ID PPSA_PYRFU Reviewed; 817 AA. AC P42850; Q59672; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2002, sequence version 3. DT 27-NOV-2024, entry version 150. DE RecName: Full=Phosphoenolpyruvate synthase; DE Short=PEP synthase; DE EC=2.7.9.2; DE AltName: Full=Pyruvate, water dikinase; GN Name=ppsA; OrderedLocusNames=PF0043; OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=186497; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1; RX PubMed=7828869; DOI=10.1016/0378-1119(94)90651-3; RA Robinson K.A., Schreier H.J.; RT "Isolation, sequence and characterization of the maltose-regulated mlrA RT gene from the hyperthermophilic archaeum Pyrococcus furiosus."; RL Gene 151:173-176(1994). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1; RX PubMed=7628701; DOI=10.1016/0378-1119(95)00128-s; RA Jones C.E., Fleming T.M., Piper P.W., Littlechild J.A., Cowan D.A.; RT "Cloning and sequencing of a gene from the archaeon Pyrococcus furiosus RT with high homology to a gene encoding phosphoenolpyruvate synthetase from RT Escherichia coli."; RL Gene 160:101-103(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1; RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299; RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., RA DiRuggiero J., Robb F.T.; RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. RT horikoshii inferred from complete genomic sequences."; RL Genetics 152:1299-1305(1999). RN [4] RP PROTEIN SEQUENCE OF 2-21, FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=11133966; DOI=10.1128/jb.183.2.709-715.2001; RA Hutchins A.M., Holden J.F., Adams M.W.W.; RT "Phosphoenolpyruvate synthetase from the hyperthermophilic archaeon RT Pyrococcus furiosus."; RL J. Bacteriol. 183:709-715(2001). CC -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to CC phosphoenolpyruvate. {ECO:0000269|PubMed:11133966}. CC -!- CATALYTIC ACTIVITY: CC Reaction=pyruvate + ATP + H2O = phosphoenolpyruvate + AMP + phosphate + CC 2 H(+); Xref=Rhea:RHEA:11364, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:58702, ChEBI:CHEBI:456215; EC=2.7.9.2; CC Evidence={ECO:0000269|PubMed:11133966}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.11 mM for pyruvate {ECO:0000269|PubMed:11133966}; CC KM=0.40 mM for phosphoenolpyruvate {ECO:0000269|PubMed:11133966}; CC KM=0.39 mM for ATP {ECO:0000269|PubMed:11133966}; CC KM=1.00 mM for AMP {ECO:0000269|PubMed:11133966}; CC KM=38.4 mM for phosphate {ECO:0000269|PubMed:11133966}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:11133966}. CC -!- DOMAIN: The N-terminal domain contains the ATP/Pi binding site, the CC central domain the pyrophosphate/phosphate carrier histidine, and the CC C-terminal domain the pyruvate binding site. {ECO:0000250}. CC -!- MISCELLANEOUS: The reaction takes place in three steps, mediated by a CC phosphocarrier histidine residue located on the surface of the central CC domain. The two first partial reactions are catalyzed at an active site CC located on the N-terminal domain, and the third partial reaction is CC catalyzed at an active site located on the C-terminal domain. For CC catalytic turnover, the central domain swivels from the concave surface CC of the N-terminal domain to that of the C-terminal domain (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. {ECO:0000305}. 