ID F3FHD3_PSESX Unreviewed; 740 AA.
AC F3FHD3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=Phosphoenolpyruvate synthase {ECO:0000256|ARBA:ARBA00021623};
DE EC=2.7.9.2 {ECO:0000256|ARBA:ARBA00011996};
DE AltName: Full=Pyruvate, water dikinase {ECO:0000256|ARBA:ARBA00033470};
DE Flags: Fragment;
GN ORFNames=PSYJA_11825 {ECO:0000313|EMBL:EGH29619.1};
OS Pseudomonas syringae pv. japonica str. M301072.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=629262 {ECO:0000313|EMBL:EGH29619.1, ECO:0000313|Proteomes:UP000004471};
RN [1] {ECO:0000313|EMBL:EGH29619.1, ECO:0000313|Proteomes:UP000004471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M301072PT {ECO:0000313|Proteomes:UP000004471};
RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT genomics of 19 Pseudomonas syringae isolates.";
RL PLoS Pathog. 7:E1002132-e1002132(2011).
CC -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC phosphoenolpyruvate. {ECO:0000256|ARBA:ARBA00002988}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + pyruvate = AMP + 2 H(+) + phosphate +
CC phosphoenolpyruvate; Xref=Rhea:RHEA:11364, ChEBI:CHEBI:15361,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001518};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC {ECO:0000256|ARBA:ARBA00004742}.
CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family.
CC {ECO:0000256|ARBA:ARBA00007837}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGH29619.1}.
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DR EMBL; AEAH01000551; EGH29619.1; -; Genomic_DNA.
DR AlphaFoldDB; F3FHD3; -.
DR HOGENOM; CLU_007308_6_2_6; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000004471; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008986; F:pyruvate, water dikinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
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 InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR006319; PEP_synth.
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; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom.
DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf.
DR NCBIfam; TIGR01418; PEP_synth; 1.
DR PANTHER; PTHR43030; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR PANTHER; PTHR43030:SF1; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR PRINTS; PR01736; PHPHTRNFRASE.
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:0000256|ARBA:ARBA00022777};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Pyruvate {ECO:0000313|EMBL:EGH29619.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGH29619.1}.
FT DOMAIN 2..327
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 364..436
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
FT DOMAIN 463..736
FT /note="PEP-utilising enzyme C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02896"
FT NON_TER 740
FT /evidence="ECO:0000313|EMBL:EGH29619.1"
SQ SEQUENCE 740 AA; 80312 MW; A07B2BD21E45A8FF CRC64;
MGGKNSSLGE MISNLAGAGV SVPGGFATTA QAYRDFLELS GLNEQIHAAL DALDVDDVNA
LARTGAQIRQ INMEAEFPEQ LNAQIRTAFA ELSAGNPNLA VAVRSSATAE DLPDASFAGQ
QETFLNIRGV ENVIRAAKEV FASLFNDRAI SYRVHQGFDH KLVALSAGVQ RIVRSETGTA
GVMFTLDTES GFRDVVFITG AYGLGETVVQ GAVNPDEFYV HKDTLAAGRP AILRRNLGSK
AIKMIYGEEA KAGRSARVID VEPADRARFC LSDAEVSELA KQAMIIEKHY KCPMDIEWAK
DGDDGKLYIV QARPETVKSR ASANVMERYL LKETGKVLVE GRAIGQRIGA GKVRIIKDVS
EMDKVQPGDV LVSDMTDPDW EPVMKRASAI VTNRGGRTCH AAIIARELGI PAVVGCGNAT
HTLQDGQGVT VSCAEGDTGY IFEGELGFDI KTNSVDAMPD LPFKIMMNVG NPDRAFDFAQ
LPNAGVGLAR LEFIINRMIG VHPKALLNYS VLPPEIRESV DKRIAGYDDP VGFYVEKLVE
GISTLAAAFT PKKVIVRLSD FKSNEYANLI GGKLYEPEEE NPMLGFRGAS RYISENFRDC
FELECRALKR VREEMGLTNV EIMVPFVRTL GEASQVIDLL AANGLKRGEN GLRIIMMCEL
PSNAILAEEF LEYFDGFSIG SNDLTQLTLG LDRDSGVIAH LFDERNPAVK KLLSNAIQAC
NKAGKYIGIC GQGPSDHPDL
//
