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E0REK9 (E0REK9_PAEP6) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 21. 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
Ordered Locus Names:PPE_01700 EMBL ADM69537.1
OrganismPaenibacillus polymyxa (strain E681) [Complete proteome] [HAMAP] EMBL ADM69537.1
Taxonomic identifier349520 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPaenibacillaceaePaenibacillus

Protein attributes

Sequence length323 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 binding75 – 762ATP By similarity HAMAP-Rule MF_00339
Nucleotide binding105 – 1084ATP By similarity HAMAP-Rule MF_00339
Region24 – 285Allosteric activator ADP binding; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Region128 – 1303Substrate binding By similarity HAMAP-Rule MF_00339
Region172 – 1743Substrate binding By similarity HAMAP-Rule MF_00339
Region188 – 1903Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region216 – 2183Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region253 – 2564Substrate binding By similarity HAMAP-Rule MF_00339

Sites

Active site1301Proton acceptor By similarity HAMAP-Rule MF_00339
Metal binding1061Magnesium; catalytic By similarity HAMAP-Rule MF_00339
Binding site141ATP; via amide nitrogen By similarity HAMAP-Rule MF_00339
Binding site1571Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site1651Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Binding site2251Substrate By similarity HAMAP-Rule MF_00339
Binding site2471Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
E0REK9 [UniParc].

Last modified November 2, 2010. Version 1.
Checksum: C9F3B9567613A0BC

FASTA32334,892
        10         20         30         40         50         60 
MTAVKKIAVL TSGGDSQGMN AAVRAVVRSG LYFGLEVFGI QRGYQGLLND DIFPMDLRSV 

        70         80         90        100        110        120 
GDIIQRGGTV LQSARCLEFT TEEGQKKGAQ ILRDRGIDGV VVIGGDGSYQ GANKLTKQGI 

       130        140        150        160        170        180 
KTMCLPGTID NDISFTDYTI GFDTAVSIVV DAINKLRDTM SSHERSSIVE VMGRHCGDIA 

       190        200        210        220        230        240 
LHAGLASGAE TILVPEVEFD LNEVSDRMKQ NFKHGKRHSI IIVAEGVGKG ENVAQVIQEN 

       250        260        270        280        290        300 
CPDYEPRVTV LGHIQRGGTP TAFDRNLASR LGDFAVRQLI EGVSDKACGT IDGKLVATDI 

       310        320 
DKVVNTKKDF NMELYELALR LSQ 

« Hide

References

[1]"Genome sequence of the polymyxin-producing plant-probiotic rhizobacterium Paenibacillus polymyxa E681."
Kim J.F., Jeong H., Park S.Y., Kim S.B., Park Y.K., Choi S.K., Ryu C.M., Hur C.G., Ghim S.Y., Oh T.K., Kim J.J., Park C.S., Park S.H.
J. Bacteriol. 192:6103-6104(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E681 EMBL ADM69537.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000154 Genomic DNA. Translation: ADM69537.1.
RefSeqYP_003870075.1. NC_014483.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADM69537; ADM69537; PPE_01700.
GeneID9774453.
KEGGppy:PPE_01700.
PATRIC42409090. VBIPaePol94484_1686.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000248870.
KOK00850.
OMAYRRGKLH.

Enzyme and pathway databases

BioCycPPOL349520:GH6J-1694-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 nameE0REK9_PAEP6
AccessionPrimary (citable) accession number: E0REK9
Entry history
Integrated into UniProtKB/TrEMBL: November 2, 2010
Last sequence update: November 2, 2010
Last modified: July 9, 2014
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)