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E3DPE1 (E3DPE1_HALPG) Unreviewed, UniProtKB/TrEMBL

Last modified July 9, 2014. Version 19. 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:Hprae_1576 EMBL ADO77703.1
OrganismHalanaerobium praevalens (strain ATCC 33744 / DSM 2228 / GSL) [Complete proteome] [HAMAP] EMBL ADO77703.1
Taxonomic identifier572479 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaHalanaerobialesHalanaerobiaceaeHalanaerobium

Protein attributes

Sequence length332 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 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
Region126 – 1283Substrate binding By similarity HAMAP-Rule MF_00339
Region170 – 1723Substrate binding By similarity HAMAP-Rule MF_00339
Region186 – 1883Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region214 – 2163Allosteric activator ADP binding By similarity HAMAP-Rule MF_00339
Region262 – 2654Substrate binding By similarity HAMAP-Rule MF_00339

Sites

Active site1281Proton 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 site1551Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site1631Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339
Binding site2121Allosteric activator ADP By similarity HAMAP-Rule MF_00339
Binding site2231Substrate By similarity HAMAP-Rule MF_00339
Binding site2561Substrate; shared with dimeric partner By similarity HAMAP-Rule MF_00339

Sequences

Sequence LengthMass (Da)Tools
E3DPE1 [UniParc].

Last modified January 11, 2011. Version 1.
Checksum: B5F5F07AA87ABDBA

FASTA33235,824
        10         20         30         40         50         60 
MKKIAVLTSG GDAPGMNPAI RSVVRTAIYH GLEVVGIRHG YKGLIEKDFF PMKRGSVADI 

        70         80         90        100        110        120 
VQRGGTILLS ARCEEFKTEA GRKKAYANMQ EEGIDGLVVI GGDGSLRGVQ KINAESDIKA 

       130        140        150        160        170        180 
VGIPGTIDND LACTDYTIGV DTAMNTIVEA INKIRDTATS HERTFVIECM GRDSGYLALM 

       190        200        210        220        230        240 
TGLAGGAEYI LVPEIDFTPQ QVCDKITQGF KRGKLHSLIL IAEGVKAPFA DLTEYHGSPG 

       250        260        270        280        290        300 
MAMGDLIREK TGMETRVTIL GHLQRGGSPT ATDRIVASRM AAKAVEILLD GQRDKMINYL 

       310        320        330 
NNSIGVCEIE NAIKKTETIN MDIYNLANIL SM 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP002175 Genomic DNA. Translation: ADO77703.1.
RefSeqYP_005836863.1. NC_017455.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADO77703; ADO77703; Hprae_1576.
GeneID12443552.
KEGGhpk:Hprae_1576.
PATRIC43056473. VBIHalPra106773_1596.

Organism-specific databases

CMRSearch...

Phylogenomic databases

KOK00850.

Enzyme and pathway databases

BioCycHPRA572479:GLDS-1622-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 nameE3DPE1_HALPG
AccessionPrimary (citable) accession number: E3DPE1
Entry history
Integrated into UniProtKB/TrEMBL: January 11, 2011
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 19 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)