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Q9YEC5 (PPSA_AERPE) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 75. 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:APE_0650.1
OrganismAeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1) [Complete proteome] [HAMAP]
Taxonomic identifier272557 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeAeropyrum

Protein attributes

Sequence length820 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 – 820820Phosphoenolpyruvate synthase
PRO_0000147040

Sites

Active site4381Tele-phosphohistidine intermediate By similarity
Active site7621Proton donor By similarity
Metal binding6891Magnesium By similarity
Metal binding7131Magnesium By similarity
Binding site5391Substrate By similarity
Binding site5871Substrate By similarity
Binding site6891Substrate By similarity
Binding site7101Substrate; via carbonyl oxygen By similarity
Binding site7111Substrate; via amide nitrogen By similarity
Binding site7121Substrate By similarity
Binding site7131Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9YEC5 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: 7E3B54DABCCA3851

FASTA82091,854
        10         20         30         40         50         60 
MERRLILWLD EISKDLLPLV GGKAAGLGEM IKAGIPVPPG FVVTSEAYRR FVFETGIAGF 

        70         80         90        100        110        120 
IKHILEETIV SGRPEEYEKA SELIRSKFVR TPMPPYLRRA IVDAYRKLGT LVGVEEPRVA 

       130        140        150        160        170        180 
VRSSATVEDL PEASFAGQQE TYLNVKGEEE VVEKVKTAWA SLWTARALSY RDSLNIDHET 

       190        200        210        220        230        240 
ALMAVVVQKM VSSRSSGVMF TIHPVTGEED KIVIESIWGL GEYIVGGKVT PDRFVVSKSD 

       250        260        270        280        290        300 
LEILEVRISR KDKALFYDPD LNENVEIKIP ESGEELEDLR RKHPAVAEVV EKYGIRPDAP 

       310        320        330        340        350        360 
SLSEKEVKEL ARLAIKVENH FARPMDIEWA IDFELSPPEN ILLLQARPET VWSRKKEEAE 

       370        380        390        400        410        420 
AKPPEEEAVP EGEVLVRGVP ASPGVASGRV KVALTVEEAA KKMEKGDVLV TKMTDPDWVP 

       430        440        450        460        470        480 
YMKMASAIVT DEGGMTAHAA IVARELGIPA VVGTGDATKK LKDGMLVTVD GSRGVVYAGA 

       490        500        510        520        530        540 
VKTEEAREEE ARPELGAAVA EVLSEVYPVT ATKIYMNLGH PEEIDRYKHL PFEGIGLMRI 

       550        560        570        580        590        600 
EFIISSWIGY HPMYLIEQGR GVYFIDKLAE GVAKVASAIY PRPVVVRFSD FKTNEYRRLK 

       610        620        630        640        650        660 
GGEKYETLDE RNPMIGWRGV SRYIHPNYEP AFRLEVRAIK KVREEWGLKN VWVMFPFVRT 

       670        680        690        700        710        720 
TWELERALKI MEEEGLSRGR DFKVWIMVEV PSTVFLADEF AKMVDGFSIG SNDLTQLVLG 

       730        740        750        760        770        780 
VDRDSGFLAK MGYFDERDPA VLRSIEILIE KAHSQGATVS ICGQGPSVYP ELVEFLVRRG 

       790        800        810        820 
IDSISVNPDA VVRVRRQVAS IERRIMLERL EELGSRLSRL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000002 Genomic DNA. Translation: BAA79621.2.
PIRE72652.
RefSeqNP_147390.2. NC_000854.2.

3D structure databases

ProteinModelPortalQ9YEC5.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1444791.
GenomeReviewsGene locus APE_0650.1 in contig BA000002_GR.
KEGGape:APE_0650.1.
NMPDRfig|272557.1.peg.498.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG284863.
ProtClustDBPRK06464.

Enzyme and pathway databases

BioCycAPER272557:APE0650-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_AERPE
AccessionPrimary (citable) accession number: Q9YEC5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 26, 2007
Last modified: January 25, 2012
This is version 75 of the entry and version 2 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