PPSA_ECOLI
ID PPSA_ECOLI Reviewed; 792 AA.
AC P23538;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 5.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Phosphoenolpyruvate synthase;
DE Short=PEP synthase;
DE EC=2.7.9.2;
DE AltName: Full=Pyruvate, water dikinase;
GN Name=ppsA; Synonyms=pps; OrderedLocusNames=b1702, JW1692;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Holzschu D.L., McElver J.A., Liao C.C., Berry A.;
RT "The cloning and sequence of the E. coli pps gene.";
RL Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-21.
RC STRAIN=K12;
RX PubMed=1310524; DOI=10.1007/bf00279808;
RA Niersbach M., Kreuzaler F., Geerse R.H., Postma P.W., Hirsch H.J.;
RT "Cloning and nucleotide sequence of the Escherichia coli K-12 ppsA gene,
RT encoding PEP synthase.";
RL Mol. Gen. Genet. 231:332-336(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP CATALYTIC ACTIVITY.
RX PubMed=4293109; DOI=10.1016/0304-4165(67)90269-3;
RA Cooper R.A., Kornberg H.L.;
RT "The mechanism of the phosphoenolpyruvate synthase reaction.";
RL Biochim. Biophys. Acta 141:211-213(1967).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=4319237; DOI=10.1016/s0021-9258(18)62756-5;
RA Berman K.M., Cohn M.;
RT "Phosphoenolpyruvate synthetase of Escherichia coli. Purification, some
RT properties, and the role of divalent metal ions.";
RL J. Biol. Chem. 245:5309-5318(1970).
RN [8]
RP PHOSPHOINTERMEDIATE OF REACTION, SUBUNIT, AND AMINO-ACID COMPOSITION.
RX PubMed=16880; DOI=10.1016/s0021-9258(17)40359-0;
RA Narindrasorasak S., Bridger W.A.;
RT "Phosphoenolypyruvate synthetase of Escherichia coli: molecular weight,
RT subunit composition, and identification of phosphohistidine in
RT phosphoenzyme intermediate.";
RL J. Biol. Chem. 252:3121-3127(1977).
RN [9]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [10]
RP ACTIVITY REGULATION.
RX PubMed=20044937; DOI=10.1186/1471-2091-11-1;
RA Burnell J.N.;
RT "Cloning and characterization of Escherichia coli DUF299: a bifunctional
RT ADP-dependent kinase--Pi-dependent pyrophosphorylase from bacteria.";
RL BMC Biochem. 11:1-1(2010).
CC -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to
CC phosphoenolpyruvate. {ECO:0000269|PubMed:4319237}.
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:4293109, ECO:0000269|PubMed:4319237};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:4319237};
CC -!- ACTIVITY REGULATION: Activated by a Pi-dependent pyrophosphorylation
CC and inactivated by an ADP-dependent phosphorylation on a regulatory
CC threonine. Both reactions are mediated by the bifunctional
CC serine/threonine kinase and phosphorylase PpsR.
CC {ECO:0000269|PubMed:20044937}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.083 mM for pyruvate {ECO:0000269|PubMed:4319237};
CC KM=0.028 mM for ATP {ECO:0000269|PubMed:4319237};
CC KM=10.4 mM for phosphate {ECO:0000269|PubMed:4319237};
CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16880}.
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; M69116; AAA24319.1; -; Genomic_DNA.
DR EMBL; X59381; CAA42024.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74772.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15471.1; -; Genomic_DNA.
DR PIR; S20554; S20554.
DR RefSeq; NP_416217.1; NC_000913.3.
DR RefSeq; WP_000069375.1; NZ_SSZK01000001.1.
DR AlphaFoldDB; P23538; -.
DR SMR; P23538; -.
DR BioGRID; 4262084; 9.
DR DIP; DIP-10552N; -.
DR IntAct; P23538; 10.
DR STRING; 511145.b1702; -.
DR SWISS-2DPAGE; P23538; -.
DR jPOST; P23538; -.
