PPSA_ARCFU
ID PPSA_ARCFU Reviewed; 753 AA.
AC O29548;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
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=AF_0710;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
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; AE000782; AAB90532.1; -; Genomic_DNA.
DR PIR; F69338; F69338.
DR RefSeq; WP_010878213.1; NC_000917.1.
DR AlphaFoldDB; O29548; -.
DR SMR; O29548; -.
DR STRING; 224325.AF_0710; -.
DR PRIDE; O29548; -.
DR EnsemblBacteria; AAB90532; AAB90532; AF_0710.
DR GeneID; 24794310; -.
DR KEGG; afu:AF_0710; -.
DR eggNOG; arCOG01111; Archaea.
DR HOGENOM; CLU_007308_6_2_2; -.
DR OMA; RRFVQMY; -.
DR OrthoDB; 3139at2157; -.
DR PhylomeDB; O29548; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002199; 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 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 Reference proteome; Transferase.
FT CHAIN 1..753
FT /note="Probable phosphoenolpyruvate synthase"
FT /id="PRO_0000147041"
FT ACT_SITE 398
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 703
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 488
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 535
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 631
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 631
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 653
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 654
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 655
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 656
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 656
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 753 AA; 83868 MW; 3D087F950321A83B CRC64;
MPVLWLADVD KNDIPLVGGK GANLGELLRA EIPVPDGFVV DARTFREFIQ KTGIAEKIYS
LLRELDVEDT EKLDAVSREI REIIEKTEMP EDIEREIREA YRKLCEEEGK EVYVAVRSSA
TAEDLPDASF AGQQETYLNV VGEDEVVEKV KKCWGSLFTP RAIYYRVQKG FRHEDVSIAV
VVQKMVNSEK SGVMFTSHPV SGEKKCIIEA VFGLGEAIVS GLVTPDTYVY DRVKRKIEEV
KIGEKKFMLT RKDGKTVKVE LPPEKANERV LSDEEIEKLV TLGELIEDHY GKPQDVEWAI
EGGKIYIVQS RPITTIRKEK KEAEEEVSEE AEGKILLKGL GASPGIASGK VKVIFSEKEI
SKVEEGDILV TTMTTPDMVP AMKRAAAIVT DEGGMTCHAA IVSRELGVPA VVGTKVATKV
LKDGMVVTVD GEKGIVYEGR IEKKEEPKPV VASAPIITAT EVKVNISIPD VAERVARETN
ADGVGLFRIE HMVLGLEKHP MKFIRDGEID RYIDLLYQEM KKVVKAFYPK PVWIRTIDAP
TDEFRAMEGG EDEPIEANPM LGFRGIRRDL AEEEHFRAEM RAIKKLVDEG YTNVGVMLPL
ITSPEEVKRA KEIAISEGLP LDKIEFGVMV ETPAAALILE DIIKEGIDFV SLGTNDLTQY
TLAVDRNNEN VAYLYNETHP AVLKLIERTI KVCKEHGVKS SICGQAGSYP HVVEKLVEFG
IDSVSANPDA VQRIREVVAR AEKRIILEKL RKI
