ID K2GW74_ENTNP Unreviewed; 886 AA.
AC K2GW74;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=pyruvate, phosphate dikinase {ECO:0000256|ARBA:ARBA00011994};
DE EC=2.7.9.1 {ECO:0000256|ARBA:ARBA00011994};
DE Flags: Fragment;
GN ORFNames=ENU1_127350 {ECO:0000313|EMBL:EKE39458.1};
OS Entamoeba nuttalli (strain P19) (Amoeba).
OC Eukaryota; Amoebozoa; Evosea; Archamoebae; Mastigamoebida; Entamoebidae;
OC Entamoeba.
OX NCBI_TaxID=1076696 {ECO:0000313|EMBL:EKE39458.1, ECO:0000313|Proteomes:UP000006769};
RN [1] {ECO:0000313|EMBL:EKE39458.1, ECO:0000313|Proteomes:UP000006769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P19 {ECO:0000313|EMBL:EKE39458.1,
RC ECO:0000313|Proteomes:UP000006769};
RA Hannick L., Karamycheva S., Lorenzi H., Caler E.;
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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; JH927573; EKE39458.1; -; Genomic_DNA.
DR RefSeq; XP_008858207.1; XM_008859985.1.
DR AlphaFoldDB; K2GW74; -.
DR EnsemblProtists; EKE39458; EKE39458; ENU1_127350.
DR GeneID; 20074384; -.
DR VEuPathDB; AmoebaDB:ENU1_127350; -.
DR OMA; HFFHEVG; -.
DR OrthoDB; 3681850at2759; -.
DR Proteomes; UP000006769; Unassembled WGS sequence.
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; 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; 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 Kinase {ECO:0000313|EMBL:EKE39458.1};
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:EKE39458.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 17..54
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 56..294
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 422..503
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 519..879
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT ACT_SITE 455
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT ACT_SITE 840
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-1"
FT BINDING 562
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 618
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 753
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 753
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="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT BINDING 777
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-3"
FT BINDING 777
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR000853-2"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EKE39458.1"
SQ SEQUENCE 886 AA; 97998 MW; 010E5044B1F2057C CRC64;
IMQRVYAFED GDGTNKKLLG GKGAGLCTMT KIGLPVPQGF VITTEMCKQF IANGNKMPEG
LMEEVKKNMQ LVEKKSGKVF GGEENPLLVS VRSGAAMSMP GMMDTILNLG LNDKTVVALA
KLTNNERFAY DSYRRFVSLF GKIALNVDDE VYDKTLENKK VEKGVKLDTE LDANDMKELA
QVFIKKTEEF TKQPFPVDPY AQLEFAICAV FRSWMGKRAV DYRREFKITP EQADGTAVSV
VSMVYGNMGN DSATGVCFTR DPGTGENMFF GEYLKNAQGE DVVAGIRTPQ IISKMAEDAD
LPGCYEQLLD IRKKLEGYFH EVQDFEFTIE RKKLYMLQTR NGKMNATATV RTGVDMVEEG
LITKEQAIMR IAPQSVDQLL HKNMPANYAE APLVKGLPAS PGAATGAVVF DADDAVEQAK
GKKVLLLREE TKPEDIHGFF VAEGILTCRG GKTSHAAVVA RGMGKPCVSG AEGIKVDVAK
KIAKIGSLEV HEGDILTIDG STGCVYKGEV PLEEPQVGSG YFGTILKWAN EIKKIGVFAN
ADLPSAAKKA LEFGAEGIGL CRTERMFNAV ERLPIVVKMI LSNTLEERKK YLNELMPLQK
QDFIGLLKTM NGLPVTVRLL DPPLHEFLPT LEELMREIFE MKLSGKTEGL AEKEVVLKKV
KELMEVNPMI GHRGIRLGTT NPEIYEMQIR AFLEATAEVI KEGVKTHAEI MIPNVTEVNE
LINLRKNVLE PVHEEVEKKY GIKVPFMYGT MVECVRAALT ADKIATEASF FSFGTNDLTQ
GTFSYSREDS ENKFIPKYVE LKILPANPFE ILDRPGVGEV MRIAVTKGRQ TRPELLVGIC
GEHGGEPSSI EWCHMIGLNY VSCSSYRIPV ARIAAAQAQI RHPREN
//
