Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q057P0 (PFKA_BUCCC) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 59. 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:
ATP-dependent 6-phosphofructokinase

Short name=ATP-PFK
Short name=Phosphofructokinase
EC=2.7.1.11
Alternative name(s):
Phosphohexokinase
Gene names
Name:pfkA
Ordered Locus Names:BCc_187
OrganismBuchnera aphidicola subsp. Cinara cedri (strain Cc) [Complete proteome] [HAMAP]
Taxonomic identifier372461 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis By similarity. HAMAP-Rule MF_00339

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_00339

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00339

Enzyme regulation

Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate By similarity. 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

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_00339

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00339.

Sequence similarities

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade "B1" sub-subfamily.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 320320ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_00339
PRO_1000059749

Regions

Nucleotide binding73 – 742ATP By similarity
Nucleotide binding103 – 1064ATP By similarity
Region126 – 1283Substrate binding By similarity
Region170 – 1723Substrate binding By similarity
Region186 – 1883Allosteric activator ADP binding By similarity
Region250 – 2534Substrate binding By similarity

Sites

Active site1281Proton acceptor By similarity
Metal binding1041Magnesium; catalytic By similarity
Binding site121ATP; via amide nitrogen By similarity
Binding site1551Allosteric activator ADP By similarity
Binding site1631Substrate; shared with dimeric partner By similarity
Binding site2121Allosteric activator ADP By similarity
Binding site2231Substrate By similarity
Binding site2441Substrate; shared with dimeric partner By similarity

Sequences

Sequence LengthMass (Da)Tools
Q057P0 [UniParc].

Last modified November 14, 2006. Version 1.
Checksum: 164259B6B644A758

FASTA32035,450
        10         20         30         40         50         60 
MIKKIGILTS GGDSPGMNAI IRSVVCTALN HNIEVKGIYN GFLGLYNNDM KLLKYSHVAN 

        70         80         90        100        110        120 
LLNQGGTILG SSRFLEFKLE KTRKIAIKNI YKRKIDCLII IGGDGSYKAA NFLTNMGVPC 

       130        140        150        160        170        180 
IGIPGTIDND VSGTDYTVGY FTALETVVDA IDKLRDTSAS HHRISIIEIM GRYCGDLTLS 

       190        200        210        220        230        240 
AAIAGGCEFI VIPEIIYQKE LLLLEIQKSI KKGNKHSIVA ITEHICDVNK LAKYIQKKTF 

       250        260        270        280        290        300 
KETRATILGH IQRGGKPVAY DRILASRMGI YAIQLLLKGY KGQCIGVINN KIVHHNINYA 

       310        320 
LKNMKKIFKK DLLNSIKKIY 

« Hide

References

[1]"A small microbial genome: the end of a long symbiotic relationship?"
Perez-Brocal V., Gil R., Ramos S., Lamelas A., Postigo M., Michelena J.M., Silva F.J., Moya A., Latorre A.
Science 314:312-313(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Cc.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000263 Genomic DNA. Translation: ABJ90659.1.
RefSeqYP_802752.1. NC_008513.1.

3D structure databases

ProteinModelPortalQ057P0.
SMRQ057P0. Positions 1-320.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING372461.BCc_187.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ90659; ABJ90659; BCc_187.
GeneID4440798.
KEGGbcc:BCc_187.
PATRIC21246321. VBIBucAph7855_0181.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000248870.
KOK00850.
OMAGFGGRCV.
OrthoDBEOG644ZRM.

Enzyme and pathway databases

BioCycBAPH372461:GHAJ-187-MONOMER.
UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_00339. Phosphofructokinase_I_B1.
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 namePFKA_BUCCC
AccessionPrimary (citable) accession number: Q057P0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 14, 2006
Last modified: July 9, 2014
This is version 59 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