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P47859 (PFKAP_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 96. 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:
ATP-dependent 6-phosphofructokinase, platelet type

Short name=ATP-PFK
Short name=PFK-P
EC=2.7.1.11
Alternative name(s):
6-phosphofructokinase type C
Phosphofructo-1-kinase isozyme C
Short name=PFK-C
Phosphohexokinase
Gene names
Name:PFKP
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length791 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis By similarity. HAMAP-Rule MF_03184

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_03184

Cofactor

Magnesium.

Enzyme regulation

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate By similarity. HAMAP-Rule MF_03184

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_03184

Subunit structure

Homo- and heterotetramers By similarity. HAMAP-Rule MF_03184

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03184.

Post-translational modification

GlcNAcylation decreases enzyme activity By similarity. HAMAP-Rule MF_03184

Sequence similarities

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 791791ATP-dependent 6-phosphofructokinase, platelet type HAMAP-Rule MF_03184
PRO_0000112026

Regions

Nucleotide binding97 – 982ATP By similarity
Nucleotide binding127 – 1304ATP By similarity
Region1 – 399399N-terminal catalytic PFK domain 1 HAMAP-Rule MF_03184
Region173 – 1753Substrate binding By similarity
Region217 – 2193Substrate binding By similarity
Region307 – 3104Substrate binding By similarity
Region400 – 41112Interdomain linker HAMAP-Rule MF_03184
Region412 – 791380C-terminal regulatory PFK domain 2 HAMAP-Rule MF_03184
Region538 – 5425Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region583 – 5853Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region671 – 6744Allosteric activator fructose 2,6-bisphosphate binding By similarity

Sites

Active site1751Proton acceptor By similarity
Binding site341ATP; via amide nitrogen By similarity
Binding site2101Substrate; shared with dimeric partner By similarity
Binding site2731Substrate By similarity
Binding site3011Substrate; shared with dimeric partner By similarity
Binding site4811Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site5761Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site6391Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site6651Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site7441Allosteric activator fructose 2,6-bisphosphate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue121Phosphoserine; by PKA Ref.2
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

Sequences

Sequence LengthMass (Da)Tools
P47859 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: 3C10A36F229FD8E8

FASTA79186,350
        10         20         30         40         50         60 
MDNKVSASPR GSYRKFLEHL SGAGKAIGVL TSGGDAQGMN AAVRAVVRMG IYVGAKVYFI 

        70         80         90        100        110        120 
YEGYQGMVDG GSNIVEANWE SVSSILQVGG TIIGSARSKA FRTREGRLKA ACNLIHRGIT 

       130        140        150        160        170        180 
NLCVIGGSGS LTGANIFRME WSGLLEELAQ DGKIDNEAVQ KYAYLNVVGM VGSIDNDFCG 

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

       250        260        270        280        290        300 
ESPPEEGWEE QMCVKLSENR AQKKRLNIII VAEGAIDTLN RPITSEKIKE LVVTQLGYDT 

       310        320        330        340        350        360 
RVTILGHVQR GGTPSAFDRI LASRMGVEAV LALLEATPET PACVVSLSGN HAVRLPLVEC 

       370        380        390        400        410        420 
VQMTQEVQKA MDERRFKDAV QLRGRSFENN LNTYKRLAIK LPDDKIQKSN CNVAVINVGA 

       430        440        450        460        470        480 
PAAGMNAAVR SAVRVGIADG HKMFAVYDGF DGFAKGQIKE IRWGDVGGWT GQGGSILGTK 

       490        500        510        520        530        540 
RILPGKYLEE IATQIRTHNI NAILIIGGFE AYLGLLELSA AREKHEEFCV PMVMVPATVS 

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

       610        620        630        640        650        660 
DAAYIFEEPF DIRDLQSNVE HLTEKMKTTI QRGLVLRNES CSENYTTDFI YQLYSEEGRG 

       670        680        690        700        710        720 
VFDCRKNVLG HMQQGGAPSP FDRNFGTKIS ARAMQWITTK LKESPGKGKR FVSDDSICVL 

       730        740        750        760        770        780 
GISKRNVLFQ PVAELKNETD FEHRIPKEQW WLKLRPLMKI LAKYKTSYDV SDSGQLVPVR 

       790 
HRGGPEEPAA I 

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References

[1]"Structure and expression of the cDNA for the C isozyme of phosphofructo-1-kinase from rabbit brain."
Li Y., Valaitis A.P., Latshaw S.P., Kwiatkowska D., Tripathi R.L., Campbell M.C., Kemp R.G.
J. Biol. Chem. 269:5781-5787(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Tissue: Brain.
[2]"The sites of phosphorylation of rabbit brain phosphofructo-1-kinase by cyclic AMP-dependent protein kinase."
Valaitis A.P., Foe L.G., Kwiatkowska D., Latshaw S.P., Kemp R.G.
Biochim. Biophys. Acta 995:187-194(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 5-17, PHOSPHORYLATION AT SER-12.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U01154 mRNA. Translation: AAA17707.1.
PIRA53206.
RefSeqNP_001076217.1. NM_001082748.1.
UniGeneOcu.6209.

3D structure databases

ProteinModelPortalP47859.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000009500.

Proteomic databases

PRIDEP47859.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100009526.

Organism-specific databases

CTD5214.

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000200154.
HOVERGENHBG000976.

Enzyme and pathway databases

UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_03184. Phosphofructokinase_I_E.
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...

Entry information

Entry namePFKAP_RABIT
AccessionPrimary (citable) accession number: P47859
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: July 9, 2014
This is version 96 of the entry and version 1 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