PPSA_AQUAE
ID PPSA_AQUAE Reviewed; 856 AA.
AC O67899;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=aq_2142;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(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; AE000657; AAC07865.1; -; Genomic_DNA.
DR PIR; G70483; G70483.
DR RefSeq; NP_214468.1; NC_000918.1.
DR RefSeq; WP_010881404.1; NC_000918.1.
DR AlphaFoldDB; O67899; -.
DR SMR; O67899; -.
DR STRING; 224324.aq_2142; -.
DR PRIDE; O67899; -.
DR EnsemblBacteria; AAC07865; AAC07865; aq_2142.
DR KEGG; aae:aq_2142; -.
DR PATRIC; fig|224324.8.peg.1656; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_007308_6_2_0; -.
DR InParanoid; O67899; -.
DR OMA; LETWFFL; -.
DR OrthoDB; 997616at2; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000000798; 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; 1.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF02896; PEP-utilizers_C; 1.
DR Pfam; PF01326; PPDK_N; 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 Reference proteome; Transferase.
FT CHAIN 1..856
FT /note="Phosphoenolpyruvate synthase"
FT /id="PRO_0000147032"
FT ACT_SITE 433
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 809
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 523
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 636
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 738
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 738
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 759
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 760
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 761
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 762
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 762
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 856 AA; 96407 MW; 0CB001DABE289912 CRC64;
MSVDKSKALV LWLDEVTIED IPIAGGKNAS LGEMIRNLSP LGVKIPYGYV VTANAYYYFL
DYNNLRDKIR KILEGLNTDD LKDLQRRGHE VRELIRGGTF PPDLEEAIKD YYNKLSEKYK
THAVDVAVRS SATAEDLPDA SFAGQQETYL NVVGAENVLV AIKNCFASLF TDRAIVYRER
FGFDHFKVGI AVGVQKMVRS DMGASGVMFT LDTETGFKDV VVINAAYGLG ELLVRGEVTP
DEYIVFKPTL MKGYSAIIEK KLGRKDRKMI YGTGDERVKI VNVPKEDQKK FALNDDEILQ
LAKWGVLIEE HYSKKNGRWT PMDIEWAKDG ILNELFVVQA RPETVHSRKK ENVVKIYKIK
TPEEERKNRV IVKGIAVGDK IATGKARVLF DLKEADQFQE GEILVTDITD PDWEPVMKKA
AAIVTNRGGR TSHAAIVARE LGIPAVVGTG NATEKIKTGE EITVSCAEGE TGYVYEGKID
YEVEEINLEN IPKPKTKIMM NIGNPESAFR YASLPNDGVG LAREEFIIAN YIKIHPLALL
HYEDLKELYE KLERENLIDE KGFVQFKLIY HYANGRLANK LAKGKDKLRV NLRKILQDIE
NLTFGYEDKA TYYIKKLSYG IAKIAAAFYP NPVIVRFSDF KSNEYANLIG GILFEPEEEN
PMLGWRGASR YYSDVFKEAF GMECKAIIRV RNKMGLTNTK VMIPFCRTPE EGEKVLQVME
EYGLRKGENG LEVYVMAELP SNIVLADRYA QIFDGFSIGS NDLTQLTLGL DRDSELVAHL
YDERNEAVKR LIAQLIKTAK EYGRKVGICG QAPSDFPEFA QFLVEQGIDS ISLNPDSVLK
TMLAVVEMEK KLGVLK
