ID H8WFY4_9POAL Unreviewed; 844 AA.
AC H8WFY4;
DT 16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT 16-MAY-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00011994};
DE EC=2.7.9.1 {ECO:0000256|ARBA:ARBA00011994};
DE Flags: Fragment;
GN Name=ppdk {ECO:0000313|EMBL:CCA60999.1};
OS Cyrtococcum patens.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; PACMAD clade;
OC Panicoideae; Panicodae; Paniceae; Boivinellinae; Cyrtococcum.
OX NCBI_TaxID=435324 {ECO:0000313|EMBL:CCA60999.1};
RN [1] {ECO:0000313|EMBL:CCA60999.1}
RP NUCLEOTIDE SEQUENCE.
RA Christin P.A., Edwards E.J., Besnard G., Boxall S.F., Gregory R.,
RA Kellogg E.A., Hartwell J., Osborne C.P.;
RT "Adaptive Evolution of C(4) Photosynthesis through Recurrent Lateral Gene
RT Transfer.";
RL Curr. Biol. 22:445-449(2012).
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:0000256|ARBA:ARBA00000529};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRSR:PIRSR000853-3};
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837}.
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DR EMBL; FR845989; CCA60999.1; -; mRNA.
DR AlphaFoldDB; H8WFY4; -.
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:0015979; P:photosynthesis; IEA:UniProtKB-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR Gene3D; 1.20.80.30; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 1.
DR Gene3D; 3.50.30.10; Phosphohistidine domain; 1.
DR Gene3D; 1.10.189.10; Pyruvate Phosphate Dikinase, domain 2; 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 NCBIfam; TIGR01828; pyru_phos_dikin; 1.
DR PANTHER; PTHR22931; PHOSPHOENOLPYRUVATE DIKINASE-RELATED; 1.
DR PANTHER; PTHR22931:SF9; PYRUVATE, PHOSPHATE DIKINASE 1, CHLOROPLASTIC; 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; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS00742; PEP_ENZYMES_2; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 2: Evidence at transcript level;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000313|EMBL:CCA60999.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|PIRSR:PIRSR000853-3};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR000853-3};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Photosynthesis {ECO:0000256|ARBA:ARBA00022531};
KW Pyruvate {ECO:0000313|EMBL:CCA60999.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..43
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 53..278
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 289..341
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 409..490
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 505..844
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 442
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 820
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 548
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 605
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 734
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 734
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 755
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 756
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 757
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 758
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 758
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:CCA60999.1"
FT NON_TER 844
FT /evidence="ECO:0000313|EMBL:CCA60999.1"
SQ SEQUENCE 844 AA; 91933 MW; B242675C9AF8FBF3 CRC64;
NKAMKELLGG KGANLAEMAS IGLSVPPGFT VSTEACQQYQ AAGRALPQGL WAEILDGLQW
VEEYMAARLG DPQRPLLLSV RSGAAVSMPG MMDTVLNLGL NDEVAAGLAA KSGDRFAYDS
YRRFLDMFGN VVMDIPHALF EEKLEAMKAA KGVKNDTDLT ASDLKELVAQ YKDVYVEAKG
EQFPSDPKKQ LELAVLAVFD SWDSPRAKKY RSINQITGLR GTAVNVQCMV FGNMGNTSGT
GVLFTRNPST GEKKLYGEFL VNAQGEDVVA GIRTPEDLDA MRDHMPEAYE ELVENCKILE
SHYKEMMDIE FTVQENRLWM LQCRTGKRTG KGAVKIAVDM VNDGLVERRT AIKMVEPGHL
DQLLHPQFEN PSAYKDKVIA TGLPASPGAA VGQIVFTAED AEAWHAQGKS AILVRTETSP
EDVGGMHAAV GILTARGGMT SHAAVVARGW GKCCVSGCSS IRVNDAEKVV VIGDMLLHEG
EWLSLNGSTG EVVLGKQPLS PPALSGDLGT FMSWVDEVRQ LKVMANADTP EDALAARNNG
AEGIGLCRTE HMFFASDERI KAVRQMIMAP TVELRQKALD RLLPYQRSDF EGIFRAMDGL
PVTIRLLDPP LHEFLPEGNV DEIVRELCSE TGANQEDALA RIEKLSEVNP MLGFRGCRLG
ISYPELTEMQ ARAIFEAAIA MTNQGVQVFP EIMVPLVGTP QELGHQVALI RQIANKVFTG
MGKTIGYKVG TMIEIPRAAL VADEIAEQAE FFSFGTNDLT QMTFGYSRDD VGKFLPIYLA
QGILQHDPFE VLDQRGVGEL VKFATERGRK ARPNLKVGIC GEHGGEPLSV AFFAKTGLDY
VSCS
//
