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Reviewed, UniProtKB/Swiss-Prot P46893 (PPSA_STAMF)

Last modified November 3, 2009. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Probable phosphoenolpyruvate synthase
      Short name=PEP synthase
    EC=2.7.9.2
Alternative name(s):
    Pyruvate, water dikinase
Gene names
Name: ppsA
Ordered Locus Names: Smar_0141
OrganismStaphylothermus marinus (strain ATCC 43588 / DSM 3639 / F1) [Complete proteome] [HAMAP]
Taxonomic identifier399550 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiDesulfurococcalesDesulfurococcaceaeStaphylothermus

Protein attributes

Sequence length834 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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.

Subunit structure

Homooligomer. Forms a large complex of about 2000 kDa.

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.

Post-translational modification

The N-terminus is blocked.

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 – 834834Probable phosphoenolpyruvate synthase
PRO_0000147038

Sites

Active site4471Tele-phosphohistidine intermediate By similarity
Active site7721Proton donor By similarity
Metal binding6991Magnesium By similarity
Metal binding7231Magnesium By similarity
Binding site5501Substrate By similarity
Binding site5981Substrate By similarity
Binding site6991Substrate By similarity
Binding site7201Substrate; via carbonyl oxygen By similarity
Binding site7211Substrate; via amide nitrogen By similarity
Binding site7221Substrate By similarity
Binding site7231Substrate; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
P46893-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 4F6C80446D4D327C

FASTA83493,736
        10         20         30         40         50         60 
MSNVPKEKRF IVWLDEVTKD DVVLVGGKNA NLGEMIRAGI PVPPGFAVTA YAYKYFIEKT 

        70         80         90        100        110        120 
GLKDKIYPLL NSIDVNDKKV LDETTAKIRQ WIMDTPMPPE VEEEIRKYYR ELAKKIGMEP 

       130        140        150        160        170        180 
EKLRVAVRSS ATAEDMPEAS FAGQQDTYLN VYGEDNVVYY VKRCWASLFT SRAVFYRVAQ 

       190        200        210        220        230        240 
GIPHEKSLMS VTVQKMVNSR TAGVMFTLHP VTGDEKVVVI EASWGLGESV VGGKVTPDEW 

       250        260        270        280        290        300 
VVDKQTLQIV DQKIHHKTLA IVFDPKKGKN VEIRWDENKQ AWVSEEGPVD IEMVKHFHPD 

       310        320        330        340        350        360 
KPALKEEEVK RLAELALLIE KHYGRHMDIE WAVDYDIPFP DNVFIVQARL ETVWSVRKEK 

       370        380        390        400        410        420 
EKAEKKAEIK GKNIVKLSEA KVLVRGLPAS PGIGAGVAKV IFDPHSKEAQ EFKEGEVLVT 

       430        440        450        460        470        480 
KMTDPDWVPL MKKAVAIVTD EGGMTSHAAI VSRELGIPAI VGTGNATQVI KSGIEVTVDG 

       490        500        510        520        530        540 
SRGVVYEGIV EDLVKPKEEV KAEVAGVGIS PEQLLPLYPV TATKIYMNLG EPDAIEKYKD 

       550        560        570        580        590        600 
LPFDGIGLMR IEFIITDWVQ YHPLYLIEQG KESLFIDKLA EGIAKVAQAI YPRPVVVRFS 

       610        620        630        640        650        660 
DFKTNEYRGL KGGEKYEPEE RNPMIGWRGV SRYIHPKYEP AFRLEVRAIK KVREEMGLTN 

       670        680        690        700        710        720 
VWVMFPFVRT TWELERALKI MEEEGLKRGK DFKVWAMAEV PSIVLLADKF AEYVDGFSIG 

       730        740        750        760        770        780 
SNDLTQLILG ADRDSNILAE MGYFDERDPA VLAGIKMIIE KAHSKGATVS ICGQAPSVYP 

       790        800        810        820        830 
EIVEFLVEAG IDSISVNPDA VIATRRLVAS IERKIMLKRL NKIMDKLNKL ELGF 

« Hide

References

« Hide 'large scale' references
[1]"Primary structure of a multimeric protein, homologous to the PEP-utilizing enzyme family and isolated from a hyperthermophilic archaebacterium."
Cicicopol C., Peters J., Kellermann J., Baumeister W.
FEBS Lett. 356:345-350(1994) [PubMed: 7805870] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 296-320; 528-546; 625-636; 638-647; 657-661; 682-694; 698-720 AND 742-752.
[2]"Complete sequence of Staphylothermus marinus F1."
Copeland A., Lucas S., Lapidus A., Barry K., Dalin E., Tice H., Pitluck S., Sun H., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Huber H., Woese C., Anderson I.J., Richardson P.
Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

S74619 Genomic DNA. Translation: AAB32888.1.
CP000575 Genomic DNA. Translation: ABN69254.1.
PIRS51006.
RefSeqYP_001040162.1.

3D structure databases

HSSPHSSP built from PDB template 1H6Z based on UniProtKB O76283.
ModBaseSearch...

Protein-protein interaction databases

STRINGP46893.

Genome annotation databases

GeneID4907183.
GenomeReviewsGene locus Smar_0141 in contig CP000575_GR.
KEGGsmr:Smar_0141.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMANKYVGIC.

Family and domain databases

InterProIPR013815. ATP_grasp_subdomain_1.
IPR008279. PEP_mobile.
IPR018274. PEP_mobile_CS.
IPR006319. PEP_synth.
IPR000121. PEP_utilizers.
IPR002192. PPDK_PEP_bd.
IPR015813. Pyrv/PenolPyrv_Kinase_cat.
[Graphical view]
Gene3DG3DSA:3.30.1490.20. ATP_grasp_subdomain_1. 1 hit.
G3DSA:3.50.30.10. PEP_mobile. 1 hit.
G3DSA:3.20.20.60. Pyrv/PenolPyrv_Kinase_cat. 1 hit.
PfamPF00391. PEP-utilizers. 1 hit.
PF02896. PEP-utilizers_C. 1 hit.
PF01326. PPDK_N. 1 hit.
[Graphical view]
ProDomPD000940. PEP_utilizers. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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_STAMF
AccessionPrimary (citable) accession number: P46893
Secondary accession number(s): A3DKU4
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 3, 2009
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents