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 17-JUN-2020, entry version 131. 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; 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=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: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 SMR; P42850; -. DR STRING; 186497.PF0043; -. DR PRIDE; P42850; -. DR EnsemblBacteria; AAL80167; AAL80167; PF0043. DR GeneID; 41711830; -. DR KEGG; pfu:PF0043; -. DR PATRIC; fig|186497.12.peg.47; -. DR eggNOG; arCOG01111; Archaea. DR eggNOG; COG0574; LUCA. DR HOGENOM; CLU_007308_6_2_2; -. DR KO; K01007; -. DR OMA; YRRFVQM; -. DR OrthoDB; 3139at2157; -. DR BioCyc; MetaCyc:MONOMER-20544; -. DR BioCyc; PFUR186497:G1FZR-47-MONOMER; -. DR BRENDA; 2.7.9.2; 5243. 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:0006090; P:pyruvate metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.60; -; 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 PANTHER; PTHR43030; PTHR43030; 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 SUPFAM; SSF51621; SSF51621; 1. DR SUPFAM; SSF52009; SSF52009; 1. DR TIGRFAMs; TIGR01418; PEP_synth; 1. DR PROSITE; PS00742; PEP_ENZYMES_2; 1. DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1. PE 1: Evidence at protein level; KW ATP-binding; Direct protein sequencing; Kinase; Magnesium; Metal-binding; KW 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 COMPBIAS 809..815 FT /note="Poly-Glu" 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 METAL 684 FT /note="Magnesium" FT /evidence="ECO:0000250" FT METAL 709 FT /note="Magnesium" FT /evidence="ECO:0000250" FT BINDING 540 FT /note="Substrate" FT /evidence="ECO:0000250" FT BINDING 587 FT /note="Substrate" FT /evidence="ECO:0000250" FT BINDING 684 FT /note="Substrate" FT /evidence="ECO:0000250" FT BINDING 706 FT /note="Substrate; via carbonyl oxygen" FT /evidence="ECO:0000250" FT BINDING 707 FT /note="Substrate; via amide nitrogen" FT /evidence="ECO:0000250" FT BINDING 708 FT /note="Substrate" FT /evidence="ECO:0000250" FT BINDING 709 FT /note="Substrate; via amide nitrogen" 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" 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 //