PPSA_AERPE
ID PPSA_AERPE Reviewed; 820 AA.
AC Q9YEC5;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
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=APE_0650.1;
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
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; BA000002; BAA79621.2; -; Genomic_DNA.
DR PIR; E72652; E72652.
DR AlphaFoldDB; Q9YEC5; -.
DR SMR; Q9YEC5; -.
DR STRING; 272557.APE_0650.1; -.
DR EnsemblBacteria; BAA79621; BAA79621; APE_0650.1.
DR KEGG; ape:APE_0650.1; -.
DR PATRIC; fig|272557.25.peg.469; -.
DR eggNOG; arCOG01111; Archaea.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000002518; 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..820
FT /note="Phosphoenolpyruvate synthase"
FT /id="PRO_0000147040"
FT ACT_SITE 438
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 762
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 539
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 587
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 689
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 689
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="substrate"
FT /evidence="ECO:0000250"
FT BINDING 713
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 713
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 820 AA; 91854 MW; 7E3B54DABCCA3851 CRC64;
MERRLILWLD EISKDLLPLV GGKAAGLGEM IKAGIPVPPG FVVTSEAYRR FVFETGIAGF
IKHILEETIV SGRPEEYEKA SELIRSKFVR TPMPPYLRRA IVDAYRKLGT LVGVEEPRVA
VRSSATVEDL PEASFAGQQE TYLNVKGEEE VVEKVKTAWA SLWTARALSY RDSLNIDHET
ALMAVVVQKM VSSRSSGVMF TIHPVTGEED KIVIESIWGL GEYIVGGKVT PDRFVVSKSD
LEILEVRISR KDKALFYDPD LNENVEIKIP ESGEELEDLR RKHPAVAEVV EKYGIRPDAP
SLSEKEVKEL ARLAIKVENH FARPMDIEWA IDFELSPPEN ILLLQARPET VWSRKKEEAE
AKPPEEEAVP EGEVLVRGVP ASPGVASGRV KVALTVEEAA KKMEKGDVLV TKMTDPDWVP
YMKMASAIVT DEGGMTAHAA IVARELGIPA VVGTGDATKK LKDGMLVTVD GSRGVVYAGA
VKTEEAREEE ARPELGAAVA EVLSEVYPVT ATKIYMNLGH PEEIDRYKHL PFEGIGLMRI
EFIISSWIGY HPMYLIEQGR GVYFIDKLAE GVAKVASAIY PRPVVVRFSD FKTNEYRRLK
GGEKYETLDE RNPMIGWRGV SRYIHPNYEP AFRLEVRAIK KVREEWGLKN VWVMFPFVRT
TWELERALKI MEEEGLSRGR DFKVWIMVEV PSTVFLADEF AKMVDGFSIG SNDLTQLVLG
VDRDSGFLAK MGYFDERDPA VLRSIEILIE KAHSQGATVS ICGQGPSVYP ELVEFLVRRG
IDSISVNPDA VVRVRRQVAS IERRIMLERL EELGSRLSRL
