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

B1L9U3 (PFKA_THESQ) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 49. 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:TRQ2_0739
OrganismThermotoga sp. (strain RQ2) [Complete proteome] [HAMAP]
Taxonomic identifier126740 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

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

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

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termAllosteric enzyme
Complete proteome
Gene Ontology (GO)
   Biological_processfructose 6-phosphate metabolic process

Inferred from electronic annotation. Source: InterPro

glycolytic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_component6-phosphofructokinase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_function6-phosphofructokinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 319319ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_00339
PRO_1000120066

Regions

Nucleotide binding72 – 732ATP By similarity
Nucleotide binding102 – 1054ATP By similarity
Region21 – 255Allosteric activator ADP binding; shared with dimeric partner By similarity
Region126 – 1283Substrate binding By similarity
Region170 – 1723Substrate binding By similarity
Region186 – 1883Allosteric activator ADP binding By similarity
Region214 – 2163Allosteric activator ADP binding By similarity
Region250 – 2534Substrate binding By similarity

Sites

Active site1281Proton acceptor By similarity
Metal binding1031Magnesium; catalytic By similarity
Binding site111ATP; via amide nitrogen By similarity
Binding site1551Allosteric activator ADP By similarity
Binding site1631Substrate; shared with dimeric partner By similarity
Binding site2121Allosteric activator ADP By similarity
Binding site2231Substrate By similarity
Binding site2441Substrate; shared with dimeric partner By similarity

Sequences

Sequence LengthMass (Da)Tools
B1L9U3 [UniParc].

Last modified April 29, 2008. Version 1.
Checksum: 3809E961382712B8

FASTA31934,479
        10         20         30         40         50         60 
MKKIAVLTSG GDAPGMNAAV RAVVRYGVRQ GLEVIGVRRG YSGLIDGDFV KLEYKDVAGI 

        70         80         90        100        110        120 
TEKGGTILRT SRCEEFKTEE GRELAAKQIK KHGIEGLVVI GGEGSLTGAH LLYEEHKIPV 

       130        140        150        160        170        180 
VGIPATIDND IGLTDMCIGV DTCLNTVMDA VQKLKDTASS HERAFIVEVM GRHSGYIALM 

       190        200        210        220        230        240 
AGLVTGAEAI IVPEIPVDYS QLADRILEER RRGKINSIII VAEGAASAYT VARHLEYRIG 

       250        260        270        280        290        300 
YETRITILGH VQRGGSPTAF DRRLALSMGV EAVDALLDGE VDVMIALQGN KLVRVPIMEA 

       310 
LSTKKTIDKK LYEIAYMLS 

« Hide

References

[1]"Complete sequence of Thermotoga sp. RQ2."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Bruce D.B., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.
Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RQ2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000969 Genomic DNA. Translation: ACB09091.1.
RefSeqYP_001738774.1. NC_010483.1.

3D structure databases

ProteinModelPortalB1L9U3.
SMRB1L9U3. Positions 1-319.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING126740.TRQ2_0739.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB09091; ACB09091; TRQ2_0739.
GeneID6092156.
KEGGtrq:TRQ2_0739.
PATRIC23948028. VBITheSp108950_0751.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000248870.
KOK00850.
OMAGFGGRCV.
OrthoDBEOG644ZRM.

Enzyme and pathway databases

BioCycTSP126740:GH49-757-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_THESQ
AccessionPrimary (citable) accession number: B1L9U3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: April 29, 2008
Last modified: July 9, 2014
This is version 49 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