ID A0A0G1P041_9BACT Unreviewed; 144 AA.
AC A0A0G1P041;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=UX38_C0011G0019 {ECO:0000313|EMBL:KKU26007.1};
OS Microgenomates group bacterium GW2011_GWC1_46_16.
OC Bacteria.
OX NCBI_TaxID=1618527 {ECO:0000313|EMBL:KKU26007.1, ECO:0000313|Proteomes:UP000034323};
RN [1] {ECO:0000313|EMBL:KKU26007.1, ECO:0000313|Proteomes:UP000034323}
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:KKU26007.1}.
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DR EMBL; LCLZ01000011; KKU26007.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1P041; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000034323; 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 InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR006319; PEP_synth.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR PANTHER; PTHR43030; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR PANTHER; PTHR43030:SF1; PHOSPHOENOLPYRUVATE SYNTHASE; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 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:KKU26007.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 19..143
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT NON_TER 144
FT /evidence="ECO:0000313|EMBL:KKU26007.1"
SQ SEQUENCE 144 AA; 15762 MW; 85AFBC87AB983FA6 CRC64;
MTAPKFVLWF HEIDKDDIAR VGGKGANLGE MTKAGFPVPG GFVVTSSAYR HMIEENQLED
KIKALLKGLN VEDADALNRA SHEVQKIIER SPFPQAIEEQ VYKAYDKLGS NPLVAVRSSA
TAEDLPNASF AGQQETYLNV RGDA
//