ID A0A0G1L805_9BACT Unreviewed; 328 AA.
AC A0A0G1L805;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=UW45_C0002G0044 {ECO:0000313|EMBL:KKT56169.1};
OS Parcubacteria group bacterium GW2011_GWC2_44_22.
OC Bacteria.
OX NCBI_TaxID=1618930 {ECO:0000313|EMBL:KKT56169.1, ECO:0000313|Proteomes:UP000034136};
RN [1] {ECO:0000313|EMBL:KKT56169.1, ECO:0000313|Proteomes:UP000034136}
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:KKT56169.1}.
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DR EMBL; LCII01000002; KKT56169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1L805; -.
DR PATRIC; fig|1618930.3.peg.124; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000034136; 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 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:KKT56169.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 29..325
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
SQ SEQUENCE 328 AA; 36348 MW; 95C85491DE44CAF6 CRC64;
MPQTKKQSSK DESAIILTFA DITRHDATLA GGKGASLGEM LRAGISVPDG FVITANAFIQ
FIENSGLESL IQTIVKTINY QDTALVDQAS QKIRVLMSKA KFPVELEKSI LAEFKKLKAD
YVAVRSSATA EDSKTASWAG ELETYLNTTE KTLIQNIKKC WSSLYTPRAL FYRAEKKLLD
TPVAVAVVVQ KMIQSEIAGI CFTVHPVTQD RSQMIIEAGW GLGEAVVSGQ ITPDSYIINK
SNLSITDINI GTQQRMIVQK SASGENKWVA VKPADRERQK LDQKQIRELA KLCLKIEEHY
GSPQDIEWAF SHGCFYITQS RPITTLLV
//
