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P21777 (PFKA1_THET8) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 107. 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 1

Short name=ATP-PFK 1
Short name=Phosphofructokinase 1
EC=2.7.1.11
Alternative name(s):
Phosphohexokinase 1
Gene names
Name:pfkA
Ordered Locus Names:TTHA1962
OrganismThermus thermophilus (strain HB8 / ATCC 27634 / DSM 579) [Reference proteome] [HAMAP]
Taxonomic identifier300852 [NCBI]
Taxonomic lineageBacteriaDeinococcus-ThermusDeinococciThermalesThermaceaeThermus

Protein attributes

Sequence length322 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.4 Ref.5

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. Ref.4 Ref.5

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00339

Enzyme regulation

Allosterically activated by ADP and other diphosphonucleosides By similarity. Allosterically inhibited by phosphoenolpyruvate which induces the dissociation of the active tetramer into an inactive two-subunit forms. Ref.4

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.5

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=0.08 mM for ATP Ref.4

KM=0.025 mM for fructose 6-phosphate

pH dependence:

Optimum pH is 8.4.

Temperature dependence:

Optimum temperature is 85 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 322322ATP-dependent 6-phosphofructokinase 1 HAMAP-Rule MF_00339
PRO_0000112001

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
Region252 – 2554Substrate 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 site2461Substrate; shared with dimeric partner By similarity

Experimental info

Sequence conflict1111C → F in AAA27501. Ref.1
Sequence conflict2731A → P in AAA27501. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P21777 [UniParc].

Last modified March 29, 2005. Version 3.
Checksum: 608CD4053E6ACEA3

FASTA32233,537
        10         20         30         40         50         60 
MKRIGVFTSG GDAPGMNAAI RAVVRQAHAL GVEVIGIRRG YAGMIQGEMV PLGVRDVANI 

        70         80         90        100        110        120 
IQRGGTILLT ARSQEFLTEE GRAKAYAKLQ AAGIEGLVAI GGDGTFRGAL CLVEEHGMPV 

       130        140        150        160        170        180 
VGVPGTIDND LYGTDYTIGF DTAVNTALEA IDRIRDTAAS HERVFFIEVM GRHAGFIALD 

       190        200        210        220        230        240 
VGLAGGAEVI AVPEEPVDPK AVAEVLEASQ RRGKKSSIVV VAEGAYPGGA AGLLAAIREH 

       250        260        270        280        290        300 
LQVEARVTVL GHIQRGGSPT AKDRILASRL GAAAVEALVG GASGVMVGEV EGEVDLTPLK 

       310        320 
EAVERRKDIN RALLRLSQVL AL 

« Hide

References

« Hide 'large scale' references
[1]"Molecular cloning of phosphofructokinase 1 gene from a thermophilic bacterium, Thermus thermophilus."
Xu J., Seki M., Denda K., Yoshida M.
Biochem. Biophys. Res. Commun. 176:1313-1318(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Complete genome sequence of Thermus thermophilus HB8."
Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T., Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: HB8 / ATCC 27634 / DSM 579.
[3]"Phosphoenolpyruvate-insensitive phosphofructokinase isozyme from Thermus thermophilus HB8."
Xu J., Oshima T., Yoshida M.
J. Biochem. 109:199-203(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-25.
[4]"Allosteric nature of thermostable phosphofructokinase from an extreme thermophilic bacterium."
Yoshida M.
Biochemistry 11:1087-1093(1972) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
Strain: HB8 / ATCC 27634 / DSM 579.
[5]"Tetramer-dimer conversion of phosphofructokinase from Thermus thermophilus induced by its allosteric effectors."
Xu J., Oshima T., Yoshida M.
J. Mol. Biol. 215:597-606(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
Strain: HB8 / ATCC 27634 / DSM 579.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M71213 Genomic DNA. Translation: AAA27501.1.
AP008226 Genomic DNA. Translation: BAD71785.1.
RefSeqYP_145228.1. NC_006461.1.

3D structure databases

ProteinModelPortalP21777.
SMRP21777. Positions 1-321.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300852.TTHA1962.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD71785; BAD71785; BAD71785.
GeneID3169721.
KEGGttj:TTHA1962.
PATRIC23958903. VBITheThe93045_1933.

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000248869.
KOK00850.
OMAYRRGKLH.
OrthoDBEOG644ZRM.
PhylomeDBP21777.

Enzyme and pathway databases

BioCycTTHE300852:GH8R-2012-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 namePFKA1_THET8
AccessionPrimary (citable) accession number: P21777
Secondary accession number(s): Q5SGW8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: March 29, 2005
Last modified: July 9, 2014
This is version 107 of the entry and version 3 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