(data stored in SCRATCH3701 zone)

SWISSPROT: PPDK_RICTY

ID   PPDK_RICTY              Reviewed;         880 AA.
AC   Q68WP2;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   11-DEC-2019, entry version 92.
DE   RecName: Full=Pyruvate, phosphate dikinase;
DE            EC=2.7.9.1 {ECO:0000250|UniProtKB:P22983};
DE   AltName: Full=Pyruvate, orthophosphate dikinase;
GN   Name=ppdK; OrderedLocusNames=RT0478;
OS   Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=257363;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-144 / Wilmington;
RX   PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA   McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA   McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA   Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA   Yu X.-J., Walker D.H., Weinstock G.M.;
RT   "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT   of other Rickettsiae.";
RL   J. Bacteriol. 186:5842-5855(2004).
CC   -!- FUNCTION: Catalyzes the reversible phosphorylation of pyruvate and
CC       phosphate. {ECO:0000250|UniProtKB:P22983}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + phosphate + pyruvate = AMP + diphosphate + H(+) +
CC         phosphoenolpyruvate; Xref=Rhea:RHEA:10756, ChEBI:CHEBI:15361,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.1;
CC         Evidence={ECO:0000250|UniProtKB:P22983};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000250|UniProtKB:P11155};
CC   -!- ACTIVITY REGULATION: Activated by light-induced dephosphorylation.
CC       Inhibited by dark-induced phosphorylation. Both reactions are catalyzed
CC       by PDRP1 (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- DOMAIN: The N-terminal domain contains the ATP/Pi active site, the
CC       central domain the pyrophosphate/phosphate carrier histidine, and the
CC       C-terminal domain the pyruvate active site. {ECO:0000250}.
CC   -!- PTM: Phosphorylation of Thr-458 in the dark inactivates the enzyme.
CC       Dephosphorylation upon light stimulation reactivates the enzyme (By
CC       similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: The reaction takes place in three steps, each mediated
CC       by a carrier histidine residue located on the surface of the central
CC       domain. The two first partial reactions are catalyzed at an active site
CC       located on the N-terminal domain, and the third partial reaction is
CC       catalyzed at an active site located on the C-terminal domain. For
CC       catalytic turnover, the central domain swivels from the concave surface
CC       of the N-terminal domain to that of the C-terminal domain.
CC   -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}.
DR   EMBL; AE017197; AAU03950.1; -; Genomic_DNA.
DR   RefSeq; WP_011190933.1; NC_006142.1.
DR   SMR; Q68WP2; -.
DR   STRING; 257363.RT0478; -.
DR   PRIDE; Q68WP2; -.
DR   EnsemblBacteria; AAU03950; AAU03950; RT0478.
DR   KEGG; rty:RT0478; -.
DR   eggNOG; ENOG4108HRN; Bacteria.
DR   eggNOG; COG0574; LUCA.
DR   HOGENOM; HOG000039664; -.
DR   KO; K01006; -.
DR   OMA; RRFVQMY; -.
DR   OrthoDB; 997616at2; -.
DR   BioCyc; RTYP257363:G1G0L-487-MONOMER; -.
DR   Proteomes; UP000000604; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.60; -; 1.
DR   Gene3D; 3.30.1490.20; -; 1.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR   InterPro; IPR018274; PEP_util_AS.
DR   InterPro; IPR000121; PEP_util_C.
DR   InterPro; IPR023151; PEP_util_CS.
DR   InterPro; IPR036637; Phosphohistidine_dom_sf.
DR   InterPro; IPR002192; PPDK_PEP-bd.
DR   InterPro; IPR010121; Pyruvate_phosphate_dikinase.
