Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q8DQ85 (PFKA_STRR6) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 73. 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:spr0796
OrganismStreptococcus pneumoniae (strain ATCC BAA-255 / R6) [Reference proteome] [HAMAP]
Taxonomic identifier171101 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length335 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 335335ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_00339
PRO_0000111991

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
Region213 – 2153Allosteric activator ADP binding By similarity
Region250 – 2534Substrate 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 site2221Substrate By similarity
Binding site2441Substrate; shared with dimeric partner By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DQ85 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 930324A2307FFC6F

FASTA33535,213
        10         20         30         40         50         60 
MKRIAVLTSG GDAPGMNAAI RAVVRQAISE GMEVFGIYDG YAGMVAGEIH PLDAASVGDI 

        70         80         90        100        110        120 
ISRGGTFLHS ARYPEFAQLE GQLKGIEQLK KHGIEGVVVI GGDGSYHGAM RLTEHGFPAI 

       130        140        150        160        170        180 
GLPGTIDNDI VGTDFTIGFD TAVTTAMDAI DKIRDTSSSH RRTFVIEVMG RNAGDIALWA 

       190        200        210        220        230        240 
GIATGADEII IPEAGFKMED IVASIKAGYE CGKKHNIIVL AEGVMSAAEF GQKLKEAGDI 

       250        260        270        280        290        300 
SDLRVTELGH IQRGGSPTPR DRVLASRMGA HAVKLLKEGI GGVAVGIRNE KMVENPILGT 

       310        320        330 
AEEGALFSLT AEGKIVVNNP HEADIELSSL NKSLS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE007317 Genomic DNA. Translation: AAK99600.1.
PIRD97971.
RefSeqNP_358390.1. NC_003098.1.

3D structure databases

ProteinModelPortalQ8DQ85.
SMRQ8DQ85. Positions 1-335.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING171101.spr0796.

Proteomic databases

PRIDEQ8DQ85.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK99600; AAK99600; spr0796.
GeneID934334.
KEGGspr:spr0796.
PATRIC19701529. VBIStrPne107296_0883.

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000248870.
KOK00850.
OMAYRRGKLH.
OrthoDBEOG644ZRM.

Enzyme and pathway databases

BioCycSPNE171101:GJC8-807-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_STRR6
AccessionPrimary (citable) accession number: Q8DQ85
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 73 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