ID A0A0G1VQS7_9BACT Unreviewed; 759 AA.
AC A0A0G1VQS7;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
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};
GN ORFNames=UY45_C0003G0055 {ECO:0000313|EMBL:KKW08848.1};
OS Parcubacteria group bacterium GW2011_GWA1_49_26.
OC Bacteria.
OX NCBI_TaxID=1618797 {ECO:0000313|EMBL:KKW08848.1, ECO:0000313|Proteomes:UP000034066};
RN [1] {ECO:0000313|EMBL:KKW08848.1, ECO:0000313|Proteomes:UP000034066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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 -!- 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:KKW08848.1}.
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DR EMBL; LCQA01000003; KKW08848.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1VQS7; -.
DR PATRIC; fig|1618797.3.peg.358; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000034066; 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; 2.
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; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR PANTHER; PTHR43030; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR PANTHER; PTHR43030:SF1; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52009; Phosphohistidine domain; 1.
DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1.
PE 4: Predicted;
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:KKW08848.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 16..299
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT DOMAIN 680..752
FT /note="PEP-utilising enzyme mobile"
FT /evidence="ECO:0000259|Pfam:PF00391"
SQ SEQUENCE 759 AA; 84838 MW; 59B866978325C1BA CRC64;
MSSIIWLEKL GQDDVAIAGG KGAQLGELKK AGFSVPDGFV VSTVVYKNLV GGSGIQEKIH
ELLSNLDLEN TEKLQEVSDK IQALFASVSL QQDVAEEILK AYKSLGGLVA VRSSATAEDR
KEASFAGQQA TFLHIKGEEA LIDAVKKCMA SLFTARAIFY RDQQRVGHED VSIAVVIQKM
VQAQKAGVAF SINPVTSDVS EVVIEAVAGL GEAVVGGQAT PDNYVLEKKT LNVKERHLQA
DNSVLQDLEI KELGELVQKI EAHYGYAQDI EWAIDENGAV QILQARPVTT LQPARETTKW
KKIISREYGV QYTELSLRSL SPENKFIVPE PFYEQVYIPE EDNEVCYIDE ARWNAFVGAL
KERYLEQPEN YDEFEKLFME TGTDYVEIAK QTAQENLEDK SSNELKKLYL DYQKKSLRYA
PFIWIQFIIN NFFADKAKEI LVEKLGQDNP KLYDFYEVIV KPSQKAASIR LGEVAAKWKE
LNYEEKNQAY ENFKWIPCLD IHNRPWTKEE FSSHVSEFVK EEKELIASSE HVLEEVNPSA
KEKRTLEIAR SLTYLKDLKD DFRRQGVFYG QVLFQEIAKR MGIELDGISY MLESEIVEFL
DSSTTGTQSV VDERKNGFVI FFSENKEIVC KSGDAIESAL RELGLAVLHE FSEEIKGVPA
SLGHAKGIVT IVRGVSNLSK VKKGDVLVAV VTHPDYVPAM QRAVAIVTDE GGITSHAAIV
SRELGLPCIV GTEHATKALK DGDFVEVDAT SGFVRKLKT
//
