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P47860 (K6PP_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
6-phosphofructokinase type C

EC=2.7.1.11
Alternative name(s):
Phosphofructo-1-kinase isozyme C
Short name=PFK-C
Phosphofructokinase 1
Phosphohexokinase
Gene names
Name:Pfkp
Synonyms:Pfkc
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length788 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the third step of glycolysis, the phosphorylation of fructose-6-phosphate (F6P) by ATP to generate fructose-1,6-bisphosphate (FBP) and ADP By similarity. HAMAP-Rule MF_00339

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_00339

Cofactor

Magnesium.

Enzyme regulation

Allosteric enzyme activated by ADP, AMP, or fructose bisphosphate and inhibited by ATP or citrate. HAMAP-Rule MF_00339

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_00339

Tissue specificity

Expressed at high level in neuroendocrine tissues.

Post-translational modification

GlcNAcylation decreases enzyme activity By similarity. HAMAP-Rule MF_00339

Sequence similarities

Belongs to the phosphofructokinase family. Two domains subfamily.

Sequence caution

The sequence AAA17757.1 differs from that shown. Reason: Frameshift at position 27.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7887886-phosphofructokinase type C HAMAP-Rule MF_00339
PRO_0000112027

Regions

Nucleotide binding44 – 485ATP By similarity
Nucleotide binding202 – 2065ATP By similarity
Nucleotide binding219 – 23517ATP By similarity

Sites

Active site1751Proton acceptor By similarity
Metal binding2331Magnesium; via carbonyl oxygen By similarity
Binding site2101Substrate By similarity
Binding site3011Substrate By similarity
Binding site3071Substrate By similarity
Binding site3101Substrate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue121Phosphoserine By similarity
Modified residue3861Phosphoserine By similarity
Modified residue3951N6-acetyllysine By similarity
Modified residue4861N6-acetyllysine By similarity
Modified residue6511Phosphotyrosine By similarity
Modified residue6881N6-acetyllysine By similarity
Glycosylation5401O-linked (GlcNAc) By similarity

Experimental info

Sequence conflict35 – 362DA → ES in AAA17757. Ref.2
Sequence conflict511I → M in AAA17757. Ref.2
Sequence conflict561K → Q in AAA17757. Ref.2
Sequence conflict1111A → T in AAA17757. Ref.2
Sequence conflict2201H → Y in AAA17757. Ref.2
Sequence conflict6001A → R in AAA17757. Ref.2
Sequence conflict7551R → L in AAA17757. Ref.2
Sequence conflict7581M → S in AAA17757. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P47860 [UniParc].

Last modified December 20, 2005. Version 2.
Checksum: 16FEB963C3297CA6

FASTA78885,720
        10         20         30         40         50         60 
MSDQDSSTSS TSFPKYLEHL SGDGKAIGVL TSGGDAQGMN AAVRAVVRMG IYTGAKVYFI 

        70         80         90        100        110        120 
YEGYQGMVDG GSNIVEAKWE CVSSILQVGG TIIGSARCQA FRSREGRLKA ACNLVRLGIT 

       130        140        150        160        170        180 
NLCVIGGDGS LTGANLFRKE WSGLLEELAK NGEIDSDTVK KHAYLNVVGM VGSIDNDFCG 

       190        200        210        220        230        240 
TDMTIGTDSA LHRIIEVVDA IMTTAQSHQR TFVLEVMGRH CGYLALVSAL ACGADWVFLP 

       250        260        270        280        290        300 
ESPPEEGWEE EMCLKLSENR ARKKRLNIII VSEGAIDTQN KPITSEKIKE LVVTNLGFDT 

       310        320        330        340        350        360 
RVTILGHVQR GGTPSAFDRI LASRMGVEAV LALLEATPET PACVVSLRGN QAVRLPLMEC 

       370        380        390        400        410        420 
VQMTQDVQKA MDERRFDEAV KLRGRSFEGN LNTYKRLAIK EPDDKIPKSN CNVAIINVGA 

       430        440        450        460        470        480 
PAAGMNAAVR SAVRVGIAEG HKMFAIYDGF DGLANGQIKE IGWGDVGGWT GQGGSILGTK 

       490        500        510        520        530        540 
RTLPGKYLEK IAEQMHSKNI NALLIIGGFE AYLGLLELAA ARNKHEAFCV PMVMVPATVS 

       550        560        570        580        590        600 
NNVPGSDFSI GADTALNTIT DTCDRIKQSA SGTKRRVFII ETMGGYCGYL ANMGGLAAGA 

       610        620        630        640        650        660 
DAAYIFEEQF DIRDLQSNVM HLTEKMKTSI QRGLVLRNEN CSVNYTTDFI YQLYSEEGKG 

       670        680        690        700        710        720 
VFDCRKNVLG HMQQGGAPSP FDRNFGTKIS AKAMEWISAK LKGSHGTGKK FVSDDSICVL 

       730        740        750        760        770        780 
GIQKRDLLFK PVAELRKATD FEHRIPKQQW WLKLRPIMKI LAKYEASYDM SDVGKLEPVH 


NHGELSAI 

« Hide

References

« Hide 'large scale' references
[1]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[2]"Structure, distribution, and functional expression of the phosphofructokinase C isozyme."
Gekakis N., Johnson R.C., Jerkins A., Mains R.E., Sul H.S.
J. Biol. Chem. 269:3348-3355(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-788.
Tissue: Hypothalamus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC088847 mRNA. Translation: AAH88847.1.
L25387 mRNA. Translation: AAA17757.1. Frameshift.
PIRA53047.
RefSeqNP_996729.1. NM_206847.1.
UniGeneRn.2278.

3D structure databases

ProteinModelPortalP47860.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid248822. 2 interactions.
IntActP47860. 2 interactions.

PTM databases

PhosphoSiteP47860.

2D gel databases

World-2DPAGE0004:P47860.

Proteomic databases

PaxDbP47860.
PRIDEP47860.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID60416.
KEGGrno:60416.
UCSCRGD:61893. rat.

Organism-specific databases

CTD5214.
RGD61893. Pfkp.

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000200154.
HOVERGENHBG000976.
InParanoidP47860.
KOK00850.
PhylomeDBP47860.

Enzyme and pathway databases

SABIO-RKP47860.
UniPathwayUPA00109; UER00182.

Gene expression databases

GenevestigatorP47860.

Family and domain databases

HAMAPMF_00339. Phosphofructokinase.
InterProIPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamPF00365. PFK. 2 hits.
[Graphical view]
PIRSFPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSPR00476. PHFRCTKINASE.
SUPFAMSSF53784. SSF53784. 2 hits.
TIGRFAMsTIGR02478. 6PF1K_euk. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio612122.

Entry information

Entry nameK6PP_RAT
AccessionPrimary (citable) accession number: P47860
Secondary accession number(s): Q5HZX8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 20, 2005
Last modified: April 16, 2014
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways