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G7ZP92 (G7ZP92_STAAU) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 16. 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
ORF Names:SAMSHR1132_15490 EMBL CCE59390.1
OrganismStaphylococcus aureus subsp. aureus MSHR1132 [Complete proteome] EMBL CCE59390.1
Taxonomic identifier985002 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesStaphylococcus

Protein attributes

Sequence length322 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. SAAS SAAS022953 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 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
Region21 – 255Allosteric activator ADP binding; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Region127 – 1293Substrate binding By similarity HAMAP-Rule MF_00339
Region171 – 1733Substrate binding By similarity HAMAP-Rule MF_00339
Region187 – 1893Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region215 – 2173Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region251 – 2544Substrate binding By similarity HAMAP-Rule MF_00339

Sites

Active site1291Proton 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 site1561Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site1641Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Binding site2131Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site2241Substrate By similarity HAMAP-Rule MF_00339
Binding site2451Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
G7ZP92 [UniParc].

Last modified January 25, 2012. Version 1.
Checksum: AA11B2DA8D59793A

FASTA32234,840
        10         20         30         40         50         60 
MKKIAVLTSG GDSPGMNAAV RAVVRTAIYN EIEVYGVYHG YQGLLNDDIH KLELGSVGDT 

        70         80         90        100        110        120 
IQRGGTFLYS ARCPEFKEQE VRKVAIENLR KRGIEGLVVI GGDGSYRGAQ RISEECKEIQ 

       130        140        150        160        170        180 
TIGIPGTIDN DINGTDFTIG FDTALNTIIG LVDKIRDTAS SHARTFIIEA MGRDCGDLAL 

       190        200        210        220        230        240 
WAGLSVGAET IVVPEVKTDI KEIADKIEQG IKRGKKHSIV LVAEGCMTAQ ECQKELSEYI 

       250        260        270        280        290        300 
NVDNRVSVLG HVQRGGSPTG ADRVLASRLG GFAVDLLMEG ETAKGVGIKN NKIVATSFDE 

       310        320 
IFDGKDHKFD YSLYELANKL SI 

« Hide

References

[1]"A very early-branching Staphylococcus aureus lineage lacking the carotenoid pigment staphyloxanthin."
Holt D.C., Holden M.T., Tong S.Y., Castillo-Ramirez S., Clarke L., Quail M.A., Currie B.J., Parkhill J., Bentley S.D., Feil E.J., Giffard P.M.
Genome Biol. Evol. 3:881-895(2011)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MSHR1132 EMBL CCE59390.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
FR821777 Genomic DNA. Translation: CCE59390.1.
RefSeqYP_005326059.1. NC_016941.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCCE59390; CCE59390; SAMSHR1132_15490.
GeneID11931668.
KEGGsuh:SAMSHR1132_15490.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00850.

Enzyme and pathway databases

BioCycSAUR985002:GLKP-1584-MONOMER.
UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_00339. Phosphofructokinase.
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 nameG7ZP92_STAAU
AccessionPrimary (citable) accession number: G7ZP92
Entry history
Integrated into UniProtKB/TrEMBL: January 25, 2012
Last sequence update: January 25, 2012
Last modified: July 9, 2014
This is version 16 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)