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E3GPC0 (E3GPC0_EUBLK) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 22. 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:ELI_3072 EMBL ADO38041.1
OrganismEubacterium limosum (strain KIST612) [Complete proteome] [HAMAP] EMBL ADO38041.1
Taxonomic identifier903814 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesEubacteriaceaeEubacterium

Protein attributes

Sequence length318 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 binding71 – 722ATP By similarity HAMAP-Rule MF_00339
Nucleotide binding101 – 1044ATP By similarity HAMAP-Rule MF_00339
Region20 – 245Allosteric activator ADP binding; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Region124 – 1263Substrate binding By similarity HAMAP-Rule MF_00339
Region168 – 1703Substrate binding By similarity HAMAP-Rule MF_00339
Region184 – 1863Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region212 – 2143Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region248 – 2514Substrate binding By similarity HAMAP-Rule MF_00339

Sites

Active site1261Proton acceptor By similarity HAMAP-Rule MF_00339
Metal binding1021Magnesium; catalytic By similarity HAMAP-Rule MF_00339
Binding site101ATP; via amide nitrogen By similarity HAMAP-Rule MF_00339
Binding site1531Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site1611Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Binding site2101Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site2211Substrate By similarity HAMAP-Rule MF_00339
Binding site2421Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
E3GPC0 [UniParc].

Last modified January 11, 2011. Version 1.
Checksum: F1D8463D76CB25F7

FASTA31834,213
        10         20         30         40         50         60 
MKIGILTSGG DAPGMNAAIR AVVRTAIYHK IDVYGINRGY AGLLDKDISP LNVYSVADIL 

        70         80         90        100        110        120 
QKGGTILRTS RSEFFPTEAG QKRAAEVLRE YGIEHLIIIG GDGSLSGALA LKKLGVSVVG 

       130        140        150        160        170        180 
IPGTIDNDFG ASDFTIGFDT AVTTAIEAIG KIRDTTFSHN RINVVQVMGR TCGDIALYAG 

       190        200        210        220        230        240 
FSVGAEALII PEIETNLEGI CDRLLAGKDR GKLHSIVMLA EGCGSYRDYC KKIEELTQVT 

       250        260        270        280        290        300 
TKGTNLGYIQ RGGSPSHFDR NLASFMGYKA VEAIVNDNTG NVVVQRKGEY IMVPLEEALE 

       310 
TPKAFRKDMY KIAKILSI 

« Hide

References

« Hide 'large scale' references
[1]"The genome sequence of Eubacterium limosum (strain KIST612)."
Roh H., Ko H.-J., Kim D., Choi D.G., Park S., Kim S., Kim K.H., Chang I.S., Choi I.-G.
Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KIST612.
[2]Roh H., Ko H.-J., Kim D., Choi D.G., Park S., Kim S., Kim K.H., Chang I.S., Choi I.-G.
Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE.
Strain: KIST612.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002273 Genomic DNA. Translation: ADO38041.1.
RefSeqYP_003961004.1. NC_014624.2.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADO38041; ADO38041; ELI_3072.
GeneID9884969.
KEGGelm:ELI_3072.
PATRIC42608983. VBIEubLim172772_2838.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000248870.
KOK00850.
OMAMELREGH.

Enzyme and pathway databases

BioCycELIM903814:GH0C-3068-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 nameE3GPC0_EUBLK
AccessionPrimary (citable) accession number: E3GPC0
Entry history
Integrated into UniProtKB/TrEMBL: January 11, 2011
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 22 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)