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Q9WY52 (PFKA_THEMA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 97. 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:TM_0209
OrganismThermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099) [Reference proteome] [HAMAP]
Taxonomic identifier243274 [NCBI]
Taxonomic lineageBacteriaThermotogaeThermotogalesThermotogaceaeThermotoga

Protein attributes

Sequence length319 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Ref.2 Ref.3

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. Ref.2 Ref.3

Cofactor

Magnesium. Can partially be replaced by manganese and iron. Ref.2

Enzyme regulation

Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate. Strongly inhibited by diphosphate, triphosphate and polyphosphate. Ref.2

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_00339

Subunit structure

Homotetramer. Ref.2 Ref.3

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.

Biophysicochemical properties

Kinetic parameters:

KM=0.2 mM for ATP (at 75 degrees Celsius) Ref.2 Ref.3

KM=7.6 mM for fructose 1,6-bisphosphate (at 75 degrees Celsius)

KM=1.4 mM for ADP (at 75 degrees Celsius)

Vmax=360 µmol/min/mg enzyme for the forward reaction (at 75 degrees Celsius)

Vmax=432 µmol/min/mg enzyme for the forward reaction (at 50 degrees Celsius)

Vmax=13 µmol/min/mg enzyme for the reverse reaction (at 75 degrees Celsius)

pH dependence:

Optimum pH is 6.7.

Temperature dependence:

Optimum temperature is 93 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 319319ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_00339
PRO_0000112000

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

Experimental info

Sequence conflict21K → R AA sequence Ref.2
Sequence conflict14 – 174PGMN → GPM AA sequence Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9WY52 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 3809E971288D12B8

FASTA31934,487
        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 KFVRVPIMEA 

       310 
LSTKKTIDKK LYEIAHMLS 

« Hide

References

« Hide 'large scale' references
[1]"Evidence for lateral gene transfer between Archaea and Bacteria from genome sequence of Thermotoga maritima."
Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A., Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M., Cotton M.D., Pratt M.S. expand/collapse author list , Phillips C.A., Richardson D.L., Heidelberg J.F., Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Nature 399:323-329(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[2]"ATP-dependent 6-phosphofructokinase from the hyperthermophilic bacterium Thermotoga maritima: characterization of an extremely thermophilic, allosterically regulated enzyme."
Hansen T., Musfeldt M., Schonheit P.
Arch. Microbiol. 177:401-409(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-39, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, ENZYME REGULATION.
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.
[3]"Thermotoga maritima phosphofructokinases: expression and characterization of two unique enzymes."
Ding Y.R., Ronimus R.S., Morgan H.W.
J. Bacteriol. 183:791-794(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT.
Strain: ATCC 43589 / MSB8 / DSM 3109 / JCM 10099.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000512 Genomic DNA. Translation: AAD35301.1.
PIRC72406.
RefSeqNP_228024.1. NC_000853.1.
YP_007976558.1. NC_021214.1.
YP_008990817.1. NC_023151.1.

3D structure databases

ProteinModelPortalQ9WY52.
SMRQ9WY52. Positions 1-319.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243274.TM0209.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD35301; AAD35301; TM_0209.
GeneID897081.
KEGGtma:TM0209.
tmi:THEMA_03680.
tmm:Tmari_0207.
PATRIC23935290. VBITheMar51294_0211.

Phylogenomic databases

eggNOGCOG0205.
KOK00850.
OMAGFGGRCV.
OrthoDBEOG644ZRM.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-363.
SABIO-RKQ9WY52.
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_THEMA
AccessionPrimary (citable) accession number: Q9WY52
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: November 1, 1999
Last modified: July 9, 2014
This is version 97 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