ID PPSA_PYRFU STANDARD; PRT; 817 AA. AC P42850; Q59672; DT 01-NOV-1995 (Rel. 32, Created) DT 01-FEB-1996 (Rel. 33, Last sequence update) DT 01-NOV-1997 (Rel. 35, Last annotation update) DE PROBABLE PHOSPHOENOLPYRUVATE SYNTHASE (EC 2.7.9.2) (PYRUVATE,WATER DE DIKINASE) (PEP SYNTHASE). GN PPSA. OS Pyrococcus furiosus. OC Archaea; Euryarchaeota; Thermococcales; Thermococcaceae; Pyrococcus. RN [1] RP SEQUENCE FROM N.A. RC STRAIN=DSM 3638; RX MEDLINE; 95129854. 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=DSM 3638; RX MEDLINE; 95354939. 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). 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: TO OTHER PEP-UTILIZING ENZYMES. CC -------------------------------------------------------------------------- CC This SWISS-PROT entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use by non-profit institutions as long as its content is in no way CC modified and this statement is not removed. Usage by and for commercial CC entities requires a license agreement (See http://www.isb-sib.ch/announce/ CC or send an email to license@isb-sib.ch). CC -------------------------------------------------------------------------- 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 HSSP; P22983; 1DIK. DR PFAM; PF00391; PEP-utilizers; 1. DR PFAM; PF01326; PPDK_N_term; 1. DR PROSITE; PS00370; PEP_ENZYMES_PHOS_SITE; 1. DR PROSITE; PS00742; PEP_ENZYMES_2; 1. KW Transferase; Kinase; ATP-binding; Phosphorylation. FT MOD_RES 442 442 PHOSPHORYLATION (BY SIMILARITY). FT DOMAIN 809 815 POLY-GLU. FT CONFLICT 747 747 Q -> K (IN REF. 2). SQ SEQUENCE 817 AA; 90485 MW; 6236657C CRC32; 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 HVIKVCQRYG VETSICGQAG SDPKMARILV RLGIDSISAN PDAVQLIRQV VAQEERKLML EAARKQLFEE EEEEELF //