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Q6P7S0 (Q6P7S0_RAT) Unreviewed, UniProtKB/TrEMBL

Last modified January 22, 2014. Version 69. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Pyruvate kinase RuleBase RU000504

EC=2.7.1.40 RuleBase RU000504
Gene names
Name:Pkm RGD 3337
Synonyms:Pkm2 RGD 3337
OrganismRattus norvegicus (Rat) EMBL AAH61541.1
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length487 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Catalytic activity

ATP + pyruvate = ADP + phosphoenolpyruvate. RuleBase RU000504

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5. RuleBase RU000504

Sequence similarities

Belongs to the pyruvate kinase family. RuleBase RU000504

Ontologies

Keywords
   Biological processGlycolysis RuleBase RU000504
   LigandMagnesium RuleBase RU000504
   Molecular functionKinase RuleBase RU000504
Transferase
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Molecular_functionmagnesium ion binding

Inferred from electronic annotation. Source: InterPro

potassium ion binding

Inferred from electronic annotation. Source: InterPro

pyruvate kinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequences

Sequence LengthMass (Da)Tools
Q6P7S0 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 8BAE1D9315BF6FBB

FASTA48752,936
        10         20         30         40         50         60 
MPKPDSEAGT AFIQTQQLHA AMADTFLEHM CRLDIDSAPI TARNTGIICT IGPASRSVEM 

        70         80         90        100        110        120 
LKEMIKSGMN VARLNFSHGT HEYHAETIKN VRAATESFAS DPILYRPVAV ALDTKGPEIR 

       130        140        150        160        170        180 
TGLIKGSGTA EVELKKGATL KITLDNAYME KCDENILWLD YKNICKVVEV GSKIYVDDGL 

       190        200        210        220        230        240 
ISLQVKEKGA DYLVTEVENG GSLGSKKGVN LPGAAVDLPA VSEKDIQDLK FGVEQDVDMV 

       250        260        270        280        290        300 
FASFIRKAAD VHEVRKVLGE KVFLAQKMMI GRCNRAGKPV ICATQMLESM IKKPRPTRAE 

       310        320        330        340        350        360 
GSDVANAVLD GADCIMLSGE TAKGDYPLEA VRMQHLIARE AEAAIYHLQL FEELRRLAPI 

       370        380        390        400        410        420 
TSDPTEAAAV GAVEASFKCC SGAIIVLTKS GRSAHQVARY RPRAPIIAVT RNPQTARQAH 

       430        440        450        460        470        480 
LYRGIFPVLC KDAVLDAWAE DVDLRVNLAM NVGKARGFFK KGDVVIVLTG WRPGSGFTNT 


MRVVPVP 

« Hide

References

[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M. expand/collapse author list , Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pituitary gland EMBL AAH61541.1.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC061541 mRNA. Translation: AAH61541.1.
UniGeneRn.1556.

3D structure databases

ProteinModelPortalQ6P7S0.
SMRQ6P7S0. Positions 13-487.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ6P7S0.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

RGD3337. Pkm.

Phylogenomic databases

HOGENOMHOG000021559.
HOVERGENHBG000941.
InParanoidQ6P7S0.

Enzyme and pathway databases

UniPathwayUPA00109; UER00188.

Gene expression databases

GenevestigatorQ6P7S0.

Family and domain databases

Gene3D2.40.33.10. 1 hit.
3.20.20.60. 3 hits.
3.40.1380.20. 1 hit.
InterProIPR001697. Pyr_Knase.
IPR015813. Pyrv/PenolPyrv_Kinase-like_dom.
IPR011037. Pyrv_Knase-like_insert_dom.
IPR015794. Pyrv_Knase_a/b.
IPR015793. Pyrv_Knase_brl.
IPR015795. Pyrv_Knase_C.
IPR015806. Pyrv_Knase_insert_dom.
[Graphical view]
PANTHERPTHR11817. PTHR11817. 1 hit.
PfamPF00224. PK. 1 hit.
PF02887. PK_C. 1 hit.
[Graphical view]
PRINTSPR01050. PYRUVTKNASE.
SUPFAMSSF50800. SSF50800. 1 hit.
SSF51621. SSF51621. 2 hits.
SSF52935. SSF52935. 1 hit.
ProtoNetSearch...

Entry information

Entry nameQ6P7S0_RAT
AccessionPrimary (citable) accession number: Q6P7S0
Entry history
Integrated into UniProtKB/TrEMBL: July 5, 2004
Last sequence update: July 5, 2004
Last modified: January 22, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)