PPSA_PYRFU
ID PPSA_PYRFU Reviewed; 817 AA.
AC P42850; Q59672;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2002, sequence version 3.
DT 03-AUG-2022, entry version 140.
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=PF0043;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=7828869; DOI=10.1016/0378-1119(94)90651-3;
RA Robinson K.A., Schreier H.J.;
RT "Isolation, sequence and characterization of the maltose-regulated mlrA
RT gene from the hyperthermophilic archaeum Pyrococcus furiosus.";
RL Gene 151:173-176(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=7628701; DOI=10.1016/0378-1119(95)00128-s;
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 furiosus
RT with high homology to a gene encoding phosphoenolpyruvate synthetase from
RT Escherichia coli.";
RL Gene 160:101-103(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [4]
RP PROTEIN SEQUENCE OF 2-21, FUNCTION, SUBUNIT, CATALYTIC ACTIVITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=11133966; DOI=10.1128/jb.183.2.709-715.2001;
RA Hutchins A.M., Holden J.F., Adams M.W.W.;
RT "Phosphoenolpyruvate synthetase from the hyperthermophilic archaeon
RT Pyrococcus furiosus.";
RL J. Bacteriol. 183:709-715(2001).
CC -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC phosphoenolpyruvate. {ECO:0000269|PubMed:11133966}.
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 Evidence={ECO:0000269|PubMed:11133966};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.11 mM for pyruvate {ECO:0000269|PubMed:11133966};
CC KM=0.40 mM for phosphoenolpyruvate {ECO:0000269|PubMed:11133966};
CC KM=0.39 mM for ATP {ECO:0000269|PubMed:11133966};
CC KM=1.00 mM for AMP {ECO:0000269|PubMed:11133966};
CC KM=38.4 mM for phosphate {ECO:0000269|PubMed:11133966};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- SUBUNIT: Homooctamer. {ECO:0000269|PubMed:11133966}.
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; U08376; AAA81512.1; -; Genomic_DNA.
DR EMBL; X80819; CAA56785.1; -; Genomic_DNA.
DR EMBL; AE009950; AAL80167.1; -; Genomic_DNA.
DR PIR; JC4176; JC4176.
DR RefSeq; WP_011011155.1; NC_018092.1.
DR AlphaFoldDB; P42850; -.
DR SMR; P42850; -.
DR STRING; 186497.PF0043; -.
DR EnsemblBacteria; AAL80167; AAL80167; PF0043.
DR GeneID; 41711830; -.
DR KEGG; pfu:PF0043; -.
DR PATRIC; fig|186497.12.peg.47; -.
DR eggNOG; arCOG01111; Archaea.
DR HOGENOM; CLU_007308_6_2_2; -.
DR OMA; RRFVQMY; -.
DR OrthoDB; 3139at2157; -.
DR PhylomeDB; P42850; -.
DR BioCyc; MetaCyc:MON-20544; -.
DR BRENDA; 2.7.9.2; 5243.
DR SABIO-RK; P42850; -.
DR UniPathway; UPA00138; -.
DR Proteomes; UP000001013; 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 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11133966"
FT CHAIN 2..817
FT /note="Phosphoenolpyruvate synthase"
FT /id="PRO_0000147044"
FT ACT_SITE 442
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 756
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 540
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 587
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 684
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 684
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 706
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 707
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 708
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 709
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 709
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 8
FT /note="W -> G (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 747
FT /note="K -> Q (in Ref. 1; AAA81512)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 817 AA; 90485 MW; DA3A7A3CF13C614F CRC64;
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 HVIKVCKRYG VETSICGQAG SDPKMARILV RLGIDSISAN
PDAVQLIRQV VAQEERKLML EAARKQLFEE EEEEELF