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; U08376; AAA81512.1; -; Genomic_DNA. DR EMBL; X80819; CAA56785.1; -; Genomic_DNA. DR EMBL; AE009950; AAL80167.1; -; Genomic_DNA. DR PIR; JC4176; JC4176. DR RefSeq; WP_011011155.1; NZ_CP023154.1. DR PDB; 8A8E; EM; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=1-817. DR PDBsum; 8A8E; -. DR AlphaFoldDB; P42850; -. DR EMDB; EMD-15230; -. DR SMR; P42850; -. DR STRING; 186497.PF0043; -. DR PaxDb; 186497-PF0043; -. DR GeneID; 41711830; -. DR KEGG; pfu:PF0043; -. DR PATRIC; fig|186497.12.peg.47; -. DR eggNOG; arCOG01111; Archaea. DR HOGENOM; CLU_007308_6_2_2; -. DR OrthoDB; 23397at2157; -. DR PhylomeDB; P42850; -. DR BioCyc; MetaCyc:MONOMER-20544; -. DR BRENDA; 2.7.9.2; 5243. DR SABIO-RK; P42850; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000001013; Chromosome. 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 Gene3D; 3.20.20.60; Phosphoenolpyruvate-binding domains; 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; IPR018274; PEP_util_AS. DR InterPro; IPR000121; PEP_util_C. DR InterPro; IPR023151; PEP_util_CS. DR InterPro; IPR036637; Phosphohistidine_dom_sf. DR InterPro; IPR002192; PPDK_AMP/ATP-bd. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR InterPro; IPR040442; Pyrv_Kinase-like_dom_sf. DR NCBIfam; TIGR01418; PEP_synth; 1. DR PANTHER; PTHR43030; PHOSPHOENOLPYRUVATE SYNTHASE; 1. DR PANTHER; PTHR43030:SF1; PHOSPHOENOLPYRUVATE SYNTHASE; 1. DR Pfam; PF00391; PEP-utilizers; 1. DR Pfam; PF02896; PEP-utilizers_C; 1. DR Pfam; PF01326; PPDK_N; 1. DR PIRSF; PIRSF000854; PEP_synthase; 1. DR PRINTS; PR01736; PHPHTRNFRASE. DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1. DR SUPFAM; SSF51621; Phosphoenolpyruvate/pyruvate domain; 1. DR SUPFAM; SSF52009; Phosphohistidine domain; 1. DR PROSITE; PS00742; PEP_ENZYMES_2; 1. DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Direct protein sequencing; Kinase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:11133966" FT CHAIN 2..817 FT /note="Phosphoenolpyruvate synthase" FT /id="PRO_0000147044" FT ACT_SITE 442 FT /note="Tele-phosphohistidine intermediate" FT /evidence="ECO:0000250" FT ACT_SITE 756 FT /note="Proton donor" FT /evidence="ECO:0000250" FT BINDING 540 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 587 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 684 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 684 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 706 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 707 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 708 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 709 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250" FT BINDING 709 FT /ligand="substrate" FT /evidence="ECO:0000250" FT