ID D8WWQ5_9FIRM Unreviewed; 334 AA.
AC D8WWQ5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 26.
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;
OS Clostridia bacterium enrichment culture clone BF.
OC Bacteria; Bacillota; Clostridia; environmental samples.
OX NCBI_TaxID=857391 {ECO:0000313|EMBL:ADJ94009.1};
RN [1] {ECO:0000313|EMBL:ADJ94009.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20545743; DOI=10.1111/j.1462-2920.2010.02248.x;
RA Abu Laban N., Selesi D., Rattei T., Tischler P., Meckenstock R.U.;
RT "Identification of enzymes involved in anaerobic benzene degradation by a
RT strictly anaerobic iron-reducing enrichment culture.";
RL Environ. Microbiol. 12:2783-2796(2010).
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}.
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DR EMBL; GU357999; ADJ94009.1; -; Genomic_DNA.
DR AlphaFoldDB; D8WWQ5; -.
DR UniPathway; UPA00138; -.
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:ADJ94009.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 14..328
FT /note="Pyruvate phosphate dikinase AMP/ATP-binding"
FT /evidence="ECO:0000259|Pfam:PF01326"
FT NON_TER 334
FT /evidence="ECO:0000313|EMBL:ADJ94009.1"
SQ SEQUENCE 334 AA; 36614 MW; 4748DB849A3BB2EB CRC64;
MIRSFKDLTI NDVPLVGGKC ASLGEMVRAG KNVPLGFAVT VNAYKQFVME TGIDQKIREA
MSEHGLNNNT DVSFHEAAKI IMPLVKATPI PNSIREAITV AYNELSEKYG TKDVMVAVRS
SATMEDAADA SYAGQHETYL NIVGLENVLE RIKECWASLF SAPALHYRSS KDIEPDEALM
AVAVQKMINS RSAGVAFTVD PVTGDTSKIV IEGAWGLGEG VVSGNVTPDH FSVDRNTMEI
LERWISPKTI HYVRDPETGE TVVRDVEKFR QNLPCINDEE IIQLARMALS IEQHYGKPQD
IEWAIDTGLA LPEGLLILQS RPVTVWGGVK AVNG
//
