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A9R6A3 (K6PF_YERPG) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 52. 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:YpAngola_A0088
OrganismYersinia pestis bv. Antiqua (strain Angola) [Complete proteome] [HAMAP]
Taxonomic identifier349746 [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_1000120069

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
A9R6A3 [UniParc].

Last modified February 5, 2008. 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]"Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals new insights into the evolution and pangenome of the plague bacterium."
Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S., Achtman M., Lindler L.E., Ravel J.
J. Bacteriol. 192:1685-1699(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Angola.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000901 Genomic DNA. Translation: ABX86207.1.
RefSeqYP_001604724.1. NC_010159.1.

3D structure databases

ProteinModelPortalA9R6A3.
SMRA9R6A3. Positions 1-327.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349746.YpAngola_A0088.

Proteomic databases

PRIDEA9R6A3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX86207; ABX86207; YpAngola_A0088.
GeneID5798553.
KEGGypg:YpAngola_A0088.
PATRIC18569001. VBIYerPes97331_0336.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycYPES349746:GHPB-90-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_YERPG
AccessionPrimary (citable) accession number: A9R6A3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 5, 2008
Last modified: April 16, 2014
This is version 52 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