ID A0A0E0ITX7_ORYNI Unreviewed; 986 AA.
AC A0A0E0ITX7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00011994};
DE EC=2.7.9.1 {ECO:0000256|ARBA:ARBA00011994};
OS Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4536 {ECO:0000313|EnsemblPlants:ONIVA10G14340.1};
RN [1] {ECO:0000313|EnsemblPlants:ONIVA10G14340.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA10G14340.1};
RA Wing R.A., Hsing Y.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ONIVA10G14340.1}
RP IDENTIFICATION.
RC STRAIN=SL10 {ECO:0000313|EnsemblPlants:ONIVA10G14340.1};
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
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 AlphaFoldDB; A0A0E0ITX7; -.
DR EnsemblPlants; ONIVA10G14340.1; ONIVA10G14340.1; ONIVA10G14340.
DR Gramene; ONIVA10G14340.1; ONIVA10G14340.1; ONIVA10G14340.
DR HOGENOM; CLU_015345_0_2_1; -.
DR Proteomes; UP000006591; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:InterPro.
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:InterPro.
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:SF39; PYRUVATE, PHOSPHATE DIKINASE 2; 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; 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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
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 Reference proteome {ECO:0000313|Proteomes:UP000006591};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 171..405
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 416..469
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 535..616
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 631..984
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT REGION 87..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 568
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 946
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 674
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 731
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 860
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 860
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 881
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 882
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 883
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 884
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 884
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 986 AA; 108202 MW; B42C54AAB5BC44FD CRC64;
MRHGQSSDIE IFSPGGEEVR RRWREVVLRS QVRACQLRAY DALPAFLKHN EFIIDYYRSE
WPIKQALLSA FVVHNETIFQ TIKQKEANLR EDQSEPSSSM APAAHRDGAA EAVGQRVFHF
GKGRSDGNKT MKDLLGGKGA NLAEMASIGL SVPPGFTVST EACQQYQAQK AMPAGLWDEI
LAALTWVEGN MGAVLGDPRR PLLLSVRSGA AVSMPGMMDT VLNLGLNDHV VAGLAHRSGE
RFAYDSYRRF LDMFGNVVMD IPHSLFEEKI EAMKAALGLR NDTELTARDL KELVAQYKNV
YVEAKGEEFP SDPKKQLHLS VLAVFNSWDS ARAKKYRSIN QITGLKGTAV NVQCMVFGNM
GDTSGTGVLF TRNPSTGERK LYGEFLVNAQ GEDVVAGIRT PQDLDTMKDC MPEPYAELVE
NCKILESHYK EMMDIEFTVQ ENRLWMLQCR TGKRTGKGAV KIAVDMVNEG LIDRRSAIKM
VEPRHLDQLL HPQFESQSSY GDKVIATGLP ASPGAAVGQI VFTADDAEAW HAQGKSVILV
RTETSPEDVG GMNAAAGILT ARGGMTSHAA VVARGWGKCC VAGCSGIRVN DAEKVVLVAD
KVLCEGEWLS LNGSTGEVIL GKLPLSPPAL SGDLGEFMSW VDEVKKLKVK ANADTPADAL
TARNNGAEGI GLCRTEHMFF SSDERIKAMR QMIMAETIEH RQIALDRLLP YQRLDFEGIF
RAMDGLPVTI RLLDPPLHEF LPEGNVEDMV RLLSSGNVYT QEEILTRIEK LSEVNPMLGF
RGCRLGISYP ELTAMQARAI FEAAISMTEQ GVKVFPEIMV PLIGTPQELA QQVDVIREVA
EKVFANAETT ISYKIGSMIE VPRAALIADE IAALAEFFSF GTNDLTQMTF GYSRDDVGKF
LPTYLSKGIL QNDPFEVFDQ KGVGELVKVA VERGRKARPD LEVGICGEHG GEPSSVAFFA
KVGLNYVSCS PFRVPIARLA AAQVML
//
