(data stored in SCRATCH zone)

SWISSPROT: Q4ZZ34_PSEU2

ID   Q4ZZ34_PSEU2            Unreviewed;       881 AA.
AC   Q4ZZ34;
DT   07-JUN-2005, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2005, sequence version 1.
DT   08-MAY-2019, entry version 91.
DE   RecName: Full=Pyruvate dehydrogenase E1 component {ECO:0000256|PIRNR:PIRNR000156};
DE            EC=1.2.4.1 {ECO:0000256|PIRNR:PIRNR000156};
GN   OrderedLocusNames=Psyr_0518 {ECO:0000313|EMBL:AAY35588.1};
OS   Pseudomonas syringae pv. syringae (strain B728a).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX   NCBI_TaxID=205918 {ECO:0000313|EMBL:AAY35588.1, ECO:0000313|Proteomes:UP000000426};
RN   [1] {ECO:0000313|EMBL:AAY35588.1, ECO:0000313|Proteomes:UP000000426}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B728a {ECO:0000313|EMBL:AAY35588.1,
RC   ECO:0000313|Proteomes:UP000000426};
RX   PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA   Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA   Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA   Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA   Kyrpides N.C., Ivanova N., Lindow S.E.;
RT   "Comparison of the complete genome sequences of Pseudomonas syringae
RT   pv. syringae B728a and pv. tomato DC3000.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(2005).
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; CP000075; AAY35588.1; -; Genomic_DNA.
DR   RefSeq; WP_003422379.1; NC_007005.1.
DR   RefSeq; YP_233626.1; NC_007005.1.
DR   SMR; Q4ZZ34; -.
DR   STRING; 205918.Psyr_0518; -.
DR   EnsemblBacteria; AAY35588; AAY35588; Psyr_0518.
DR   GeneID; 3365994; -.
DR   KEGG; psb:Psyr_0518; -.
DR   PATRIC; fig|205918.7.peg.538; -.
DR   eggNOG; ENOG4105DAQ; Bacteria.
DR   eggNOG; COG2609; LUCA.
DR   HOGENOM; HOG000115215; -.
DR   KO; K00163; -.
DR   OMA; REPWFPG; -.
DR   BioCyc; PSYR205918:G1G4J-519-MONOMER; -.
DR   Proteomes; UP000000426; 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; Q4ZZ34.
DR   SWISS-2DPAGE; Q4ZZ34.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000426};
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:AAY35588.1};
KW   Pyruvate {ECO:0000256|PIRNR:PIRNR000156};
KW   Thiamine pyrophosphate {ECO:0000256|PIRNR:PIRNR000156,
KW   ECO:0000256|SAAS:SAAS01133301}.
FT   DOMAIN       80    287       TRANSKETOLASE_1. {ECO:0000259|Pfam:
FT                                PF00456}.
FT   DOMAIN      469    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;  99303 MW;  F20AD47D0B458614 CRC64;
     MQDLDPVETQ EWLDALESVL DKEGEDRAHY LMTRLGELAT RSGSQLPYAI TTPYRNTIPV
     THEARMPGDL FMERRIRSLV RWNALAMVVK TNIGDPDLGG HISSFASSAT LYDIGFNYFF
     QAPTDEHGGD LIYFQGHASP GVYARAFMEG RITEEQMTNF RQEVDGNGLS SYPHPWLMKD
     FWQFPTVSMG LGPIQAIYQA RFMKYLEHRG YIPEGKQKVW CFLGDGETDE PESLGAIALA
     GREKLDNLIF VVNCNLQRLD GPVRGNAKII QELEGVFRGA QWNVTKVIWG RFWDPLLAKD
     VDGILQRRMD EVIDGEYQNY KAKDGAFVRE HFFNSPELKA MVADLSDDEI WKLNRGGHDP
     YKVYAAYHEA VNHKGQPTVV LAKTIKGYGT GAGEAKNTAH NTKKVDVDSL RHFRDRFDIP
     VKDSELEALP FYKPEEGSAE ARYLSERRAA LGGFVPQRRA QSFSLPTPPL ETLKAILDGS
     GDREISTTMA FVRILTQLVK DKEIGQRIVP IIPDEARTFG MEGMFRQLGI YSSVGQLYEP
     VDKEQVMFYR EDKKGQILEE GINEAGAMSS FIAAGTSYSS HNQPMIPFYI FYSMFGFQRI
     GDLAWAAGDS RTRGFLIGGT AGRTTLNGEG LQHEDGHSHI LASTIPNCRT FDPTYGYELA
     VIIQDGMRRM FEEQQDVFYY LTVMNESYAQ PAMPAGVEEG IVKGMYLLEE DTKEAAHHVQ
     LLGSGTILRE VREAAKILRD EFNIGADVWS VTSFNELRRD GLAAERNNRL HPGQKPQLSY
     VEECLNGRKG PVIASTDYMK LFADQIRQWV PTKEYKVLGT DGFGRSDSRK KLRHFFEVDR
     HFVVLAALEA LADRGDIEPK VVAEAIAKFG IDPEKRNPLD C
//

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