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P23538 (PPSA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoenolpyruvate synthase
Short name=PEP synthase
EC=2.7.9.2
Alternative name(s):
Pyruvate, water dikinase
Gene names
Name:ppsA
Synonyms:pps
Ordered Locus Names:b1702, JW1692
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length792 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate. Ref.7

Catalytic activity

ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate. Ref.6 Ref.7

Cofactor

Magnesium. Ref.7

Enzyme regulation

Activated by a Pi-dependent pyrophosphorylation and inactivated by an ADP-dependent phosphorylation on a regulatory threonine. Both reactions are mediated by the bifunctional serine/threonine kinase and phosphorylase PpsR. Ref.10

Pathway

Carbohydrate biosynthesis; gluconeogenesis.

Subunit structure

Homodimer. Ref.8

Domain

The N-terminal domain contains the ATP/Pi binding site, the central domain the pyrophosphate/phosphate carrier histidine, and the C-terminal domain the pyruvate binding site By similarity.

Miscellaneous

The reaction takes place in three steps, mediated by a phosphocarrier histidine residue located on the surface of the central domain. The two first partial reactions are catalyzed at an active site located on the N-terminal domain, and the third partial reaction is catalyzed at an active site located on the C-terminal domain. For catalytic turnover, the central domain swivels from the concave surface of the N-terminal domain to that of the C-terminal domain By similarity.

Sequence similarities

Belongs to the PEP-utilizing enzyme family.

Biophysicochemical properties

Kinetic parameters:

KM=0.083 mM for pyruvate Ref.7

KM=0.028 mM for ATP

KM=10.4 mM for phosphate

Binary interactions

With

Entry

#Exp.

IntAct

Notes

rplBP604221EBI-1114517,EBI-543515

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 792791Phosphoenolpyruvate synthase
PRO_0000147034

Sites

Active site4211Tele-phosphohistidine intermediate By similarity
Active site7511Proton donor By similarity
Metal binding6801Magnesium By similarity
Metal binding7041Magnesium By similarity
Binding site5111Substrate By similarity
Binding site5781Substrate By similarity
Binding site6801Substrate By similarity
Binding site7011Substrate; via carbonyl oxygen By similarity
Binding site7021Substrate; via amide nitrogen By similarity
Binding site7031Substrate By similarity
Binding site7041Substrate; via amide nitrogen By similarity

Experimental info

Sequence conflict194 – 1952RM → AGL in AAA24319. Ref.1
Sequence conflict341 – 36020RSRGQ…GKIIA → AHAVRSWSVIRCIHRVRLSP in AAA24319. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P23538 [UniParc].

Last modified January 23, 2007. Version 5.
Checksum: DBBAB0BA9B9F7DD9

FASTA79287,435
        10         20         30         40         50         60 
MSNNGSSPLV LWYNQLGMND VDRVGGKNAS LGEMITNLSG MGVSVPNGFA TTADAFNQFL 

        70         80         90        100        110        120 
DQSGVNQRIY ELLDKTDIDD VTQLAKAGAQ IRQWIIDTPF QPELENAIRE AYAQLSADDE 

       130        140        150        160        170        180 
NASFAVRSSA TAEDMPDASF AGQQETFLNV QGFDAVLVAV KHVFASLFND RAISYRVHQG 

       190        200        210        220        230        240 
YDHRGVALSA GVQRMVRSDL ASSGVMFSID TESGFDQVVF ITSAWGLGEM VVQGAVNPDE 

       250        260        270        280        290        300 
FYVHKPTLAA NRPAIVRRTM GSKKIRMVYA PTQEHGKQVK IEDVPQEQRD IFSLTNEEVQ 

       310        320        330        340        350        360 
ELAKQAVQIE KHYGRPMDIE WAKDGHTGKL FIVQARPETV RSRGQVMERY TLHSQGKIIA 

       370        380        390        400        410        420 
EGRAIGHRIG AGPVKVIHDI SEMNRIEPGD VLVTDMTDPD WEPIMKKASA IVTNRGGRTC 

       430        440        450        460        470        480 
HAAIIARELG IPAVVGCGDA TERMKDGENV TVSCAEGDTG YVYAELLEFS VKSSSVETMP 

       490        500        510        520        530        540 
DLPLKVMMNV GNPDRAFDFA CLPNEGVGLA RLEFIINRMI GVHPRALLEF DDQEPQLQNE 

       550        560        570        580        590        600 
IREMMKGFDS PREFYVGRLT EGIATLGAAF YPKRVIVRLS DFKSNEYANL VGGERYEPDE 

       610        620        630        640        650        660 
ENPMLGFRGA GRYVSDSFRD CFALECEAVK RVRNDMGLTN VEIMIPFVRT VDQAKAVVEE 

