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A5UD89 (K6PF_HAEIE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 51. 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:CGSHiEE_07055
OrganismHaemophilus influenzae (strain PittEE) [Complete proteome] [HAMAP]
Taxonomic identifier374930 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length321 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 – 3213216-phosphofructokinase HAMAP-Rule MF_00339
PRO_1000059766

Regions

Nucleotide binding22 – 265ATP By similarity
Nucleotide binding156 – 1605ATP By similarity
Nucleotide binding173 – 18917ATP By similarity

Sites

Active site1291Proton acceptor By similarity
Metal binding1871Magnesium; via carbonyl oxygen By similarity
Metal binding1891Magnesium By similarity
Binding site1641Substrate By similarity
Binding site2451Substrate By similarity
Binding site2511Substrate By similarity
Binding site2541Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
A5UD89 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: A26F285077951523

FASTA32134,922
        10         20         30         40         50         60 
MIKKIAVLTS GGDAPGMNAA IRGVVRSALA EGLEVFGIYD GYQGLYNNKI KQLNRYSVSD 

        70         80         90        100        110        120 
VINRGGTFLG SARFPEFKDP NIRAKCAEIL RSHGIDALVV IGGDGSYMGA KLLTEEHSFP 

       130        140        150        160        170        180 
CVGLPGTIDN DVAGTDYTIG YQTALQTAVD AIDRLRDTSS SHQRISIVEI MGRHCSDLTI 

       190        200        210        220        230        240 
SAGIAGGCEY IVASEIEFNR EELIQQIERS IIRGKRHAII AITELLTDVH SLAKEIEARV 

       250        260        270        280        290        300 
GHETRATVLG HIQRGGSPCA FDRILASRMG AYAVDLLLQG KGGYCVGIQN EQLVHHDIID 

       310        320 
AINNMQRVFK ADWLKVAKRL E 

« Hide

References

[1]"Characterization and modeling of the Haemophilus influenzae core and supragenomes based on the complete genomic sequences of Rd and 12 clinical nontypeable strains."
Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., Ehrlich G.D.
Genome Biol. 8:R103.1-R103.18(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PittEE.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000671 Genomic DNA. Translation: ABQ98740.1.
RefSeqYP_001291123.1. NC_009566.1.

3D structure databases

ProteinModelPortalA5UD89.
SMRA5UD89. Positions 1-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING374930.CGSHiEE_07055.

Proteomic databases

PRIDEA5UD89.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ98740; ABQ98740; CGSHiEE_07055.
GeneID5226105.
KEGGhip:CGSHiEE_07055.
PATRIC20278975. VBIHaeInf81350_1422.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycHINF374930:GJDD-1304-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_HAEIE
AccessionPrimary (citable) accession number: A5UD89
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 10, 2007
Last modified: April 16, 2014
This is version 51 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