CONFLICT 8 FT /note="W -> G (in Ref. 4; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 747 FT /note="K -> Q (in Ref. 1; AAA81512)" FT /evidence="ECO:0000305" FT STRAND 512..519 FT /evidence="ECO:0007829|PDB:8A8E" FT STRAND 521..525 FT /evidence="ECO:0007829|PDB:8A8E" FT HELIX 526..529 FT /evidence="ECO:0007829|PDB:8A8E" FT TURN 530..532 FT /evidence="ECO:0007829|PDB:8A8E" FT STRAND 534..540 FT /evidence="ECO:0007829|PDB:8A8E" FT HELIX 542..545 FT /evidence="ECO:0007829|PDB:8A8E" FT STRAND 548..550 FT /evidence="ECO:0007829|PDB:8A8E" FT HELIX 552..558 FT /evidence="ECO:0007829|PDB:8A8E" FT HELIX 561..578 FT /evidence="ECO:0007829|PDB:8A8E" FT STRAND 580..582 FT /evidence="ECO:0007829|PDB:8A8E" FT STRAND 584..587 FT /evidence="ECO:0007829|PDB:8A8E" FT HELIX 593..595 FT /evidence="ECO:0007829|PDB:8A8E" FT TURN 596..598 FT /evidence="ECO:0007829|PDB:8A8E" FT TURN 600..603 FT /evidence="ECO:0007829|PDB:8A8E" FT HELIX 611..613 FT /evidence="ECO:0007829|PDB:8A8E" FT HELIX 617..623 FT /evidence="ECO:0007829|PDB:8A8E" FT HELIX 625..639 FT /evidence="ECO:0007829|PDB:8A8E" FT TURN 640..642 FT /evidence="ECO:0007829|PDB:8A8E" FT STRAND 646..650 FT /evidence="ECO:0007829|PDB:8A8E" FT HELIX 656..668 FT /evidence="ECO:0007829|PDB:8A8E" FT TURN 673..675 FT /evidence="ECO:0007829|PDB:8A8E" FT STRAND 676..683 FT /evidence="ECO:0007829|PDB:8A8E" FT HELIX 686..690 FT /evidence="ECO:0007829|PDB:8A8E" FT HELIX 692..696 FT /evidence="ECO:0007829|PDB:8A8E" FT TURN 697..699 FT /evidence="ECO:0007829|PDB:8A8E" FT STRAND 702..706 FT /evidence="ECO:0007829|PDB:8A8E" FT HELIX 707..715 FT /evidence="ECO:0007829|PDB:8A8E" FT TURN 722..724 FT /evidence="ECO:0007829|PDB:8A8E" FT HELIX 725..727 FT /evidence="ECO:0007829|PDB:8A8E" FT HELIX 733..749 FT /evidence="ECO:0007829|PDB:8A8E" FT STRAND 752..758 FT /evidence="ECO:0007829|PDB:8A8E" FT HELIX 759..761 FT /evidence="ECO:0007829|PDB:8A8E" FT HELIX 763..772 FT /evidence="ECO:0007829|PDB:8A8E" FT STRAND 775..779 FT /evidence="ECO:0007829|PDB:8A8E" FT HELIX 784..806 FT /evidence="ECO:0007829|PDB:8A8E" SQ SEQUENCE 817 AA; 90485 MW; DA3A7A3CF13C614F CRC64; MAYRFIKWFE ELSKNDVPLV GGKGANLGEM TNAGIPVPPG FCVTAEAYKY FVENVKVSKE DVKRILGEKV NKGTISEVLA QAPDEPRPLQ DWIMDIISKT DVDDSKMLQE NTEAIRTLIK SLDMPSEIAE EIKQAYKELS QRFGQEEVYV AVRSSATAED LPEASFAGQQ ETYLDVLGAD DVIDKVKRCW ASLWTARATF YRAKQGFDHS KVYLSAVVQK MVNSEKSGVM FTANPVTNNR NEIMINASWG LGEAVVSGAV TPDEYIVEKG TWKIKEKVIA KKEVMVIRNP ETGRGTVMVK VAEYLGPEWV EKQVLTDEQI IEVAKMGQKI EDHYGWPQDI EWAYDKDDGK LYIVQSRPIT TLKEEATAEE AEEVEEAEVI LKGLGASPGI GAGRVVVIFD ASEIDKVKEG DILVTTMTNP DMVPAMKRAA AIVTDEGGRT SHAAIVSREL GIPCVVGTKE ATKKLKTGMY VTVDGTRGLV YKGIVKSLVK KKEEAKAEGG QVVVAGAPLV TGTMVKVNVS MPEVAERAAA TGADGVGLLR AEHMILSIGQ HPIKFIKEGK EEELVEKLAE GIEKVAAAFY PRPVWYRTLD APTNEFREMP GGEDEPEERN PMLGWRGIRR GLDQPELLRA EFKAIKKVVE KGYNNIGVML PLVSHPEQIR EAKRIAREVG LEPHKDVAWG VMIEVPAAAI IIEDLIKEGI DFVSFGTNDL TQYTLAIDRD NERVAKLYDE THPAVLKLIK HVIKVCKRYG VETSICGQAG SDPKMARILV RLGIDSISAN PDAVQLIRQV VAQEERKLML EAARKQLFEE EEEEELF //