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B8D996 (K6PF_BUCA5) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 36. 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:BUAP5A_299
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (strain 5A) [Complete proteome] [HAMAP]
Taxonomic identifier563178 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

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_1000192365

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
B8D996 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 01BC92C6C13521B9

FASTA32035,278
        10         20         30         40         50         60 
MIKKIGVLTS GGDAPGMNAA IRGVVRTALS ERLEVFGIYD GYLGLYENRM VQLDRYSVSD 

        70         80         90        100        110        120 
MINRGGTFLG SARFASFYQD KIRSIAVQNI KKRKIDALVV IGGDGSYIGA QKLTEMGIPC 

       130        140        150        160        170        180 
ISIPGTIDND VSGTDYTIGY FTALQTVVEA IDRLRDTSSS HQRISIVEVM GRHCGDLTLA 

       190        200        210        220        230        240 
AAIAGGCEFI VLPEIDYKKE DLVIEIQAGI AKGKKHAIVA ITEYICDVEE LAQYIEKKTN 

       250        260        270        280        290        300 
RETRATILGH IQRGGAPVVY DRILASRMGA YSVELLIKGY QGKCVGIQNE KMVFNDIKNA 

       310        320 
LKNMKRTFKK DWLITAKKLY 

« Hide

References

[1]"The dynamics and time scale of ongoing genomic erosion in symbiotic bacteria."
Moran N.A., McLaughlin H.J., Sorek R.
Science 323:379-382(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 5A.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001161 Genomic DNA. Translation: ACL30667.1.
RefSeqYP_002468055.1. NC_011833.1.

3D structure databases

ProteinModelPortalB8D996.
SMRB8D996. Positions 1-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING107806.BU305.

Proteomic databases

PRIDEB8D996.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL30667; ACL30667; BUAP5A_299.
GeneID7262565.
KEGGbap:BUAP5A_299.
PATRIC21242853. VBIBucAph51993_0304.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycBAPH563178:GHDF-300-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_BUCA5
AccessionPrimary (citable) accession number: B8D996
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: April 16, 2014
This is version 36 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