Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q9ZMV4 (PPSA_HELPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·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
Ordered Locus Names:jhp_0111
OrganismHelicobacter pylori (strain J99) (Campylobacter pylori J99) [Complete proteome] [HAMAP]
Taxonomic identifier85963 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter ›

Protein attributes

Sequence length812 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the phosphorylation of pyruvate to phosphoenolpyruvate By similarity.

Catalytic activity

ATP + pyruvate + H2O = AMP + phosphoenolpyruvate + phosphate.

Cofactor

Magnesium By similarity.

Pathway

Carbohydrate biosynthesis; gluconeogenesis.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 812812Phosphoenolpyruvate synthase
PRO_0000147037

Sites

Active site4301Tele-phosphohistidine intermediate By similarity
Active site7611Proton donor By similarity
Metal binding6901Magnesium By similarity
Metal binding7141Magnesium By similarity
Binding site5201Substrate By similarity
Binding site5881Substrate By similarity
Binding site6901Substrate By similarity
Binding site7111Substrate; via carbonyl oxygen By similarity
Binding site7121Substrate; via amide nitrogen By similarity
Binding site7131Substrate By similarity
Binding site7141Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZMV4 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: A088D459B3E47512

FASTA81291,291
        10         20         30         40         50         60 
MRYIKFFKEL NNKNVNLVGG KNASIGEMFQ ELVPIGIKVP DGFAITSEAY WYLLEQGGAK 

        70         80         90        100        110        120 
QKIIELLENV DATEIDVLKI RSKQIRELIF GTPFPSDLRD EIFQAYEILS QQYHMKEADV 

       130        140        150        160        170        180 
AVRSSATAED LPDASFAGQQ DTYLNIKGKT ELIHYIKSCL ASLFTDRAIS YRASRGFDHL 

       190        200        210        220        230        240 
KVALSVGVQK MVRADKGSAG VMFSIDTETG FKDAVFITSA WGLGENVVGG TINPDEFYVF 

       250        260        270        280        290        300 
KPTLEQNKRP IIKRQLGNKT QKMVYAPRGS EHPTRNIKTT KKEWQSFSLS DEDVLILAKY 

       310        320        330        340        350        360 
AIEIEKHYSK EAKQYRPMDI EWAKDGESGE IFIVQARPET VQSQKTKEEN QVFEKFKFKN 

       370        380        390        400        410        420 
PNEKKEIILQ GRAIGSKIGS GKVRIINDLE HMNSFKEGEI LVTDNTDPDW EPCMKKASAV 

       430        440        450        460        470        480 
ITNRGGRTCH AAIVAREIGV PAIVGVSGAT DSLYTGMEIT VSCAEGEEGY VYAGIYEHEI 

       490        500        510        520        530        540 
ERVELSNMQE TQTKIYINIG NPEKAFSFSQ LPNHGVGLAR MEMIILNQIK AHPLALVDLH 

       550        560        570        580        590        600 
HKKSVKEKNE IENLMAGYAN PKDFFVKKIA EGIGMISAAF YPKPVIVRTS DFKSNEYMRM 

       610        620        630        640        650        660 
LGGSSYEPNE ENPMLGYRGA SRYYSESYNE AFSWECEALA LVREEMGLTN MKVMIPFLRT 

       670        680        690        700        710        720 
IEEGKKVLEI LRKNNLESGK NGLEIYIMCE LPVNVILADD FLSLFDGFSI GSNDLTQLTL 

       730        740        750        760        770        780 
GVDRDSELVS HVFDERNEAM LKMFKKAIEA CKRHNKYCGI CGQAPSDYPE VTEFLVKEGI 

       790        800        810 
TSISLNPDSV IPTWNAVAKL EKELKDHGLT AR

« Hide

References

[1]"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori."
Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. expand/collapse author list , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.
Nature 397:176-180(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE001439 Genomic DNA. Translation: AAD05690.1.
PIRE71972.
RefSeqNP_222832.1. NC_000921.1.

3D structure databases

ProteinModelPortalQ9ZMV4.
ModBaseSearch...

Protein-protein interaction databases

STRING85963.jhp0111.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD05690; AAD05690; jhp_0111.
GeneID889485.
KEGGhpj:jhp0111.
PATRIC20604828. VBIHelPyl98156_0126.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0574.
KOK01007.
OMANVMERYL.
ProtClustDBPRK06464.

Enzyme and pathway databases

BioCycHPYL85963:GJB9-118-MONOMER.
UniPathwayUPA00138.

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.
IPR006318. PEP_util_enz.
IPR002192. PPDK_PEP-bd.
IPR015813. Pyrv/PenolPyrv_Kinase.
[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.
PRINTSPR01736. PHPHTRNFRASE.
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_HELPJ
AccessionPrimary (citable) accession number: Q9ZMV4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: May 1, 2013
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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