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O67899 (PPSA_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 78. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:aq_2142
OrganismAquifex aeolicus (strain VF5)
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length856 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 – 856856Phosphoenolpyruvate synthase
PRO_0000147032

Sites

Active site4331Tele-phosphohistidine intermediate By similarity
Active site8091Proton donor By similarity
Metal binding7381Magnesium By similarity
Metal binding7621Magnesium By similarity
Binding site5231Substrate By similarity
Binding site6361Substrate By similarity
Binding site7381Substrate By similarity
Binding site7591Substrate; via carbonyl oxygen By similarity
Binding site7601Substrate; via amide nitrogen By similarity
Binding site7611Substrate By similarity
Binding site7621Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
O67899 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 0CB001DABE289912

FASTA85696,407
        10         20         30         40         50         60 
MSVDKSKALV LWLDEVTIED IPIAGGKNAS LGEMIRNLSP LGVKIPYGYV VTANAYYYFL 

        70         80         90        100        110        120 
DYNNLRDKIR KILEGLNTDD LKDLQRRGHE VRELIRGGTF PPDLEEAIKD YYNKLSEKYK 

       130        140        150        160        170        180 
THAVDVAVRS SATAEDLPDA SFAGQQETYL NVVGAENVLV AIKNCFASLF TDRAIVYRER 

       190        200        210        220        230        240 
FGFDHFKVGI AVGVQKMVRS DMGASGVMFT LDTETGFKDV VVINAAYGLG ELLVRGEVTP 

       250        260        270        280        290        300 
DEYIVFKPTL MKGYSAIIEK KLGRKDRKMI YGTGDERVKI VNVPKEDQKK FALNDDEILQ 

       310        320        330        340        350        360 
LAKWGVLIEE HYSKKNGRWT PMDIEWAKDG ILNELFVVQA RPETVHSRKK ENVVKIYKIK 

       370        380        390        400        410        420 
TPEEERKNRV IVKGIAVGDK IATGKARVLF DLKEADQFQE GEILVTDITD PDWEPVMKKA 

       430        440        450        460        470        480 
AAIVTNRGGR TSHAAIVARE LGIPAVVGTG NATEKIKTGE EITVSCAEGE TGYVYEGKID 

       490        500        510        520        530        540 
YEVEEINLEN IPKPKTKIMM NIGNPESAFR YASLPNDGVG LAREEFIIAN YIKIHPLALL 

       550        560        570        580        590        600 
HYEDLKELYE KLERENLIDE KGFVQFKLIY HYANGRLANK LAKGKDKLRV NLRKILQDIE 

       610        620        630        640        650        660 
NLTFGYEDKA TYYIKKLSYG IAKIAAAFYP NPVIVRFSDF KSNEYANLIG GILFEPEEEN 

       670        680        690        700        710        720 
PMLGWRGASR YYSDVFKEAF GMECKAIIRV RNKMGLTNTK VMIPFCRTPE EGEKVLQVME 

       730        740        750        760        770        780 
EYGLRKGENG LEVYVMAELP SNIVLADRYA QIFDGFSIGS NDLTQLTLGL DRDSELVAHL 

       790        800        810        820        830        840 
YDERNEAVKR LIAQLIKTAK EYGRKVGICG QAPSDFPEFA QFLVEQGIDS ISLNPDSVLK 

       850 
TMLAVVEMEK KLGVLK 

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References

[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed: 9537320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: VF5.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC07865.1.
PIRG70483.
RefSeqNP_214468.1. NC_000918.1.

3D structure databases

ProteinModelPortalO67899.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1193888.
GenomeReviewsGene locus aq_2142 in contig AE000657_GR.
KEGGaae:aq_2142.
NMPDRfig|224324.1.peg.1483.
PATRIC20961126. VBIAquAeo85532_1656.

Phylogenomic databases

HOGENOMHBG284863.
OMAINNHIKA.
PhylomeDBO67899.
ProtClustDBPRK06464.

Enzyme and pathway databases

BioCycAAEO224324:AQ_2142-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.
IPR006318. PEP_util_enz.
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. 2 hits.
KOK01007.
PfamPF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
PF01326. PPDK_N. 1 hit.
[Graphical view]
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_AQUAE
AccessionPrimary (citable) accession number: O67899
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: August 1, 1998
Last modified: January 25, 2012
This is version 78 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