ID J7T0D5_CLOS1 Unreviewed; 855 AA. AC J7T0D5; DT 31-OCT-2012, integrated into UniProtKB/TrEMBL. DT 31-OCT-2012, sequence version 1. DT 27-MAR-2024, entry version 40. 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=CLOSPO_03029 {ECO:0000313|EMBL:EDU36860.1}; OS Clostridium sporogenes (strain ATCC 15579). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=471871 {ECO:0000313|EMBL:EDU36860.1, ECO:0000313|Proteomes:UP000006610}; RN [1] {ECO:0000313|Proteomes:UP000006610} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15579 {ECO:0000313|Proteomes:UP000006610}; RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D., RA Gordon J., Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., RA Johnson M., Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., RA Wilson R.K.; RT "Draft genome sequence of Clostridium sporogenes ATCC 15579."; RL Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases. 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:EDU36860.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; ABKW02000004; EDU36860.1; -; Genomic_DNA. DR RefSeq; WP_003485735.1; NZ_DS981517.1. DR AlphaFoldDB; J7T0D5; -. DR HOGENOM; CLU_005950_0_0_9; -. DR Proteomes; UP000006610; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0008986; F:pyruvate, water dikinase activity; IEA:InterPro. 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; 3.50.30.10; 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; 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. PE 4: Predicted; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EDU36860.1}; 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:EDU36860.1}; KW Transferase {ECO:0000256|ARBA:ARBA00022679}. FT DOMAIN 16..314 FT /note="Pyruvate phosphate dikinase AMP/ATP-binding" FT /evidence="ECO:0000259|Pfam:PF01326" FT DOMAIN 777..849 FT /note="PEP-utilising enzyme mobile" FT /evidence="ECO:0000259|Pfam:PF00391" FT REGION 728..748 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 855 AA; 95144 MW; 5A9E46BF34ADEADD CRC64; MIYYILPLAY KQATLEMVGG KGMSLSKLMT AGIPVPDGFH VTTASYQSFV EMNRIQPHIN KLLDGIDSNN TSQLEDVSTQ IGMLFHNGEM PQEVSAAIKT AYAGLGNIAV AVRSSATAED LPDASFAGQQ ETYLNIQGEN EVLAAVKRCW ASLWTARAIA YRVKNDIKQE IVALAVVVQK LAFSDASGVM FTLNPINGRR SEMIINAAWG LGESVVSSLV TPDTIVVDKN AERIVSYEVA NKEIMTVRTS DGTEEIPVPE RLRKKHALTR NQVMRLTQLG KKIEKYYQMP MDVEWALEKD KLYIVQARPI TVLPPEWTLP EKDVIYTKGS LAEHLPNPVT PLFATLGLEI VNRASALLWV DMFGKSAKKL LPENGAYTII NGYVYLSAKS KPLLIAVKSL SPRSLRRALT NSVARWEAAR KEFEDVIKQW EEKPMHMLNA HQIMEGIQTV FYAACIYFTR IQLTLPAASI SETLFTKLFQ GAARRAGMTD TSVFLLGFDT IALQAEKNLW SLSEWVKQNS TLNLYLQNNP TTKIAEDFMS SVLPAEVSQE VWIEWKNRIN QYFKEFGRTA YEFDFAYSTP QETLTPTFES IKTFVEGKGE SPFLRQATFE KRRKQAEEEI LQHIGSSRKK LFLKLLHWAQ ETAPMRENAI YLMGMGHPLI RRMFQEISAR LIRGGVTSHL DDIYWLTKSE LEKLIVQLDE NIPLSDRSKA ILARKTELKK YQGYVPPAQL PEKNAKSTSH APQKQKDGKT VLRGIGTSSG VVTARACVLN SPADFENFQP GSVLVAVTTT PAWTPLFASA SAIVTDIGGP LSHSSIVARE YGIPAVMATH TATRSIESGQ MITVDGSEGT VTING //