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Q8DJB1 (PFKA_THEEB) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 70. 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:tll1316
OrganismThermosynechococcus elongatus (strain BP-1) [Reference proteome] [HAMAP]
Taxonomic identifier197221 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesThermosynechococcus

Protein attributes

Sequence length369 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_01976

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_01976

Cofactor

Magnesium By similarity. HAMAP-Rule MF_01976

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_01976

Subunit structure

Homodimer or homotetramer By similarity. HAMAP-Rule MF_01976

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_01976.

Sequence similarities

Belongs to the phosphofructokinase type A (PFKA) family. Mixed-substrate PFK group III subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 369369ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_01976
PRO_0000111997

Regions

Nucleotide binding81 – 822ATP By similarity
Nucleotide binding108 – 1114ATP By similarity
Region132 – 1343Substrate binding By similarity
Region176 – 1783Substrate binding By similarity
Region272 – 2754Substrate binding By similarity

Sites

Active site1341Proton acceptor By similarity
Metal binding1091Magnesium; catalytic By similarity
Binding site151ATP; via amide nitrogen By similarity
Binding site1691Substrate; shared with dimeric partner By similarity
Binding site2301Substrate By similarity
Binding site2661Substrate; shared with dimeric partner By similarity
Site1101Important for substrate specificity; cannot use PPi as phosphoryl donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8DJB1 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: 2FE4A8C249105916

FASTA36939,271
        10         20         30         40         50         60 
MSSSRKRLGV FTSGGDCPGL NTAIRAIVAH ATLSYGWEVL GILHATQGLI ERKAIPLNAE 

        70         80         90        100        110        120 
GLGGMDVLLN MGGTILGAIN KGDTLGHADE VIAGYYELGL DALIAICGDG SLRILHQLAQ 

       130        140        150        160        170        180 
KGNWNFLAIP KTIDNDVALT DRAIGFDTAV NTVVEALNRI TSTAASHDRV FVVEVMGRTA 

       190        200        210        220        230        240 
GHLALYSGIA GGADIILIPE IPYSIEGICQ HLQKLRDRWG RQFALIVVAE GSKQLEEDAN 

       250        260        270        280        290        300 
HPRHCSIGQY IADKIAQHSP IPIELRVSVL GHIQRGGAPM AMDRLLAAGM GNTAVDLAAQ 

       310        320        330        340        350        360 
GTFGRMVAWQ AGQVVTVPIA DVVAKCPRHV DPNSFLIRTA QGLGIYVGDK PMLPYVDPTL 


CRDQVICAI 

« Hide

References

[1]"Complete genome structure of the thermophilic cyanobacterium Thermosynechococcus elongatus BP-1."
Nakamura Y., Kaneko T., Sato S., Ikeuchi M., Katoh H., Sasamoto S., Watanabe A., Iriguchi M., Kawashima K., Kimura T., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Sugimoto M. expand/collapse author list , Takeuchi C., Yamada M., Tabata S.
DNA Res. 9:123-130(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BP-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000039 Genomic DNA. Translation: BAC08868.1.
RefSeqNP_682106.1. NC_004113.1.

3D structure databases

ProteinModelPortalQ8DJB1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING197221.tll1316.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAC08868; BAC08868; BAC08868.
GeneID1012416.
KEGGtel:tll1316.
PATRIC23927976. VBITheElo119873_1384.

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000248869.
KOK00850.
OMARGDFGRM.
OrthoDBEOG644ZRM.

Enzyme and pathway databases

UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_01976. Phosphofructokinase_III.
InterProIPR012003. ATP_PFK_prok.
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.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePFKA_THEEB
AccessionPrimary (citable) accession number: Q8DJB1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: March 1, 2003
Last modified: July 9, 2014
This is version 70 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