       670        680        690        700        710        720 
LARQGLKRGE NGLKIIMMCE IPSNALLAEQ FLEYFDGFSI GSNDMTQLAL GLDRDSGVVS 

       730        740        750        760        770        780 
ELFDERNDAV KALLSMAIRA AKKQGKYVGI CGQGPSDHED FAAWLMEEGI DSLSLNPDTV 

       790 
VQTWLSLAEL KK

« Hide

References

« Hide 'large scale' references
[1]"The cloning and sequence of the E. coli pps gene."
Holzschu D.L., McElver J.A., Liao C.C., Berry A.
Submitted (JUN-1991) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Cloning and nucleotide sequence of the Escherichia coli K-12 ppsA gene, encoding PEP synthase."
Niersbach M., Kreuzaler F., Geerse R.H., Postma P.W., Hirsch H.J.
Mol. Gen. Genet. 231:332-336(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-21.
Strain: K12.
[3]"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map."
Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. expand/collapse author list , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T.
DNA Res. 3:363-377(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[5]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"The mechanism of the phosphoenolpyruvate synthase reaction."
Cooper R.A., Kornberg H.L.
Biochim. Biophys. Acta 141:211-213(1967) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY.
[7]"Phosphoenolpyruvate synthetase of Escherichia coli. Purification, some properties, and the role of divalent metal ions."
Berman K.M., Cohn M.
J. Biol. Chem. 245:5309-5318(1970) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
[8]"Phosphoenolypyruvate synthetase of Escherichia coli: molecular weight, subunit composition, and identification of phosphohistidine in phosphoenzyme intermediate."
Narindrasorasak S., Bridger W.A.
J. Biol. Chem. 252:3121-3127(1977) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHOINTERMEDIATE OF REACTION, SUBUNIT, AMINO-ACID COMPOSITION.
[9]"Escherichia coli proteome analysis using the gene-protein database."
VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY 2D-GEL.
[10]"Cloning and characterization of Escherichia coli DUF299: a bifunctional ADP-dependent kinase--Pi-dependent pyrophosphorylase from bacteria."
Burnell J.N.
BMC Biochem. 11:1-1(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M69116 Genomic DNA. Translation: AAA24319.1.
X59381 Genomic DNA. Translation: CAA42024.1.
U00096 Genomic DNA. Translation: AAC74772.1.
AP009048 Genomic DNA. Translation: BAA15471.1.
PIRS20554.
RefSeqNP_416217.1. NC_000913.2.
YP_489964.1. NC_007779.1.

3D structure databases

ProteinModelPortalP23538.
SMRP23538. Positions 10-788.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-10552N.
IntActP23538. 6 interactions.
STRING511145.b1702.

PTM databases

PhosSiteP0810424.

2D gel databases

SWISS-2DPAGEP23538.

Proteomic databases

PaxDbP23538.
PRIDEP23538.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC74772; AAC74772; b1702.
BAA15471; BAA15471; BAA15471.
GeneID12933090.
946209.
KEGGecj:Y75_p1677.
eco:b1702.
PATRIC32118710. VBIEscCol129921_1773.

Organism-specific databases

EchoBASEEB0752.
EcoGeneEG10759. pps.

Phylogenomic databases

eggNOGCOG0574.
HOGENOMHOG000230913.
KOK01007.
OMANVMERYL.
ProtClustDBPRK06464.

Enzyme and pathway databases

BioCycEcoCyc:PEPSYNTH-MONOMER.
ECOL316407:JW1692-MONOMER.
MetaCyc:PEPSYNTH-MONOMER.
BRENDA2.7.9.2. 2026.
SABIO-RKP23538.
UniPathwayUPA00138.

Gene expression databases

GenevestigatorP23538.

Family and domain databases

Gene3D3.20.20.60. 1 hit.
3.30.1490.20. 1 hit.
3.30.470.20. 1 hit.
InterProIPR013815. ATP_grasp_subdomain_1.
IPR013816. ATP_grasp_subdomain_2.
IPR008279. PEP-util_enz_mobile_dom.
IPR006319. PEP_synth.
IPR018274. PEP_util_AS.
IPR000121. PEP_util_C.
IPR023151. PEP_util_CS.
IPR002192. PPDK_PEP-bd.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
[Graphical view]
PfamPF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
PF01326. PPDK_N. 1 hit.
[Graphical view]
PIRSFPIRSF000854. PEP_synthase. 1 hit.
SUPFAMSSF52009. PEP_mobile. 1 hit.
SSF51621. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
TIGRFAMsTIGR01418. PEP_synth. 1 hit.
PROSITEPS00742. PEP_ENZYMES_2. 1 hit.
PS00370. PEP_ENZYMES_PHOS_SITE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePPSA_ECOLI
AccessionPrimary (citable) accession number: P23538
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: January 23, 2007
Last modified: May 29, 2013
This is version 117 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents