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

D9S2K5 (D9S2K5_THEOJ) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 24. 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 EMBL ADL07632.1
Ordered Locus Names:Toce_0870 EMBL ADL07632.1
OrganismThermosediminibacter oceani (strain ATCC BAA-1034 / DSM 16646 / JW/IW-1228P) [Complete proteome] [HAMAP] EMBL ADL07632.1
Taxonomic identifier555079 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisThermosediminibacter

Protein attributes

Sequence length319 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
Region21 – 255Allosteric activator ADP binding; shared with dimeric partner 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
Region213 – 2153Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region249 – 2524Substrate 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 site1541Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site1621Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Binding site2111Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site2221Substrate By similarity HAMAP-Rule MF_00339
Binding site2431Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
D9S2K5 [UniParc].

Last modified October 5, 2010. Version 1.
Checksum: 43F266758F2DD5F6

FASTA31934,238
        10         20         30         40         50         60 
MKRIGILTSG GDAPGMNAAI RAVVRSGIYN DMEVYGIRRG YAGLINGDFV KMDLGSVGDI 

        70         80         90        100        110        120 
IHRGGTILRT ARSEEFKTPE GMEKALKNIE ALGLEGLVVI GGDGSFRGAI ELSKRGVATI 

       130        140        150        160        170        180 
GIPGTIDNDI PFTDYSIGFD TAVNTVVEAV NKIRDTATSH ERTFIIEVMG RESGNLALYS 

       190        200        210        220        230        240 
GVACGAETIL VPEMPFTIKD VCEKIMSGFR RGKLHSIIIL AEGAGQGFDV GREIKNITGF 

       250        260        270        280        290        300 
ETRIIVLGHL QRGGTPTAFD RILASQMGGK AVELLKSGVS NKMVGWVKGE LLVTDLEQIL 

       310 
TTNKPFNMEL YELANILSI 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002131 Genomic DNA. Translation: ADL07632.1.
RefSeqYP_003825255.1. NC_014377.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADL07632; ADL07632; Toce_0870.
GeneID9510506.
KEGGtoc:Toce_0870.
PATRIC42456868. VBITheOce34679_0944.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000248869.
KOK00850.
OMAGFGGRCV.

Enzyme and pathway databases

BioCycTOCE555079:GHIS-879-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 nameD9S2K5_THEOJ
AccessionPrimary (citable) accession number: D9S2K5
Entry history
Integrated into UniProtKB/TrEMBL: October 5, 2010
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 24 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)