RA   Brettin T.S., Bentley S.D., Hothersall J., Stephens E., Thomas C.M.,
RA   Parkhill J., Levy S.B., Rainey P.B., Thomson N.R.;
RT   "Genomic and genetic analyses of diversity and plant interactions of
RT   Pseudomonas fluorescens.";
RL   Genome Biol. 10:R51.1-R51.16(2009).
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}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000094; ABA72207.1; -; Genomic_DNA.
DR   RefSeq; WP_011332129.1; NC_007492.2.
DR   STRING; 205922.Pfl01_0463; -.
DR   World-2DPAGE; 0008:Q3KJ49; -.
DR   PRIDE; Q3KJ49; -.
DR   EnsemblBacteria; ABA72207; ABA72207; Pfl01_0463.
DR   KEGG; pfo:Pfl01_0463; -.
DR   eggNOG; ENOG4105DAQ; Bacteria.
DR   eggNOG; COG2609; LUCA.
DR   HOGENOM; HOG000115215; -.
DR   KO; K00163; -.
DR   OMA; REPWFPG; -.
DR   BioCyc; PFLU205922:G1G4S-468-MONOMER; -.
DR   Proteomes; UP000002704; 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; Q3KJ49.
DR   SWISS-2DPAGE; Q3KJ49.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002704};
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:ABA72207.1};
KW   Pyruvate {ECO:0000256|PIRNR:PIRNR000156, ECO:0000313|EMBL:ABA72207.1};
KW   Thiamine pyrophosphate {ECO:0000256|PIRNR:PIRNR000156,
KW   ECO:0000256|SAAS:SAAS01133301}.
FT   DOMAIN      194    287       TRANSKETOLASE_1. {ECO:0000259|Pfam:
FT                                PF00456}.
FT   DOMAIN      467    691       PDH_E1_M. {ECO:0000259|Pfam:PF17831}.
FT   METAL       225    225       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR000156-1}.
FT   METAL       255    255       Magnesium. {ECO:0000256|PIRSR:
FT                                PIRSR000156-1}.
FT   METAL       257    257       Magnesium; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000156-1}.
SQ   SEQUENCE   881 AA;  99525 MW;  245C2C789A2EDD3E CRC64;
     MQDLDPVETQ EWLDALESVL DKEGEDRAHY LMTRMGELAT RSGSQLPYAI TTPYRNTIPV
     THEARMPGDL FMERRIRSLV RWNAMAMVMR TNLKDSDLGG HISSFASSAT LYDIGFNYFF
     QAPTDEHGGD LIYFQGHTSP GVYARAFMEG RITEDQMNNF RQEVDGQGLS SYPHPWLMPD
     FWQFPTVSMG LGPIQAIYQA RFMKYLEHRG FIQPGKQKVW CFLGDGECDE PESLGAISLA
     GREKLDNLIF VINCNLQRLD GPVRGNGKII QELEGVFRGA QWNVTKVIWG RFWDPLLAKD
     VDGILQRRMD EVIDGEYQNY KAKDGAFVRE HFFNTPELKA MVADLSDDEI WKLNRGGHDP
     YKVYAAYHEA VNHKEQPTVI LAKTIKGYGT GAGEAKNTAH NTKKVDVDSL KLFRDRFDIP
     VKDEELENLP FFKPEPNSAE ARYLAERRAA LGGFVPQRRA QSFSVPTPDL DTLKAILDGS
     GDREISTTMA FVRILAQLVK DKEIGPRIVP IIPDEARTFG MEGMFRQLGI YSSVGQLYEP
     VDKDQVMFYK EDQKGQILEE GINEAGAMSS FIAAGTSYSS HNQPMLPFYI FYSMFGFQRI
     GDLAWAAGDS RTRGFLIGGT AGRTTLNGEG LQHEDGHSHL LAATIPNCRT YDPTYGYELA
     VIIQDGMKKM TEEQQDIFYY ITVMNESYQQ PAMPAGAEEG IKKGMYLLEE DTRDAAHHVQ
     LMGSGTILRE VREAAKILRE EFNIGADVWS VTSFNELRRD GLAVERSNRL KPGQKPKRSY
     VEECLSGRKG PVIASTDYMK LFAEQIRQWV PSKEFKVLGT DGFGRSDSRK KLRHFFEVDR
     HFVVLAALEA LADRGDIEPK VVAEAITKFG IDPEKRNPLD C
//

If you have problems or comments...

PBIL Back to PBIL home page