DR   InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR   InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR   PANTHER; PTHR22931; PTHR22931; 1.
DR   Pfam; PF00391; PEP-utilizers; 1.
DR   Pfam; PF02896; PEP-utilizers_C; 1.
DR   Pfam; PF01326; PPDK_N; 2.
DR   PIRSF; PIRSF000853; PPDK; 1.
DR   SUPFAM; SSF51621; SSF51621; 1.
DR   SUPFAM; SSF52009; SSF52009; 1.
DR   TIGRFAMs; TIGR01828; pyru_phos_dikin; 1.
DR   PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR   PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q68WP2.
DR   SWISS-2DPAGE; Q68WP2.
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Transferase.
FT   CHAIN           1..880
FT                   /note="Pyruvate, phosphate dikinase"
FT                   /id="PRO_0000289279"
FT   REGION          1..348
FT                   /note="N-terminal"
FT   REGION          349..405
FT                   /note="Linker 1"
FT   REGION          406..503
FT                   /note="Central"
FT   REGION          504..538
FT                   /note="Linker 2"
FT   REGION          539..879
FT                   /note="C-terminal"
FT   ACT_SITE        460
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250|UniProtKB:P11155"
FT   ACT_SITE        836
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P11155"
FT   METAL           750
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250|UniProtKB:P11155"
FT   METAL           774
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000250|UniProtKB:P11155"
FT   BINDING         97
FT                   /note="ATP"
FT                   /evidence="ECO:0000255"
FT   BINDING         566
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11155"
FT   BINDING         622
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11155"
FT   BINDING         750
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11155"
FT   BINDING         771
FT                   /note="Substrate; via carbonyl oxygen"
FT                   /evidence="ECO:0000250|UniProtKB:P11155"
FT   BINDING         772
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:P11155"
FT   BINDING         773
FT                   /note="Substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P11155"
FT   BINDING         774
FT                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000250|UniProtKB:P11155"
FT   MOD_RES         458
FT                   /note="Phosphothreonine; by PDRP1"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   880 AA;  98165 MW;  FFFE55AEEA138B34 CRC64;
     MNKLIYYFGN NGSDGNASMK NILGNKGAGL AEMSNLKLPI PNGFTITTEL CNYFYKHNNN
     LPKNFQNELQ QAITKLEITT GKIFGSTTSN PLLLSVRSGS TVSMPGMMDT ILNLGMNNEV
     CNALADSCGN KLFALDSYRR FLEMYGSTVL SIPSDLFEQI YEKHKVQADI YKDSDITVEL
     LEKIIDDFKR LHIKYTKQLI KDPYEQLESA IKAVLYSWKN NRAIVYRKLN NISEDFGTAI
     NIQEMVFGNL GKTSATGVVF TRSPSTGEKK LFGEFLINAQ GEDIVSGTRT PMPIIANDSN
     SMQAMMPEVF TKLSQIAKKL EEHYLDMQDI EFTIENNKLY ILQTRTAKRT AIAAINIAVQ
     MVEEKLISKE QALMRIDPES LNQLLHTRID YSKKLTAIAE GLPASPGAAT GIVVFSPYDA
     EKLSHHHKVI LVRHDTSPED INGMHVASGI LTIRGGMTSH AAVVARGMGK PCVCGTNNLS
     IDEQKQILIA GDIVIKQGDI ITIDGGSGKI FLGEMPLIQP TFSEESTLIL DWADEISSLK
     VRANAETVND ALVSIKFGAQ GIGLCRSEHM FFDKNKIPLV REMIIAPDIE RRQCALQKLL
     PLQTEDFKAL FRVMKNKPVN IRLLDPPLHE FLPTTDEDKK NLAHSLNLPL SMIHQRLHAM
     HEVNPMLGHR GCRLGICLPE IYQMQIEAIL TAIFELHKKE HIESNLELMI PLISNVAEIK
     KLKMDIYAVV KKLEQRYSYK FSFTLGTMIE LPRAALGSKK IAKEVDYFSF GTNDLTQTTY
     GISRDDIASF LPYYLEEKIF ESDPFTTLDE EGVGELIKIA IKRGKSSNAN LKLGACGEHA
     GNPTSIAFFH KMNLNYVSCS PYRIPIARIA AAQAKIKQGS
//

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