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E4SPH7 (E4SPH7_STRTN) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 19. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_00339

Short name=ATP-PFK HAMAP-Rule MF_00339
Short name=Phosphofructokinase HAMAP-Rule MF_00339
EC=2.7.1.11 HAMAP-Rule MF_00339
Alternative name(s):
Phosphohexokinase HAMAP-Rule MF_00339
Gene names
Name:pfkA HAMAP-Rule MF_00339
Ordered Locus Names:STND_1133 EMBL ADQ63175.1
OrganismStreptococcus thermophilus (strain ND03) [Complete proteome] [HAMAP] EMBL ADQ63175.1
Taxonomic identifier767463 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus

Protein attributes

Sequence length339 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 SAAS SAAS022953

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 SAAS SAAS012828

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00339

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00339 SAAS SAAS022953.

Sequence similarities

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade "B1" sub-subfamily. HAMAP-Rule MF_00339

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding72 – 732ATP By similarity HAMAP-Rule MF_00339
Nucleotide binding102 – 1054ATP By similarity HAMAP-Rule MF_00339
Region125 – 1273Substrate binding By similarity HAMAP-Rule MF_00339
Region169 – 1713Substrate binding By similarity HAMAP-Rule MF_00339
Region185 – 1873Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region214 – 2163Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region251 – 2544Substrate binding By similarity HAMAP-Rule MF_00339

Sites

Active site1271Proton acceptor By similarity HAMAP-Rule MF_00339
Metal binding1031Magnesium; catalytic By similarity HAMAP-Rule MF_00339
Binding site111ATP; via amide nitrogen By similarity HAMAP-Rule MF_00339
Binding site1621Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Binding site2231Substrate By similarity HAMAP-Rule MF_00339
Binding site2451Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
E4SPH7 [UniParc].

Last modified February 8, 2011. Version 1.
Checksum: 492DF7076EC443DC

FASTA33935,982
        10         20         30         40         50         60 
MKRIAVLTSG GDAPGMNAAV RAVVLKAISE GIEVFGINRG YAGMVEGDIF KLDAKRVENI 

        70         80         90        100        110        120 
LSRGGTFLQS ARYPEFAQLE GQLKGIEQLK KYGIEGVVVI GGDGSYHGAM RLTEHGFPAV 

       130        140        150        160        170        180 
GLPGTIDNDI VGTDYTIGFD TAVATATEAL DKIQDTAFSH GRTFVVEVMG RNAGDIALWA 

       190        200        210        220        230        240 
GIASGADQII VPEEEYDINE VVRKVKEGYE SGEKSHHIIV LAEGVMGAEE FAAKMKEAGD 

       250        260        270        280        290        300 
TSDLRATNLG HVIRGGSPTA RDRVLASWMG AHAVDLLKEG IGGVAVGIHN EQLVESPILG 

       310        320        330 
TAEEGALFSL TEDGKIIVNN PHKARLDFAE LNRSLANLK 

« Hide

References

[1]"Complete genome sequence of Streptococcus thermophilus strain ND03."
Sun Z., Chen X., Wang J., Zhao W., Shao Y., Wu L., Zhou Z., Sun T., Wang L., Meng H., Zhang H., Chen W.
J. Bacteriol. 193:793-794(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ND03 EMBL ADQ63175.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002340 Genomic DNA. Translation: ADQ63175.1.
RefSeqYP_006002679.1. NC_017563.1.

3D structure databases

ProteinModelPortalE4SPH7.
SMRE4SPH7. Positions 1-304.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADQ63175; ADQ63175; STND_1133.
GeneID12591289.
KEGGstn:STND_1133.
PATRIC43255790. VBIStrThe160185_1211.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00850.

Enzyme and pathway databases

BioCycSTHE767463:GLLS-1189-MONOMER.
UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_00339. Phosphofructokinase.
InterProIPR012003. ATP_PFK_prok.
IPR012828. PFKA_ATP.
IPR022953. Phosphofructokinase.
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.
ProtoNetSearch...

Entry information

Entry nameE4SPH7_STRTN
AccessionPrimary (citable) accession number: E4SPH7
Entry history
Integrated into UniProtKB/TrEMBL: February 8, 2011
Last sequence update: February 8, 2011
Last modified: July 9, 2014
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)