ID   PPSA_PYRHO              Reviewed;         821 AA.
AC   O57830;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=Probable phosphoenolpyruvate synthase;
DE            Short=PEP synthase;
DE            EC=2.7.9.2;
DE   AltName: Full=Pyruvate, water dikinase;
GN   Name=ppsA; OrderedLocusNames=PH0092;
OS   Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS   100139 / OT-3).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Pyrococcus.
OX   NCBI_TaxID=70601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX   PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA   Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA   Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA   Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA   Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA   Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT   "Complete sequence and gene organization of the genome of a hyper-
RT   thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL   DNA Res. 5:55-76(1998).
CC   -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC       phosphoenolpyruvate. {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
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}.
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DR   EMBL; BA000001; BAA29161.1; -; Genomic_DNA.
DR   PIR; B71229; B71229.
DR   AlphaFoldDB; O57830; -.
DR   SMR; O57830; -.
DR   STRING; 70601.3256478; -.
DR   EnsemblBacteria; BAA29161; BAA29161; BAA29161.
DR   KEGG; pho:PH0092; -.
DR   eggNOG; arCOG01111; Archaea.
DR   OMA; RRFVQMY; -.
DR   UniPathway; UPA00138; -.
DR   Proteomes; UP000000752; 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; 3.20.20.60; -; 1.
DR   Gene3D; 3.30.1490.20; -; 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   PANTHER; PTHR43030; PTHR43030; 2.
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   3: Inferred from homology;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Transferase.
FT   CHAIN           1..821
FT                   /note="Probable phosphoenolpyruvate synthase"
FT                   /id="PRO_0000147045"
FT   ACT_SITE        444
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        759
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         543
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         590
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         687
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         687
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         709
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         710
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         711
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         712
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         712
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   821 AA;  90812 MW;  A93816D865F8A0BF CRC64;
     MDKMAYKFIK WFEELRKDDV PLVGGKGANL GEMTNAGIPV PPGFCVTAEA YKYFVENVKV
     SKEDVKKILG EKANKGTIAE VLASAPDEPR TLQEWIMDII NRTNVDDSKQ LQENTAIIRE
     LIESLEMPNE IADEIKQAYK ELSQRFGKDE IYVAVRSSAT AEDLPEASFA GQQETYLDVL
     GADDVIDKVK KCWASLWTAR ATFYRAKQGF DHSKVYLSAV VQKMVNSEKS GVMFTANPVT
     NNRNEIMINA SWGLGEAVVS GAVTPDEYIV EKGTWKIKEK VIAKKEVMVI RNPETGKGTV
     QVKVAEYLGP EWVEKQVLTD EQIIEVAKMG QKIEEHYGWP QDIEWAYDKD DGKLYIVQSR
     PITTLKETTT EEVEEVEEAE VILKGLGASP GIGAGRVVVI FDASEIDKVK EGDVLVTTMT
     NPDMVPAMKR ASAIITDEGG RTSHAAIVSR ELGIPAVVGT KEATKKLKTG DYVTVDGTRG
     LVYKGIVKSL VEKKKKEEAA AAPGAAVAAA PLVTGTLVKV NVSMPEVAER AAATGADGVG
     LLRAEHMILS IGQHPVKFIK EGKEDELVER LAEGIEKVAA AFYPRPVWYR TLDAPTNEFR
     EMPGGEDEPE ERNPMLGWRG IRRGLDQPEL LRAEFKAIKK VVEKGYNNIG VMLPLVSHPE
     QIRKAKEIAR EVGLEPHKDV AWGIMIEVPA AAIIIEDLIK EGIDFVSFGT NDLTQYTLAI
     DRDNERVAKL YDETHPAVLK LIKHVIKVCK KYGVETSICG QAGSDPKMAR ILVRLGIDSI
     SANPDAVQLI RQVVAQEERK LMLEAARKKL LEEEEEEEDL F