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 15-MAR-2017, entry version 113. 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 RT mlrA 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 RT furiosus with high homology to a gene encoding phosphoenolpyruvate RT synthetase from 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 RT P. 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: ATP + pyruvate + H(2)O = AMP + CC phosphoenolpyruvate + phosphate. {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 CC {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, CC the central domain the pyrophosphate/phosphate carrier histidine, CC and the C-terminal domain the pyruvate binding site. CC {ECO:0000250}. CC -!- MISCELLANEOUS: The reaction takes place in three steps, mediated CC by a phosphocarrier histidine residue located on the surface of CC the central domain. The two first partial reactions are catalyzed CC at an active site located on the N-terminal domain, and the third CC partial reaction is catalyzed at an active site located on the C- CC terminal domain. For catalytic turnover, the central domain CC swivels from the concave surface of the N-terminal domain to that CC of the C-terminal domain (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. CC {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; NC_003413.1. DR ProteinModelPortal; P42850; -. DR SMR; P42850; -. DR STRING; 186497.PF0043; -. DR PRIDE; P42850; -. DR EnsemblBacteria; AAL80167; AAL80167; PF0043. DR GeneID; 1467872; -. DR KEGG; pfu:PF0043; -. DR eggNOG; arCOG01111; Archaea. DR eggNOG; COG0574; LUCA. DR HOGENOM; HOG000230912; -. DR KO; K01007; -. DR OMA; QIRQWIM; -. DR OrthoDB; POG093Z00IO; -. 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 Gene3D; 3.30.1490.20; -; 2. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.50.30.10; -; 1. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. 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; IPR002192; PPDK_PEP-bd. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR PANTHER; PTHR43030:SF1; PTHR43030:SF1; 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; Complete proteome; Direct protein sequencing; Kinase; KW Magnesium; Metal-binding; Nucleotide-binding; Reference proteome; KW Transferase. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:11133966}. FT CHAIN 2 817 Phosphoenolpyruvate synthase. FT /FTId=PRO_0000147044. FT COMPBIAS 809 815 Poly-Glu. FT ACT_SITE 442 442 Tele-phosphohistidine intermediate. FT {ECO:0000250}. FT ACT_SITE 756 756 Proton donor. {ECO:0000250}. FT METAL 684 684 Magnesium. {ECO:0000250}. FT METAL 709 709 Magnesium. {ECO:0000250}. FT BINDING 540 540 Substrate. {ECO:0000250}. FT BINDING 587 587 Substrate. {ECO:0000250}. FT BINDING 684 684 Substrate. {ECO:0000250}. FT BINDING 706 706 Substrate; via carbonyl oxygen. FT {ECO:0000250}. FT BINDING 707 707 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 708 708 Substrate. {ECO:0000250}. FT BINDING 709 709 Substrate; via amide nitrogen. FT {ECO:0000250}. FT CONFLICT 8 8 W -> G (in Ref. 4; AA sequence). FT {ECO:0000305}. FT CONFLICT 747 747 K -> Q (in Ref. 1; AAA81512). FT {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 //