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O08333 (K6PF1_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 98. 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 1

EC=2.7.1.11
Alternative name(s):
ATP-PFK
Phosphofructokinase 1
Phosphohexokinase 1
Gene names
Name:pfkA1
Synonyms:pfk1, pfkA
Ordered Locus Names:SCO2119
ORF Names:SC6E10.13c
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length342 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Enzyme regulation

Allosterically inhibited by phosphoenolpyruvate. 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 By similarity. HAMAP-Rule MF_00339

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00339.

Sequence similarities

Belongs to the phosphofructokinase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3423426-phosphofructokinase 1 HAMAP-Rule MF_00339
PRO_0000111986

Regions

Nucleotide binding20 – 245ATP By similarity
Nucleotide binding155 – 1595ATP By similarity
Nucleotide binding172 – 18817ATP By similarity

Sites

Active site1281Proton acceptor By similarity
Metal binding1861Magnesium; via carbonyl oxygen By similarity
Binding site1631Substrate By similarity
Binding site2661Substrate By similarity
Binding site2721Substrate By similarity
Binding site2751Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
O08333 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: CEEFC7B74092AB34

FASTA34236,664
        10         20         30         40         50         60 
MKVGVLTGGG DCPGLNAVIR AVVRKGVQEY GYDFTGFRDG WRGPLEGDTV PLDIPAVRGI 

        70         80         90        100        110        120 
LPRGGTVLGS SRTNPLKQRD GIRRIKDNLA ALGVEALITI GGEDTLGVAT RLADEYGVPC 

       130        140        150        160        170        180 
VGVPKTIDND LSATDYTFGF DTAVGIATEA IDRLHTTAES HMRVLVVEVM GRHAGWIALH 

       190        200        210        220        230        240 
SGLAGGANVI LIPEQRFDVE QVCSWVTSRF RASYAPIVVV AEGAMPRDGD MVLKDESLDS 

       250        260        270        280        290        300 
YGHVRLSGVG EWLAKQIEKR TGNEARTTVL GHVQRGGTPS AFDRWLATRF GLHAVDCVHD 

       310        320        330        340 
GDFGKMVALR GTDIVRVPIA EATARLKTVD PALYEEVGVF FG 

« Hide

References

« Hide 'large scale' references
[1]"Identification of ATP-dependent phosphofructokinase as a regulatory step in the glycolytic pathway of the actinomycete Streptomyces coelicolor A3(2)."
Alves A.M.C.R., Euverink G.J.W., Bibb M.J., Dijkhuizen L.
Appl. Environ. Microbiol. 63:956-961(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: A3(2) / 1109.
[2]"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)."
Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. expand/collapse author list , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.
Nature 417:141-147(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-471 / A3(2) / M145.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U51728 Genomic DNA. Translation: AAC45135.1.
AL939111 Genomic DNA. Translation: CAB51967.1.
PIRT35500.
RefSeqNP_626376.1. NC_003888.3.

3D structure databases

ProteinModelPortalO08333.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO2119.

PTM databases

PhosSiteP1007943.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB51967; CAB51967; CAB51967.
GeneID1097553.
KEGGsco:SCO2119.
PATRIC23733890. VBIStrCoe124346_2154.

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000248869.
KOK00850.
OMADIMELPR.
OrthoDBEOG644ZRM.
PhylomeDBO08333.
ProtClustDBPRK03202.

Enzyme and pathway databases

UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_00339. Phosphofructokinase.
InterProIPR012003. ATP_PFK_prok.
IPR012829. PFK.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamPF00365. PFK. 1 hit.
[Graphical view]
PIRSFPIRSF000532. ATP_PFK_prok. 1 hit.
PRINTSPR00476. PHFRCTKINASE.
SUPFAMSSF53784. SSF53784. 1 hit.
TIGRFAMsTIGR02483. PFK_mixed. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameK6PF1_STRCO
AccessionPrimary (citable) accession number: O08333
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 98 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways