ID A0A0A1UES6_ENTIV Unreviewed; 884 AA.
AC A0A0A1UES6;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=Pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00011994, ECO:0000256|PIRNR:PIRNR000853};
DE EC=2.7.9.1 {ECO:0000256|ARBA:ARBA00011994, ECO:0000256|PIRNR:PIRNR000853};
GN ORFNames=EIN_153430 {ECO:0000313|EMBL:ELP91326.1};
OS Entamoeba invadens IP1.
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=370355 {ECO:0000313|EMBL:ELP91326.1, ECO:0000313|Proteomes:UP000014680};
RN [1] {ECO:0000313|EMBL:ELP91326.1, ECO:0000313|Proteomes:UP000014680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IP1 {ECO:0000313|EMBL:ELP91326.1,
RC ECO:0000313|Proteomes:UP000014680};
RA Zafar N., Inman J., Hall N., Lorenzi H., Caler E.;
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
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|PIRNR:PIRNR000853};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|PIRNR:PIRNR000853, ECO:0000256|PIRSR:PIRSR000853-3};
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837, ECO:0000256|PIRNR:PIRNR000853}.
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DR EMBL; KB206474; ELP91326.1; -; Genomic_DNA.
DR RefSeq; XP_004258097.1; XM_004258049.1.
DR AlphaFoldDB; A0A0A1UES6; -.
DR EnsemblProtists; ELP91326; ELP91326; EIN_153430.
DR GeneID; 14890162; -.
DR KEGG; eiv:EIN_153430; -.
DR VEuPathDB; AmoebaDB:EIN_153430; -.
DR OrthoDB; 3681850at2759; -.
DR Proteomes; UP000014680; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050242; F:pyruvate, phosphate dikinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:UniProtKB-UniRule.
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; 1.
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.
DR PROSITE; PS50889; S4; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000313|EMBL:ELP91326.1};
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 Pyruvate {ECO:0000313|EMBL:ELP91326.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000014680};
KW RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00182};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ELP91326.1}.
FT DOMAIN 54..297
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 421..502
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 519..878
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 454
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 839
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 561
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 617
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 752
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 752
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 773
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 774
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 775
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 776
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 776
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
SQ SEQUENCE 884 AA; 97546 MW; BBCACCF166D53F34 CRC64;
MRSVYDFEDG DGTNKKLLGG KGAGLCTMTK IGLPVPQGFV ITTEQCKAFI ANNNKLPEGL
MEEVKKHMAA VEKKSGKVFG GETNPLLVSV RSGAAMSMPG MMDTILNLGL NDKTVVALAK
LTNNERFAYD SYRRFVSLFG RIALGVEDAV YDKPLEEKKV AKGVKLDTEL SAEDMKELAQ
IYIKKTEEAT KNAFPMCPFA QLECAISAVF RSWMGRRAVD YRREFKITDE QADGTGVSVV
SMVYGNMGND SATGVCFTRD PGTGENVFFG EYLKNAQGED VVAGIRTPQP INTMADDKDL
PDAYNQLLDI RKKLEGYFHE VQDFEFTIEK NKVYMLQTRN GKMNAVSTVR TGVEMVSEGL
ITKEQAILRL SPQSVDQLLH KNIPVDFKGT PLVQGLPASP GAACGAVVFD ADDAVEQSKA
KKVLLLREET KPEDIHGFFV AQGILTCRGG KTSHAAVVAR GMGKPCVSGA EGIKVDVNKK
VATIGSLTVK EGDILTIDGS TGKVYQGELK LEEPNIGSGY FGTMLQWANE IKKIGVFANA
DLPSAAKKAI EFGAEGIGLC RTERMFNAVE RLPIVVKMIL AETIEERNKF LNELMPLQKE
DFRGLLTTMN GLPVTIRLLD PPLHEFLPTL EELMREIFEM KLANKTEGLA DKERVMRKVK
ELMEVNPMIG HRGIRLGTTN PEIYEMQIRA FLEATAEVIK AGIKTHAEIM IPNVTEVNEL
IHLRKTVLDR VHKEVETKYG IKVPFMYGTM VECVRAALTA DKIATEAEFF SFGTNDLTQG
TFSYSREDCE NKFLPKYVEL KILPANPFEI LDRPGVGEVM KIGVERGRKT RPDLIVGICG
EHGGEPSSIE WCHMIGLNYV SCSSFRIPVA RIAAAQAQIR HPKN
//
