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Q9K0I2 (PPSA_NEIMB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:NMB0618
OrganismNeisseria meningitidis serogroup B
Taxonomic identifier491 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Neisseria

Protein attributes

Sequence length794 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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

Present in outer membrane vesicle formulations which are used as vaccines in human.

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 – 794794Phosphoenolpyruvate synthase
PRO_0000320270

Sites

Active site4221Tele-phosphohistidine intermediate By similarity
Active site7521Proton donor By similarity
Metal binding6811Magnesium By similarity
Metal binding7051Magnesium By similarity
Binding site5121Substrate By similarity
Binding site5791Substrate By similarity
Binding site6811Substrate By similarity
Binding site7021Substrate; via carbonyl oxygen By similarity
Binding site7031Substrate; via amide nitrogen By similarity
Binding site7041Substrate By similarity
Binding site7051Substrate; via amide nitrogen By similarity

Secondary structure

1 ...................................................................................................................................... 794
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9K0I2 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 2165BDF3CFA67E56

FASTA79487,170
        10         20         30         40         50         60 
MADNYVIWFE NLRMTDVERV GGKNASLGEM ISQLTEKGVR VPGGFATTAE AYRAFLAHNG 

        70         80         90        100        110        120 
LSERISAALA KLDVEDVAEL ARVGKEIRQW ILDTPFPEQL DAEIEAAWNK MVADAGGADI 

       130        140        150        160        170        180 
SVAVRSSATA EDLPDASFAG QQETFLNING LDNVKEAMHH VFASLYNDRA ISYRVHKGFE 

       190        200        210        220        230        240 
HDIVALSAGV QRMVRSDSGA SGVMFTLDTE SGYDQVVFVT SSYGLGENVV QGAVNPDEFY 

       250        260        270        280        290        300 
VFKPTLKAGK PAILRKTMGS KHIKMIFTDK AEAGKSVTNV DVPEEDRNRF SITDEEITEL 

       310        320        330        340        350        360 
AHYALTIEKH YGRPMDIEWG RDGLDGKLYI LQARPETVKS QEEGNRNLRR FAINGDKTVL 

       370        380        390        400        410        420 
CEGRAIGQKV GQGKVRLIKD ASEMDSVEAG DVLVTDMTDP DWEPVMKRAS AIVTNRGGRT 

       430        440        450        460        470        480 
CHAAIIAREL GIPAVVGCGN ATELLKNGQE VTVSCAEGDT GFIYAGLLDV QITDVALDNM 

       490        500        510        520        530        540 
PKAPVKVMMN VGNPELAFSF ANLPSEGIGL ARMEFIINRQ IGIHPKALLE FDKQDDELKA 

       550        560        570        580        590        600 
EITRRIAGYA SPVDFYVDKI AEGVATLAAS VYPRKTIVRM SDFKSNEYAN LVGGNVYEPH 

       610        620        630        640        650        660 
EENPMLGFRG AARYVADNFK DCFALECKAL KRVRDEMGLT NVEIMIPFVR TLGEAEAVVK 

       670        680        690        700        710        720 
ALKENGLERG KNGLRLIMMC ELPSNAVLAE QFLQYFDGFS IGSNDMTQLT LGLDRDSGLV 

       730        740        750        760        770        780 
SESFDERNPA VKVMLHLAIS ACRKQNKYVG ICGQGPSDHP DFAKWLVEEG IESVSLNPDT 

       790 
VIETWLYLAN ELNK

« Hide

References

[1]"Complete genome sequence of Neisseria meningitidis serogroup B strain MC58."
Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E., Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C., Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H., Salzberg S.L., White O. expand/collapse author list , Fleischmann R.D., Dougherty B.A., Mason T.M., Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D., Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V., Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M., Moxon E.R., Rappuoli R., Venter J.C.
Science 287:1809-1815(2000) [PubMed: 10710307] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MC58 / Serogroup B.
[2]"Characterization of the protein content of a meningococcal outer membrane vesicle vaccine by polyacrylamide gel electrophoresis and mass spectrometry."
Vipond C., Wheeler J.X., Jones C., Feavers I.M., Suker J.
Hum. Vaccin. 1:80-84(2005) [PubMed: 17038831] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE002098 Genomic DNA. Translation: AAF41044.1.
PIRG81177.
RefSeqNP_273662.1. NC_003112.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2OLSX-ray2.40A1-794[»]
ProteinModelPortalQ9K0I2.
SMRQ9K0I2. Positions 4-792.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBNEIT00000009330; EBNEIP00000008950; EBNEIG00000009330.
GeneID902731.
GenomeReviewsGene locus NMB0618 in contig AE002098_GR.
KEGGnme:NMB0618.
NMPDRfig|122586.1.peg.596.
PATRIC20356525. VBINeiMen85645_0782.
TIGRNMB0618.

Phylogenomic databases

GeneTreeEBGT00050000020666.
HOGENOMHBG284863.
OMAKNVEIMI.
ProtClustDBPRK06464.

Enzyme and pathway databases

BioCycNMEN122586:NMB_0618-MONOMER.

Family and domain databases

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.
[Graphical view]
Gene3DG3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit.
G3DSA:3.30.470.20. ATP_grasp_subdomain_2. 1 hit.
G3DSA:3.50.30.10. PEP_mobile. 1 hit.
G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
KOK01007.
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_NEIMB
AccessionPrimary (citable) accession number: Q9K0I2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 1, 2000
Last modified: January 25, 2012
This is version 67 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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