PPDK_GIAIN
ID PPDK_GIAIN Reviewed; 884 AA.
AC P51776;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Pyruvate, phosphate dikinase;
DE EC=2.7.9.1;
DE AltName: Full=Pyruvate, orthophosphate dikinase;
OS Giardia intestinalis (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=5741;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CH-O2-4A1;
RX PubMed=8813668; DOI=10.1016/0166-6851(96)02605-9;
RA Bruderer T., Wehrli C., Koehler P.;
RT "Cloning and characterization of the gene encoding pyruvate phosphate
RT dikinase from Giardia duodenalis.";
RL Mol. Biochem. Parasitol. 77:225-234(1996).
CC -!- FUNCTION: Catalyzes the reversible phosphorylation of pyruvate and
CC phosphate.
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 binding site, the
CC central domain the pyrophosphate/phosphate carrier histidine, and the
CC C-terminal domain the pyruvate binding site. {ECO:0000250}.
CC -!- PTM: Phosphorylation of Thr-462 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; Z54168; CAA90880.1; -; Genomic_DNA.
DR AlphaFoldDB; P51776; -.
DR SMR; P51776; -.
DR PRIDE; P51776; -.
DR VEuPathDB; GiardiaDB:DHA2_9909; -.
DR VEuPathDB; GiardiaDB:GL50581_4299; -.
DR VEuPathDB; GiardiaDB:GL50803_009909; -.
DR eggNOG; ENOG502QREJ; Eukaryota.
DR BRENDA; 2.7.9.1; 2401.
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..884
FT /note="Pyruvate, phosphate dikinase"
FT /id="PRO_0000147052"
FT REGION 1..351
FT /note="N-terminal"
FT REGION 352..408
FT /note="Linker 1"
FT REGION 409..507
FT /note="Central"
FT REGION 508..542
FT /note="Linker 2"
FT REGION 543..884
FT /note="C-terminal"
FT ACT_SITE 464
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 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 570
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 626
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 753
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 753
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="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 777
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT BINDING 777
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P11155"
FT MOD_RES 462
FT /note="Phosphothreonine; by PDRP1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 884 AA; 97630 MW; 82E2BE9C09C0E772 CRC64;
MSTRRVYFFG ETPENQPANS ELCRKVLGGK GISLAAMIKL GMPVPLGFTI TCQTCVEYQK
TASWPKGLKE EVASNLKLLE EKMGKTFGDN TNPLLVSVRS GAAVSMPGMM DTILNLGLND
ESVKGLAAVT GNARFAYDSY RRFMQMFGDV CLGIDHDKFE HALDAVKTRY GRKTDPELTA
DELEEVCEAY RKICVAATGK TFPQCPHEQL ELAINAVFKS WTNPRAQAYR TLNKLDHNMG
TAVNVQSMVF GNTGDDSGTG VGFTRCPKTG EKFSYLYGEF LQNAQGEDVV AGIRTPVNLK
EMPTINASWK ACYDELSLIY AKLEGYYNDM VDLEFTVENG KLWMLQARAG KRTGFAMVRI
AIDMCKEGML TEEEALLRID ANKINEFLFK RFDPSVKPVV LGKGIPASPG AAVGVICFCP
MRTCELAEQG KKVILTRIET SPEDILGMDR AVGILTARGG QTSHAAVVAR GMGKCCVAGA
DCCQINYATK TLVIGDRKFK EGDFISINGT TGEIYNGAVQ TIEPGITDDL QTIMDWSDKY
RVLKIRTNAD TPHDAAVARK FGAEGIGLCR TEHMFFAADR IMAMREMILS DDEGARRTAL
NKLLPFQRED FIGIFKAMDG KGVNIRLLDP PLHEFLPHTR DLQKKLAEDM NKKHRHIHER
VEDLHEVNPM LGFRGVRLGI VYPEISEMQV RAILEAACIV SREGVTVKPE IMIPVLFSEN
EMEIMHALVN RVAASVFKEH GTTVDYEVGT MIELPRACVM ADKIAQTAQY FSFGTNDLTQ
TTFGISRDDA GKFIPKYIDR GIFKVDPFVT LDQQGVGALM KMAIEGGRST RTDMKIGICG
EQTDPASILF LHKIGLNYVS CSPYRVPVAR VAAAIAAIKA RTNQ
