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P47858 (K6PF_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. 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, muscle type

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

Protein attributes

Sequence length780 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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

Subunit structure

Homotetramer.

Post-translational modification

GlcNAcylation decreases enzyme activity By similarity. HAMAP-Rule MF_00339

Sequence similarities

Belongs to the phosphofructokinase family. Two domains subfamily.

Ontologies

Keywords
   Biological processGlycolysis
   DomainRepeat
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate phosphorylation

Inferred from direct assay PubMed 12161PubMed 2931076PubMed 3159721PubMed 8593533. Source: GOC

cellular glucose homeostasis

Non-traceable author statement Ref.1. Source: RGD

fructose 1,6-bisphosphate metabolic process

Inferred from direct assay PubMed 12161PubMed 2931076PubMed 3159721PubMed 8593533. Source: RGD

fructose 6-phosphate metabolic process

Inferred from direct assay PubMed 12161PubMed 2931076PubMed 3159721PubMed 8593533. Source: RGD

glycolysis

Inferred from direct assay PubMed 2931076PubMed 8593533. Source: RGD

protein homotetramerization

Inferred from direct assay PubMed 2931076. Source: RGD

   Cellular_component6-phosphofructokinase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_function6-phosphofructokinase activity

Inferred from sequence or structural similarity. Source: UniProtKB

AMP binding

Inferred from direct assay PubMed 12161PubMed 3159721. Source: RGD

ATP binding

Inferred from direct assay PubMed 12161PubMed 2931076PubMed 3159721. Source: RGD

carbohydrate binding

Inferred from direct assay PubMed 8593533. Source: RGD

fructose-6-phosphate binding

Inferred from direct assay PubMed 12161PubMed 2931076PubMed 3159721. Source: RGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phosphofructokinase activity

Inferred from mutant phenotype PubMed 14522413. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 7807796-phosphofructokinase, muscle type HAMAP-Rule MF_00339
PRO_0000112020

Regions

Nucleotide binding35 – 395ATP By similarity
Nucleotide binding193 – 1975ATP By similarity
Nucleotide binding210 – 22617ATP By similarity

Sites

Active site1661Proton acceptor By similarity
Metal binding2241Magnesium; via carbonyl oxygen By similarity
Binding site2011Substrate By similarity
Binding site2921Substrate By similarity
Binding site2981Substrate By similarity
Binding site3011Substrate By similarity

Amino acid modifications

Modified residue21N-acetylthreonine By similarity
Modified residue7751Phosphoserine By similarity
Glycosylation5301O-linked (GlcNAc) By similarity

Experimental info

Sequence conflict331T → A in BAA21013. Ref.3
Sequence conflict461L → A in BAA21013. Ref.3
Sequence conflict1501R → A in BAA21013. Ref.3
Sequence conflict1601F → G in BAA21013. Ref.3
Sequence conflict1801S → F in BAA21013. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P47858 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: CECC3995C4F271FA

FASTA78085,560
        10         20         30         40         50         60 
MTHEEHHEAK TLGIGKAIAV LTSGGDAQGM NATVRAVVRV GIFTGLRVFF VHEGYQGLVD 

        70         80         90        100        110        120 
GGEHIREATW ESVSMMLQLG GTVIGSARCK DFREREGRLR AAHNLVKRGI TNLCVIGGDG 

       130        140        150        160        170        180 
SLTGADTFRS EWSDLLNDLQ KDGKITAEER TKSSYLNIVF LVGSIDNDFC GTDMTIGTDS 

       190        200        210        220        230        240 
ALHRIVEIVD AITTTAQSHQ RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDDWE 

       250        260        270        280        290        300 
EHLCRRLSET RTRGSRLNII IVAEGAIDKN GKPITSEDIK NLVVKRLGYD TRVTVLGHVQ 

       310        320        330        340        350        360 
RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NTAVRLPLME CVQVTKDVTK 

       370        380        390        400        410        420 
AMDEKRFDEA IKLRGRSFMN NWEVYKLLAH VRPPVSKGGL HTVAVMNVGA PAAGMNAAVR 

       430        440        450        460        470        480 
STVRIGLIQG NRVLVVHDGF EGLAKGQIEE AGWSYVGGWT GQGGSKLGTK RTLPKKNLEQ 

       490        500        510        520        530        540 
ISANITKYNI QGLVIIGGFE AYTGGLELME GRKQFDELCI PFVVIPATVS NNVPGSDFSI 

       550        560        570        580        590        600 
GADTALNTIC TTCDRIKQSA AGTKRRVFII ETMGGYCGYL ATMAGLAAGA DAAYIFEEPF 

       610        620        630        640        650        660 
TIRDLQVNVE HLVQKMKTTV KRGLVLRNEK CNENYTTDFI FNLYSEEGKG IFDSRKNVLG 

       670        680        690        700        710        720 
HMQQGGNPTP FDRNFATKMG AKATNWMSGK IKESYRNGRI FANTPDSGCV LGMRKRALVF 

       730        740        750        760        770        780 
QPVTELKDQT DFEHRIPKEQ WWLKLRPILK ILAKYEIDLD TSDHAHLEHI SRKRSGEAAV 

« Hide

References

[1]"Characterization of expression of phosphofructokinase isoforms in isolated rat pancreatic islets and purified beta cells and cloning and expression of the rat phosphofructokinase-A isoform."
Ma Z., Ramanadham S., Turk J., Kempe K., Hu Z., Ladenson J.
Biochim. Biophys. Acta 1308:151-163(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Pancreatic islet.
[2]Ma Z.
Submitted (SEP-1996) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION TO 163-170 AND 494-498.
[3]Nakajima H.
Submitted (NOV-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-213.
Strain: Sprague-Dawley.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U25651 mRNA. Translation: AAC52786.1.
D21869 mRNA. Translation: BAA21013.1.
PIRS71429.
RefSeqNP_113903.1. NM_031715.1.
UniGeneRn.11004.

3D structure databases

ProteinModelPortalP47858.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249268. 1 interaction.
IntActP47858. 1 interaction.
MINTMINT-89284.

PTM databases

PhosphoSiteP47858.

Proteomic databases

PaxDbP47858.
PRIDEP47858.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID65152.
KEGGrno:65152.
UCSCRGD:68419. rat.

Organism-specific databases

CTD5213.
RGD68419. Pfkm.

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000200154.
HOVERGENHBG000976.
InParanoidP47858.
KOK00850.
PhylomeDBP47858.

Enzyme and pathway databases

SABIO-RKP47858.
UniPathwayUPA00109; UER00182.

Gene expression databases

GenevestigatorP47858.

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

NextBio613989.

Entry information

Entry nameK6PF_RAT
AccessionPrimary (citable) accession number: P47858
Secondary accession number(s): Q63736
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 115 of the entry and version 3 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