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I6T1F7 (I6T1F7_ENTHA) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 18. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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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:EHR_14015 EMBL AFM71652.1
ORF Names:I584_01369 EMBL EOU05472.1, UAE_02067 EMBL EOH69574.1
OrganismEnterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258) [Complete proteome] [HAMAP] EMBL AFM71652.1
Taxonomic identifier768486 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliLactobacillalesEnterococcaceaeEnterococcus

Protein attributes

Sequence length320 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. SAAS SAAS022953 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. SAAS SAAS012828 HAMAP-Rule MF_00339

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00339

Subcellular location

Cytoplasm By similarity SAAS SAAS022953 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. HAMAP-Rule MF_00339

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding72 – 732ATP By similarity HAMAP-Rule MF_00339
Nucleotide binding102 – 1054ATP By similarity HAMAP-Rule MF_00339
Region21 – 255Allosteric activator ADP binding; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Region125 – 1273Substrate binding By similarity HAMAP-Rule MF_00339
Region169 – 1713Substrate binding By similarity HAMAP-Rule MF_00339
Region185 – 1873Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region213 – 2153Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region249 – 2524Substrate binding By similarity HAMAP-Rule MF_00339

Sites

Active site1271Proton acceptor By similarity HAMAP-Rule MF_00339
Metal binding1031Magnesium; catalytic By similarity HAMAP-Rule MF_00339
Binding site111ATP; via amide nitrogen By similarity HAMAP-Rule MF_00339
Binding site1541Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site1621Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Binding site2111Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site2221Substrate By similarity HAMAP-Rule MF_00339
Binding site2431Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
I6T1F7 [UniParc].

Last modified October 3, 2012. Version 1.
Checksum: 6FCD34771774AFE2

FASTA32034,236
        10         20         30         40         50         60 
MKRIGILTSG GDAPGMNAAI RAVVRKGIYE GLEVYGINYG FAGLVAGDIR RLDVADVGDK 

        70         80         90        100        110        120 
IQRGGTFLYS ARYPEFATEE GQLKGIEQLK KFGIEGLVVI GGDGSYHGAM ALTRRGFPAV 

       130        140        150        160        170        180 
GVPGTIDNDI PGTDFTIGFD TAINTVLESI DRIRDTATSH VRTFVIEVMG RNAGDIALWS 

       190        200        210        220        230        240 
GVAGGADEII IPEHDFDMAS VAKKIQEGRD RGKKHCLIIL AEGVMGGNEF AEKLSEYGDY 

       250        260        270        280        290        300 
HTRVSILGHV VRGGSPSARD RVLASKFGAY AVDLLRAGKG GLCVGIRDNE MVAADIIETL 

       310        320 
ESNKHKPDLS LYDLNNSLSF 

« Hide

References

« Hide 'large scale' references
[1]"Genome sequence of Enterococcus hirae (Streptococcus faecalis) ATCC 9790, a model organism for the study of ion transport, bioenergetics, and copper homeostasis."
Gaechter T., Wunderlin C., Schmidheini T., Solioz M.
J. Bacteriol. 194:5126-5127(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9790 EMBL AFM71652.1 and ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258.
[2]"The Genome Sequence of Enterococcus hirae ATCC_8043."
The Broad Institute Genome Sequencing Platform, The Broad Institute Genome Sequencing Center for Infectious Disease
Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A., Gujja S. expand/collapse author list , Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C., Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.
Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ATCC 9790 EMBL EOH69574.1.
[3]"The Genome Sequence of Enterococcus hirae ATCC_8043 (PacBio/Illumina hybrid assembly)."
The Broad Institute Genomics Platform, The Broad Institute Genome Sequencing Center for Infectious Disease
Earl A., Russ C., Gilmore M., Surin D., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J. expand/collapse author list , Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.
Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: ATCC 9790 EMBL EOU05472.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP003504 Genomic DNA. Translation: AFM71652.1.
AJAI01000018 Genomic DNA. Translation: EOH69574.1.
ASVZ01000002 Genomic DNA. Translation: EOU05472.1.
RefSeqYP_006488543.1. NC_018081.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAFM71652; AFM71652; EHR_14015.
EOH69574; EOH69574; UAE_02067.
EOU05472; EOU05472; I584_01369.
GeneID13176784.
KEGGehr:EHR_14015.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00850.

Enzyme and pathway databases

BioCycEHIR768486:GLCW-2747-MONOMER.
UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_00339. Phosphofructokinase.
InterProIPR012003. ATP_PFK_prok.
IPR012828. PFKA_ATP.
IPR022953. Phosphofructokinase.
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.
ProtoNetSearch...

Entry information

Entry nameI6T1F7_ENTHA
AccessionPrimary (citable) accession number: I6T1F7
Entry history
Integrated into UniProtKB/TrEMBL: October 3, 2012
Last sequence update: October 3, 2012
Last modified: July 9, 2014
This is version 18 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)