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P0DD03 (PFKA_STRPQ) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 22. 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
Synonyms:pfk
Ordered Locus Names:SPs1112
OrganismStreptococcus pyogenes serotype M3 (strain SSI-1) [Complete proteome] [HAMAP]
Taxonomic identifier193567 [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_0000411439

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
P0DD03 [UniParc].

Last modified July 27, 2011. Version 1.
Checksum: 8099570A8BF38125

FASTA33735,762
        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 VPEEEFDIEK VASTIQYDFE HKGKNHHIIV LAEGVMSGEA FAQKLKEAGD 

       250        260        270        280        290        300 
KSDLRVTNLG HILRGGSPTA RDRVIASWMG SHAVELLKEG KGGLAVGIHN EELVESPILG 

       310        320        330 
TAEEGALFSL TEEGQIIVNN PHKARLDFAA LNRSLSQ 

« Hide

References

[1]"Genome sequence of an M3 strain of Streptococcus pyogenes reveals a large-scale genomic rearrangement in invasive strains and new insights into phage evolution."
Nakagawa I., Kurokawa K., Yamashita A., Nakata M., Tomiyasu Y., Okahashi N., Kawabata S., Yamazaki K., Shiba T., Yasunaga T., Hayashi H., Hattori M., Hamada S.
Genome Res. 13:1042-1055(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SSI-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000034 Genomic DNA. Translation: BAC64207.1.
RefSeqNP_802374.1. NC_004606.1.

3D structure databases

ProteinModelPortalP0DD03.
SMRP0DD03. Positions 1-298.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC64207; BAC64207; BAC64207.
GeneID1065432.
KEGGsps:SPs1112.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000248870.
KOK00850.
OMAYRRGKLH.
OrthoDBEOG644ZRM.

Enzyme and pathway databases

BioCycSPYO193567:GHDO-1168-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_STRPQ
AccessionPrimary (citable) accession number: P0DD03
Secondary accession number(s): Q8K7A2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 27, 2011
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 22 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