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C0MGJ9 (PFKA_STRS7) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 39. 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

Short name=ATP-PFK
Short name=Phosphofructokinase
EC=2.7.1.11
Alternative name(s):
Phosphohexokinase
Gene names
Name:pfkA
Ordered Locus Names:SZO_10830
OrganismStreptococcus equi subsp. zooepidemicus (strain H70) [Complete proteome] [HAMAP]
Taxonomic identifier553483 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length337 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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_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

Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate 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

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00339

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00339.

Sequence similarities

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade "B1" sub-subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 337337ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_00339
PRO_1000205251

Regions

Nucleotide binding72 – 732ATP By similarity
Nucleotide binding102 – 1054ATP By similarity
Region21 – 255Allosteric activator ADP binding; shared with dimeric partner By similarity
Region125 – 1273Substrate binding By similarity
Region169 – 1713Substrate binding By similarity
Region185 – 1873Allosteric activator ADP binding By similarity
Region214 – 2163Allosteric activator ADP binding By similarity
Region251 – 2544Substrate binding By similarity

Sites

Active site1271Proton acceptor By similarity
Metal binding1031Magnesium; catalytic By similarity
Binding site111ATP; via amide nitrogen By similarity
Binding site1541Allosteric activator ADP By similarity
Binding site1621Substrate; shared with dimeric partner By similarity
Binding site2121Allosteric activator ADP By similarity
Binding site2231Substrate By similarity
Binding site2451Substrate; shared with dimeric partner By similarity

Sequences

Sequence LengthMass (Da)Tools
C0MGJ9 [UniParc].

Last modified May 5, 2009. Version 1.
Checksum: 0C90BC8764FF5AB9

FASTA33735,689
        10         20         30         40         50         60 
MKRIAVLTSG GDAPGMNAAI RAVVRKAISE GMEVYGINRG YAGMVDGDIF PLGSKEVGDK 

        70         80         90        100        110        120 
ISRGGTFLYS ARYPEFAQLE GQLAGIEQLK KHGIEGVVVI GGDGSYHGAM RLTEHGFPAV 

       130        140        150        160        170        180 
GIPGTIDNDI AGTDYTIGFD TAVNTAVEAI DKLRDTSSSH GRTFVVEVMG RNAGDIALWA 

       190        200        210        220        230        240 
GIASGADQII VPEEEFDIHK VVSTIKDDFE NRGKNHHIIV LAEGVMSGEA FAQQLKEAGD 

       250        260        270        280        290        300 
ESDLRVTNLG HILRGGSPTA RDRVIASWMG AHAVELLKEG KGGLAVGIRN EELVESPILG 

       310        320        330 
SAEDGALFSL TDEGNIVVNN PHKARLDYAA LNRSLAQ 

« Hide

References

[1]"Genomic evidence for the evolution of Streptococcus equi: host restriction, increased virulence, and genetic exchange with human pathogens."
Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K., Ainslie F., Jourdan T., Bason N.C., Holroyd N.E., Mungall K., Quail M.A., Sanders M., Simmonds M., Willey D., Brooks K., Aanensen D.M., Spratt B.G., Jolley K.A. expand/collapse author list , Maiden M.C.J., Kehoe M., Chanter N., Bentley S.D., Robinson C., Maskell D.J., Parkhill J., Waller A.S.
PLoS Pathog. 5:E1000346-E1000346(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: H70.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FM204884 Genomic DNA. Translation: CAW99465.1.
RefSeqYP_002744610.1. NC_012470.1.

3D structure databases

ProteinModelPortalC0MGJ9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING553483.SZO_10830.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAW99465; CAW99465; SZO_10830.
GeneID7695043.
KEGGseq:SZO_10830.
PATRIC19651896. VBIStrEqu35012_1145.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000248870.
KOK00850.
OMAYRRGKLH.
OrthoDBEOG644ZRM.

Enzyme and pathway databases

BioCycSEQU40041:GC8B-1167-MONOMER.
UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_00339. Phosphofructokinase_I_B1.
InterProIPR012003. ATP_PFK_prok.
IPR012828. PFKA_ATP.
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.
TIGRFAMsTIGR02482. PFKA_ATP. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePFKA_STRS7
AccessionPrimary (citable) accession number: C0MGJ9
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: May 5, 2009
Last modified: July 9, 2014
This is version 39 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