ID PPSA_PYRFU STANDARD; PRT; 817 AA. AC P42850; Q59672; DT 01-NOV-1995 (Rel. 32, Created) DT 28-FEB-2003 (Rel. 41, Last sequence update) DT 25-OCT-2004 (Rel. 45, Last annotation update) DE Probable phosphoenolpyruvate synthase (EC 2.7.9.2) (Pyruvate, water DE dikinase) (PEP synthase). GN Name=ppsA; OrderedLocusNames=PF0043; OS Pyrococcus furiosus. OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=2261; RN [1] RP SEQUENCE FROM N.A. RC STRAIN=Vc1 / DSM 3638 / ATCC 43587 / JCM 8422; RX MEDLINE=95129854; 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 SEQUENCE FROM N.A. RC STRAIN=Vc1 / DSM 3638 / ATCC 43587 / JCM 8422; RX MEDLINE=95354939; 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 SEQUENCE FROM N.A. RC STRAIN=Vc1 / DSM 3638 / ATCC 43587 / JCM 8422; RA Weiss R.B., Dunn D.M., Robb F.T., Brown J.R.; RT "The complete sequence of the Pyrococcus furiosus genome."; RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: ATP + pyruvate + H(2)O = AMP + CC phosphoenolpyruvate + phosphate. CC -!- PATHWAY: Essential step in gluconeogenesis when pyruvate and CC lactate are used as a carbon source. CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. 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; -. DR EMBL; X80819; CAA56785.1; -. DR EMBL; AE010130; AAL80167.1; -. DR PIR; JC4176; JC4176. DR HSSP; O76283; 1H6Z. DR InterPro; IPR008279; PEP_mobile. DR InterPro; IPR006318; PEP_P_trans. DR InterPro; IPR006319; PEP_synth. DR InterPro; IPR000121; PEP_utilizers. DR InterPro; IPR002192; PPDK_N_term. DR Pfam; PF00391; PEP-utilizers; 1. DR Pfam; PF02896; PEP-utilizers_C; 1. DR Pfam; PF01326; PPDK_N; 1. DR PRINTS; PR01736; PHPHTRNFRASE. DR ProDom; PD002376; K_bP_aldolase; 1. DR ProDom; PD000940; PEP_utilizers; 1. DR TIGRFAMs; TIGR01418; PEP_synth; 1. DR PROSITE; PS00742; PEP_ENZYMES_2; 1. DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1. KW ATP-binding; Complete proteome; Kinase; Phosphorylation; Transferase. FT ACT_SITE 442 442 Tele-phosphohistidine intermediate (By FT similarity). FT MOD_RES 442 442 Phosphohistidine (By similarity). FT DOMAIN 809 815 Poly-Glu. FT CONFLICT 747 747 K -> Q (in Ref. 1). 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 //