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O08333 (PFP_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 101. 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:
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase

EC=2.7.1.90
Alternative name(s):
6-phosphofructokinase, pyrophosphate dependent
PPi-dependent phosphofructokinase
Short name=PPi-PFK
Pyrophosphate-dependent 6-phosphofructose-1-kinase
Gene names
Name:pfkA1
Synonyms:pfk1, pfkA, pfp
Ordered Locus Names:SCO2119
ORF Names:SC6E10.13c
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group

Protein attributes

Sequence length342 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions By similarity. HAMAP-Rule MF_01976

Catalytic activity

Diphosphate + D-fructose 6-phosphate = phosphate + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_01976

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01976

Enzyme regulation

Non-allosteric By similarity. HAMAP-Rule MF_01976

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

No effect. Ref.3

Sequence similarities

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

Caution

Was originally characterized as ATP-dependent phosphofructokinase (Ref.1). However, inspection of the original N-terminal sequence showed that the characterized enzyme was not pfkA1 (SCO2119), but pfkA2 (SCO5426) instead, another isozyme in S.coelicolor (Ref.3).

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processfructose 6-phosphate metabolic process

Inferred from electronic annotation. Source: InterPro

glycolytic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_component6-phosphofructokinase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_function6-phosphofructokinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 342342Pyrophosphate--fructose 6-phosphate 1-phosphotransferase HAMAP-Rule MF_01976
PRO_0000111986

Regions

Region126 – 1283Substrate binding By similarity
Region170 – 1723Substrate binding By similarity
Region272 – 2754Substrate binding By similarity

Sites

Active site1281Proton acceptor By similarity
Metal binding1031Magnesium; catalytic By similarity
Binding site101Diphosphate; via amide nitrogen By similarity
Binding site1631Substrate; shared with dimeric partner By similarity
Binding site2221Substrate By similarity
Binding site2661Substrate; shared with dimeric partner By similarity
Site1041Important for catalytic activity and substrate specificity; stabilizes the transition state when the phosphoryl donor is PPi; prevents ATP from binding by mimicking the alpha-phosphate group of ATP By similarity
Site1251Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi 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].
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.
[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.

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.
OMAHRHRAHA.
OrthoDBEOG644ZRM.
PhylomeDBO08333.

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 namePFP_STRCO
AccessionPrimary (citable) accession number: O08333
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 1, 1997
Last modified: July 9, 2014
This is version 101 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