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Q72ZD8 (K6PF_BACC1) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 71. 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:BCE_4730
OrganismBacillus cereus (strain ATCC 10987) [Complete proteome] [HAMAP]
Taxonomic identifier222523 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Protein attributes

Sequence length319 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 – 3193196-phosphofructokinase HAMAP-Rule MF_00339
PRO_1000059740

Regions

Nucleotide binding21 – 255ATP By similarity
Nucleotide binding154 – 1585ATP By similarity
Nucleotide binding171 – 18717ATP By similarity

Sites

Active site1271Proton acceptor By similarity
Metal binding1851Magnesium; via carbonyl oxygen By similarity
Metal binding1871Magnesium By similarity
Binding site1621Substrate By similarity
Binding site2431Substrate By similarity
Binding site2491Substrate By similarity
Binding site2521Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q72ZD8 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: F655330A5044C628

FASTA31934,308
        10         20         30         40         50         60 
MKRIGVLTSG GDSPGMNAAI RAVVRKAIFH DIEVYGIYHG YAGLISGHIE KLELGSVGDI 

        70         80         90        100        110        120 
IHRGGTKLYT ARCPEFKDPE VRLKGIEQLK KHGIEGLVVI GGDGSYQGAK KLTEQGFPCV 

       130        140        150        160        170        180 
GVPGTIDNDI PGTDFTIGFD TALNTVIDAI DKIRDTATSH ERTYVIEVMG RHAGDIALWA 

       190        200        210        220        230        240 
GLADGAETIL IPEEEYDMED VIARLKRGSE RGKKHSIIVV AEGVGSAIDI GKHIEEATNF 

       250        260        270        280        290        300 
DTRVTVLGHV QRGGSPSAQD RVLASRLGAR AVELLIAGKG GRCVGIQDNK LVDHDIIEAL 

       310 
AQKHTIDKDM YQLSKELSI 

« Hide

References

[1]"The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic adaptations and a large plasmid related to Bacillus anthracis pXO1."
Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L., Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F., Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.
Nucleic Acids Res. 32:977-988(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 10987.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017194 Genomic DNA. Translation: AAS43631.1.
RefSeqNP_981023.1. NC_003909.8.

3D structure databases

ProteinModelPortalQ72ZD8.
SMRQ72ZD8. Positions 1-319.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING222523.BCE_4730.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAS43631; AAS43631; BCE_4730.
GeneID2749493.
KEGGbca:BCE_4730.
PATRIC18858076. VBIBacCer118379_4533.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000248869.
KOK00850.
OMAKMVHHDI.
OrthoDBEOG644ZRM.
ProtClustDBPRK03202.

Enzyme and pathway databases

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_BACC1
AccessionPrimary (citable) accession number: Q72ZD8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 5, 2004
Last modified: April 16, 2014
This is version 71 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