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Q1C297 (K6PF_YERPA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 63. 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:YPA_3463
OrganismYersinia pestis bv. Antiqua (strain Antiqua) [Complete proteome] [HAMAP]
Taxonomic identifier360102 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length327 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 – 3273276-phosphofructokinase HAMAP-Rule MF_00339
PRO_1000059812

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
Q1C297 [UniParc].

Last modified July 11, 2006. Version 1.
Checksum: 1D54B3BABD0E430D

FASTA32735,395
        10         20         30         40         50         60 
MVKKIGVLTS GGDAPGMNAA IRGVVRAALS AGLDVFGIED GYLGLYENRM KKLDRYSVSD 

        70         80         90        100        110        120 
MINRGGTFLG SARFPEFRDP EVRKVALKNM HERGIDGLVV IGGDGSYAGA DLLTKEGGIH 

       130        140        150        160        170        180 
CVGLPGTIDN DVAGTDYTIG FFTALETVVE AIDRLRDTSS SHQRISIVEV MGRYCGDLTL 

       190        200        210        220        230        240 
AAAIAGGCEF IAIPEVEFKR DDLVAEIKAG IAKGKKHAIV AITEKLDDID SLAKYIEKET 

       250        260        270        280        290        300 
GRETRGTVLG HIQRGGAPVA YDRILASRMG AYAVDLLLQD HDYKKGGFCV GVQNEKMVHE 

       310        320 
LISVCIAPEN KKSKFKEDWY DTAKKLF 

« Hide

References

[1]"Complete genome sequence of Yersinia pestis strains Antiqua and Nepal516: evidence of gene reduction in an emerging pathogen."
Chain P.S.G., Hu P., Malfatti S.A., Radnedge L., Larimer F., Vergez L.M., Worsham P., Chu M.C., Andersen G.L.
J. Bacteriol. 188:4453-4463(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Antiqua.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000308 Genomic DNA. Translation: ABG15425.1.
RefSeqYP_653370.1. NC_008150.1.

3D structure databases

ProteinModelPortalQ1C297.
SMRQ1C297. Positions 1-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING360102.YPA_3463.

Proteomic databases

PRIDEQ1C297.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG15425; ABG15425; YPA_3463.
GeneID4121180.
KEGGypa:YPA_3463.
PATRIC18586835. VBIYerPes1796_4207.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycYPES360102:GHZU-3538-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_YERPA
AccessionPrimary (citable) accession number: Q1C297
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 11, 2006
Last modified: April 16, 2014
This is version 63 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