DR PaxDb; P23538; -.
DR PRIDE; P23538; -.
DR EnsemblBacteria; AAC74772; AAC74772; b1702.
DR EnsemblBacteria; BAA15471; BAA15471; BAA15471.
DR GeneID; 66674404; -.
DR GeneID; 946209; -.
DR KEGG; ecj:JW1692; -.
DR KEGG; eco:b1702; -.
DR PATRIC; fig|1411691.4.peg.555; -.
DR EchoBASE; EB0752; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG1080; Bacteria.
DR HOGENOM; CLU_007308_6_2_6; -.
DR InParanoid; P23538; -.
DR OMA; RRFVQMY; -.
DR PhylomeDB; P23538; -.
DR BioCyc; EcoCyc:PEPSYNTH-MON; -.
DR BioCyc; MetaCyc:PEPSYNTH-MON; -.
DR BRENDA; 2.7.9.2; 2026.
DR SABIO-RK; P23538; -.
DR UniPathway; UPA00138; -.
DR PRO; PR:P23538; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IDA:EcoCyc.
DR GO; GO:0008986; F:pyruvate, water dikinase activity; IDA:EcoCyc.
DR GO; GO:0006094; P:gluconeogenesis; IMP:EcoCyc.
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:1310524"
FT CHAIN 2..792
FT /note="Phosphoenolpyruvate synthase"
FT /id="PRO_0000147034"
FT ACT_SITE 421
FT /note="Tele-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT ACT_SITE 751
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 511
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 578
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 680
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 680
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 701
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 702
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 703
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 704
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 704
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT CONFLICT 194..195
FT /note="RM -> AGL (in Ref. 1; AAA24319)"
FT /evidence="ECO:0000305"
FT CONFLICT 341..360
FT /note="RSRGQVMERYTLHSQGKIIA -> AHAVRSWSVIRCIHRVRLSP (in
FT Ref. 1; AAA24319)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 792 AA; 87435 MW; DBBAB0BA9B9F7DD9 CRC64;
MSNNGSSPLV LWYNQLGMND VDRVGGKNAS LGEMITNLSG MGVSVPNGFA TTADAFNQFL
DQSGVNQRIY ELLDKTDIDD VTQLAKAGAQ IRQWIIDTPF QPELENAIRE AYAQLSADDE
NASFAVRSSA TAEDMPDASF AGQQETFLNV QGFDAVLVAV KHVFASLFND RAISYRVHQG
YDHRGVALSA GVQRMVRSDL ASSGVMFSID TESGFDQVVF ITSAWGLGEM VVQGAVNPDE
FYVHKPTLAA NRPAIVRRTM GSKKIRMVYA PTQEHGKQVK IEDVPQEQRD IFSLTNEEVQ
ELAKQAVQIE KHYGRPMDIE WAKDGHTGKL FIVQARPETV RSRGQVMERY TLHSQGKIIA
EGRAIGHRIG AGPVKVIHDI SEMNRIEPGD VLVTDMTDPD WEPIMKKASA IVTNRGGRTC
HAAIIARELG IPAVVGCGDA TERMKDGENV TVSCAEGDTG YVYAELLEFS VKSSSVETMP
DLPLKVMMNV GNPDRAFDFA CLPNEGVGLA RLEFIINRMI GVHPRALLEF DDQEPQLQNE
IREMMKGFDS PREFYVGRLT EGIATLGAAF YPKRVIVRLS DFKSNEYANL VGGERYEPDE
ENPMLGFRGA GRYVSDSFRD CFALECEAVK RVRNDMGLTN VEIMIPFVRT VDQAKAVVEE
LARQGLKRGE NGLKIIMMCE IPSNALLAEQ FLEYFDGFSI GSNDMTQLAL GLDRDSGVVS
ELFDERNDAV KALLSMAIRA AKKQGKYVGI CGQGPSDHED FAAWLMEEGI DSLSLNPDTV
VQTWLSLAEL KK
