PPDK_ENTHI
ID PPDK_ENTHI Reviewed; 885 AA.
AC P37213;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Pyruvate, phosphate dikinase;
DE EC=2.7.9.1;
DE AltName: Full=Pyruvate, orthophosphate dikinase;
GN Name=PPDK;
OS Entamoeba histolytica.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=5759;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RX PubMed=8114821; DOI=10.1016/0166-6851(93)90193-2;
RA Bruchhaus I., Tannich E.;
RT "Primary structure of the pyruvate phosphate dikinase in Entamoeba
RT histolytica.";
RL Mol. Biochem. Parasitol. 62:153-156(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 442-626.
RC STRAIN=ATCC 30459 / HM-1:IMSS;
RX PubMed=1340319;
RA Saavedra-Lira E., Robinson O., Perez-Montfort R.;
RT "Partial nucleotide sequence of the enzyme pyruvate, orthophosphate
RT dikinase of Entamoeba histolytica HM1:IMSS.";
RL Arch. Med. Res. 23:39-40(1992).
CC -!- FUNCTION: Catalyzes the reversible phosphorylation of pyruvate and
CC phosphate. In E.histolytica and C.symbiosus, PPDK functions in the
CC direction of ATP synthesis.
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 -!- 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-452 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; X74596; CAA52673.1; -; Genomic_DNA.
DR EMBL; L03389; AAA19026.1; -; Unassigned_DNA.
DR PIR; S36601; S36601.
DR AlphaFoldDB; P37213; -.
DR SMR; P37213; -.
DR STRING; 5759.rna_EHI_009530-1; -.
DR PRIDE; P37213; -.
DR VEuPathDB; AmoebaDB:EHI5A_102340; -.
DR VEuPathDB; AmoebaDB:EHI7A_182430; -.
DR VEuPathDB; AmoebaDB:EHI8A_212360; -.
DR VEuPathDB; AmoebaDB:EHI_009530; -.
DR VEuPathDB; AmoebaDB:KM1_287560; -.
DR eggNOG; ENOG502QREJ; Eukaryota.
DR BRENDA; 2.7.9.1; 2080.
DR SABIO-RK; P37213; -.
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..885
FT /note="Pyruvate, phosphate dikinase"
FT /id="PRO_0000147051"
FT REGION 1..342
FT /note="N-terminal"
FT REGION 343..399
FT /note="Linker 1"
FT REGION 400..497
FT /note="Central"
FT REGION 498..533
FT /note="Linker 2"
FT REGION 534..885
FT /note="C-terminal"
FT ACT_SITE 454
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT ACT_SITE 839
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 91
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 561
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 617
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 752
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 752
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 773
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 774
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 775
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 776
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 776
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT MOD_RES 452
FT /note="Phosphothreonine; by PDRP1"
FT /evidence="ECO:0000250"
FT CONFLICT 539..540
FT /note="AG -> NA (in Ref. 2; AAA19026)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 885 AA; 98060 MW; 6F5FEAD7C21CC8DC CRC64;
MQRVYAFEDG DGTNKKLLGG KGAGLCTMTK IGLPVPQGFV ITTEMCKQFI ANGNKMPEGL
MEEVKKEYQL VEKKSGKVFG GEENPLLVSV RSGAAMSMPG MMDTILNLGL NDKTVVALAK
LTNNERFAYD SYRRFVSLFG KIALNACDEV YDKTLENKKV EKGVKLDTEL DANDMKELAQ
VFIKKTEEFT KQPFPVDPYA QLEFAICAVF RSWMGKRAVD YRREFKITPE QADGTAVSVV
SMVYGNMGND SATGVCFTRD PGTGENMFFG EYLKNAQGED VVAGIRTPQI ISKMAEDRDL
PGCYEQLLDI RKKLEGYFHE VQDFEFTIER KKLYMLQTRN GKMNATATVR TGVDMVEEGL
ITKEQAIMRI APQSVDQLLH KNMPANYAEA PLVKGLPASP GAATGAVVFD ADDAVEQAKG
KKVLLLREET KPEDIHGFFV AEGILTCRGG KTSHAAVVAR GMGKPCVSGA EGIKVDVAKK
IAKIGSLEVH EGDILTIDGS TGCVYKGEVP LEEPQVGSGY FGTILKWANE IKKIGVFAAG
DLPSAAKKAL EFGAEGIGLC RTERMFNAVE RLPIVVKMIL SNTLEERKKY LNELMPLQKQ
DFIGLLKTMN GLPVTVRLLD PPLHEFLPTL EELMREIFEM KLSGKTEGLA EKEVVLKKVK
ELMEVNPMIG HRGIRLGTTN PEIYEMQIRA FLEATREVIK EGINDHREIM IPNVTEVNEL
INLRKNVLEP VHEEVEKKYG IKVPFSYGTM VECVRAALTA DKIATEASFF SFGTNDLTQG
TFSYSREDSE NKFIPKYVEL KILPANPFEI LDRPGVGEVM RIAVTKGRQT RPELLVGICG
EHGGEPSSIE WCHMIGLNYV SCSSYRIPVA RIAAAQAQIR HPREN
