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Q9L1L8 (PFKA2_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 95. 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 2

Short name=ATP-PFK 2
Short name=Phosphofructokinase 2
EC=2.7.1.11
Alternative name(s):
Phosphohexokinase 2
Gene names
Name:pfkA2
Synonyms:pfk2
Ordered Locus Names:SCO5426
ORF Names:SC6A11.02
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group

Protein attributes

Sequence length341 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. Ref.2

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. Ref.2

Cofactor

Magnesium. Ref.2

Enzyme regulation

Allosterically inhibited by phosphoenolpyruvate. Ref.2

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_01976

Subunit structure

Homodimer or homotetramer By similarity. HAMAP-Rule MF_01976

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01976.

Disruption phenotype

Accumulates glucose 6-phosphate and fructose 6-phosphate. Has an increased carbon flux through the pentose phosphate pathway, resulting in a higher production of the pigmented antibiotics actinorhodin and undecylprodigiosin. Ref.3

Sequence similarities

Belongs to the phosphofructokinase type A (PFKA) family. Mixed-substrate PFK group III subfamily.

Caution

The nucleotide sequence reported in Ref.2 was not that of the characterized enzyme. Inspection of the original N-terminal sequence showed that the characterized enzyme was pfkA2 (SCO5426) and not pfkA1 (SCO2119), another isozyme in S.coelicolor (Ref.3).

Biophysicochemical properties

Kinetic parameters:

KM=0.4 mM for ATP Ref.2

Vmax=165 µmol/min/mg enzyme

pH dependence:

Optimum pH is 7.5-8.

Temperature dependence:

Optimum temperature is 30-50 degrees Celsius.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 341341ATP-dependent 6-phosphofructokinase 2 HAMAP-Rule MF_01976
PRO_0000111987

Regions

Nucleotide binding72 – 732ATP By similarity
Nucleotide binding102 – 1054ATP By similarity
Region125 – 1273Substrate binding By similarity
Region169 – 1713Substrate binding By similarity
Region272 – 2754Substrate binding By similarity

Sites

Active site1271Proton acceptor By similarity
Metal binding1031Magnesium; catalytic By similarity
Binding site101ATP; via amide nitrogen By similarity
Binding site1621Substrate; shared with dimeric partner By similarity
Binding site2221Substrate By similarity
Binding site2661Substrate; shared with dimeric partner By similarity
Site1041Important for substrate specificity; cannot use PPi as phosphoryl donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9L1L8 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 6C0B09B76FE90BBD

FASTA34136,434
        10         20         30         40         50         60 
MRIGVLTAGG DCPGLNAVIR SVVHRAVDNY GDEVIGFEDG YAGLLDGRYR ALDLNAVSGI 

        70         80         90        100        110        120 
LARGGTILGS SRLERDRLRE ACENAGDMIQ NFGIDALIPI GGEGTLTAAR MLSDAGLPVV 

       130        140        150        160        170        180 
GVPKTIDNDI SSTDRTFGFD TAVGVATEAM DRLKTTAESH QRVMVVEVMG RHAGWIALES 

       190        200        210        220        230        240 
GMAAGAHGIC LPERPFDPAD LVKMVEERFS RGKKFAVVCV AEGAHPAEGS MDYGKGAIDK 

       250        260        270        280        290        300 
FGHERFQGIG TALAFELERR LGKEAKPVIL GHVQRGGVPT AYDRVLATRF GWHAVEAAHR 

       310        320        330        340 
GDFGRMTALR GTDVVMVPLA EAVTELKTVP KDRMDEAESV F 

« Hide

References

« Hide 'large scale' references
[1]"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.
[2]"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: PARTIAL PROTEIN SEQUENCE OF 1-28, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ENZYME REGULATION.
Strain: A3(2) / 1109.
[3]"Antibiotic overproduction in Streptomyces coelicolor A3(2) mediated by phosphofructokinase deletion."
Borodina I., Siebring J., Zhang J., Smith C.P., van Keulen G., Dijkhuizen L., Nielsen J.
J. Biol. Chem. 283:25186-25199(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL939123 Genomic DNA. Translation: CAB72402.1.
RefSeqNP_629564.1. NC_003888.3.

3D structure databases

ProteinModelPortalQ9L1L8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO5426.

Proteomic databases

PRIDEQ9L1L8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB72402; CAB72402; CAB72402.
GeneID1100866.
KEGGsco:SCO5426.
PATRIC23740702. VBIStrCoe124346_5507.

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000248869.
KOK00850.
OMARGDFGRM.
OrthoDBEOG644ZRM.
PhylomeDBQ9L1L8.

Enzyme and pathway databases

UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_01976. Phosphofructokinase_III.
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 namePFKA2_STRCO
AccessionPrimary (citable) accession number: Q9L1L8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: October 1, 2000
Last modified: July 9, 2014
This is version 95 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