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B1XB82 (K6PF_ECODH) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 43. 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:
6-phosphofructokinase

Short name=Phosphofructokinase
EC=2.7.1.11
Alternative name(s):
Phosphohexokinase
Gene names
Name:pfkA
Ordered Locus Names:ECDH10B_4105
OrganismEscherichia coli (strain K12 / DH10B) [Complete proteome] [HAMAP]
Taxonomic identifier316385 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00339.

Sequence similarities

Belongs to the phosphofructokinase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processfructose 6-phosphate metabolic process

Inferred from electronic annotation. Source: InterPro

glycolysis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_component6-phosphofructokinase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_function6-phosphofructokinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

ATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3203206-phosphofructokinase HAMAP-Rule MF_00339
PRO_1000120040

Regions

Nucleotide binding22 – 265ATP By similarity
Nucleotide binding155 – 1595ATP By similarity
Nucleotide binding172 – 18817ATP By similarity

Sites

Active site1281Proton acceptor By similarity
Metal binding1861Magnesium; via carbonyl oxygen By similarity
Metal binding1881Magnesium By similarity
Binding site1631Substrate By similarity
Binding site2441Substrate By similarity
Binding site2501Substrate By similarity
Binding site2531Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
B1XB82 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: D03D79F6A5536A41

FASTA32034,842
        10         20         30         40         50         60 
MIKKIGVLTS GGDAPGMNAA IRGVVRSALT EGLEVMGIYD GYLGLYEDRM VQLDRYSVSD 

        70         80         90        100        110        120 
MINRGGTFLG SARFPEFRDE NIRAVAIENL KKRGIDALVV IGGDGSYMGA MRLTEMGFPC 

       130        140        150        160        170        180 
IGLPGTIDND IKGTDYTIGF FTALSTVVEA IDRLRDTSSS HQRISVVEVM GRYCGDLTLA 

       190        200        210        220        230        240 
AAIAGGCEFV VVPEVEFSRE DLVNEIKAGI AKGKKHAIVA ITEHMCDVDE LAHFIEKETG 

       250        260        270        280        290        300 
RETRATVLGH IQRGGSPVPY DRILASRMGA YAIDLLLAGY GGRCVGIQNE QLVHHDIIDA 

       310        320 
IENMKRPFKG DWLDCAKKLY 

« Hide

References

[1]"The complete genome sequence of Escherichia coli DH10B: insights into the biology of a laboratory workhorse."
Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B., Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B., Posfai G., Weinstock G.M., Blattner F.R.
J. Bacteriol. 190:2597-2606(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / DH10B.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000948 Genomic DNA. Translation: ACB04928.1.
RefSeqYP_001732706.1. NC_010473.1.

3D structure databases

ProteinModelPortalB1XB82.
SMRB1XB82. Positions 1-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING316385.ECDH10B_4105.

Proteomic databases

PRIDEB1XB82.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB04928; ACB04928; ECDH10B_4105.
GeneID6059835.
KEGGecd:ECDH10B_4105.
PATRIC18468199. VBIEscCol59506_4136.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000248870.
KOK00850.
OMAKMVHHDI.
OrthoDBEOG644ZRM.
ProtClustDBPRK03202.

Enzyme and pathway databases

BioCycECOL316385:GJ8B-3926-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 nameK6PF_ECODH
AccessionPrimary (citable) accession number: B1XB82
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: May 20, 2008
Last modified: April 16, 2014
This is version 43 of the entry and version 1 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