PPDK_RICFE
ID PPDK_RICFE Reviewed; 878 AA.
AC Q4ULI7;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=RF_0735;
OS Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=315456;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1525 / URRWXCal2;
RX PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA Parinello H., Claverie J.-M., Raoult D.;
RT "The genome sequence of Rickettsia felis identifies the first putative
RT conjugative plasmid in an obligate intracellular parasite.";
RL PLoS Biol. 3:1-12(2005).
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-457 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}.
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DR EMBL; CP000053; AAY61586.1; -; Genomic_DNA.
DR RefSeq; WP_011271065.1; NC_007109.1.
DR AlphaFoldDB; Q4ULI7; -.
DR SMR; Q4ULI7; -.
DR STRING; 315456.RF_0735; -.
DR EnsemblBacteria; AAY61586; AAY61586; RF_0735.
DR KEGG; rfe:RF_0735; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_015345_0_2_5; -.
DR OMA; RRFVQMY; -.
DR OrthoDB; 997616at2; -.
DR Proteomes; UP000008548; 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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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_AMP/ATP-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; 3.
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;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Phosphoprotein; Transferase.
FT CHAIN 1..878
FT /note="Pyruvate, phosphate dikinase"
FT /id="PRO_0000289278"
FT REGION 1..347
FT /note="N-terminal"
FT REGION 348..404
FT /note="Linker 1"
FT REGION 405..502
FT /note="Central"
FT REGION 503..537
FT /note="Linker 2"
FT REGION 538..878
FT /note="C-terminal"
FT ACT_SITE 459
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT ACT_SITE 835
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 96
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 565
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 621
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 749
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 749
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 770
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 771
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 772
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 773
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 773
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT MOD_RES 457
FT /note="Phosphothreonine; by PDRP1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 878 AA; 98041 MW; 580312F71297D782 CRC64;
MKKLIYYFGS NGSDGNASMK NVLGNKGAGL AEMSNLKLPI PDGFTITTEL CNYFYTHNNN
FPKNFQNDLK KAITELEITT GKIFGSTSNP LLLSVRSGST VSMPGMMDTI LNLGMNNEVC
NALTDSCGDK RFALDSYKRF LEMYGTTVLS IPSDLFEQIY EKHKIQADIH KDSDITVELL
EKIIDDFKWL HIKYTKQLIN DPYEQLESAI KAVLHSWMSN RAVIYRKINN ISEGFGTAIN
IQAMVFGNLG KTSATGVAFT RSPSTGEKKL FGEFLINAQG EDIVSGTRTP MPIIANDSNS
MQAMMPEVFK ELSQIAKKLE EHYLDMQDIE FTIENNKLYI LQTRTAKRTA IAAINIAVQM
VEEKLISKEQ ALMRIDPESL NQLLHTRIDY SKGLTSIAEG LPASPGAATG IAVFSPYDAE
KLSHHHKVIL VRHDTSPEDI NGMHVSSGIL TIRGGMTSHA AVVARGMGKP CVCGTSNLSI
DEKKQILTAG DIVIKQGDII TIDGGSGKIF LGEMPLIQPT FSEESKLILD WADEISSLKV
RANAETVNDA LVSIKFGAQG IGLCRSEHMF FDKNKIPLVR EMIIAPDIER RKLAVQKLLP
LQMEDFKALF RVMKDKPVNI RLLDPPLHEF LPTTEEDKKN LANSLNLPLS MINQRLHAMH
EVNPMLGHRG CRLGICSPEI YQMQIEAIFT AIFELHKKEH IECNLELMMP LISNVGEIKK
LKMDIYEVIE ELEQRYRYKF SFMLGTMIEL PRAALGSKKI AKEVDYFSFG TNDLTQTTYG
ISRDDIASFL PYYLEEKIFE SDPFTTLDEE GVGELIEIAL KRGKSSNANL KLGACGEHAG
NPASIEFFHR MNLNYVSCSP YRIPIARIAS AQAKIKHG
