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Q5R636 (K6PP_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 59. 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
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length784 AA.
Sequence statusComplete.
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 By similarity. HAMAP-Rule MF_00339

Enzyme regulation

Allosteric enzyme activated by ADP, AMP, or fructose bisphosphate and inhibited by ATP or citrate By similarity. 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

Post-translational modification

GlcNAcylation decreases enzyme activity By similarity. HAMAP-Rule MF_00339

Sequence similarities

Belongs to the phosphofructokinase family. Two domains subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7847846-phosphofructokinase type C HAMAP-Rule MF_00339
PRO_0000284442

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
Modified residue7831Phosphoserine By similarity
Glycosylation5401O-linked (GlcNAc) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R636 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 6DC468B4629E235D

FASTA78485,525
        10         20         30         40         50         60 
MDADDSRAPK GSLRKFLEHL SGAGKAIGVL TSGGDAQGMN AAVRAVVRMG IYVGAKVCFI 

        70         80         90        100        110        120 
YEGYQGMVDG GSNIAEADWE SVSSILQVGG TIIGSARCQA FRTREGRLKA ACNLLQRGIT 

       130        140        150        160        170        180 
NLCVIGGDGS LTGANLFRKE WSGLLEELAR NGQIDKEAVQ KYAYLNVVGM VGSIDNDFCG 

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

       250        260        270        280        290        300 
ESPPEEGWEE QMCVKLSENR ARKKRLNIII VAEGAIDTQN KPITSEKIKE LVVTQLGYDT 

       310        320        330        340        350        360 
RVTILGHVQR GGTPSAFDRI LASRMGVEAV IALLEATPDT PACVVSLNGN HAVRLPLMEC 

       370        380        390        400        410        420 
VQMTQDVQKA MDERRFQDAV RLRGRSFAGN LNTYKRLAIK LPDDQIPKTN CNVAVINVGA 

       430        440        450        460        470        480 
PAAGMNAAVR SAVRVGIADG HRMLAIYDGF DGFAKGQIKE IGWTDVGGWT GQGGSILGTK 

       490        500        510        520        530        540 
RVLPGKYLEE IATQMRTHSI NALLIIGGFE AYLGLLELSA AREKHEEFCV PMVMVPATVS 

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

       610        620        630        640        650        660 
DAAYIFEEPF DIRDLQSSVE HLTEKMKTTI QRGLVLRNES CSENYTTDFI YQLYSEEGKG 

       670        680        690        700        710        720 
VFDCRKNVLG HMQQGGAPSP FDRNFGTKIS ARAMEWITAK LKETRGRGKK FTTDDSVCVL 

       730        740        750        760        770        780 
GISKRNVIFQ PVAELKKQTD FEHRIPKEQW WLKLRPLMKI LAKYKASYDV SDSGQLEHVQ 


PWSV 

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References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR860660 mRNA. Translation: CAH92780.1.
RefSeqNP_001126622.1. NM_001133150.1.
UniGenePab.4970.

3D structure databases

ProteinModelPortalQ5R636.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5R636.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100173619.
KEGGpon:100173619.

Organism-specific databases

CTD5214.

Phylogenomic databases

HOVERGENHBG000976.
InParanoidQ5R636.
KOK00850.

Enzyme and pathway databases

UniPathwayUPA00109; UER00182.

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...

Entry information

Entry nameK6PP_PONAB
AccessionPrimary (citable) accession number: Q5R636
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 59 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