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Q1C297 (PFKA_YERPA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 66. 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: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)

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 – 327327ATP-dependent 6-phosphofructokinase HAMAP-Rule MF_00339
PRO_1000059812

Regions

Nucleotide binding73 – 742ATP By similarity
Nucleotide binding103 – 1064ATP By similarity
Region22 – 265Allosteric activator ADP binding; shared with dimeric partner By similarity
Region55 – 606Allosteric activator ADP binding; shared with dimeric partner By similarity
Region127 – 1293Substrate binding By similarity
Region171 – 1733Substrate binding By similarity
Region187 – 1893Allosteric activator ADP binding By similarity
Region215 – 2173Allosteric activator ADP binding By similarity
Region251 – 2544Substrate binding By similarity

Sites

Active site1291Proton acceptor By similarity
Metal binding1041Magnesium; catalytic By similarity
Binding site121ATP; via amide nitrogen By similarity
Binding site1561Allosteric activator ADP By similarity
Binding site1641Substrate; shared with dimeric partner By similarity
Binding site2131Allosteric activator ADP By similarity
Binding site2241Substrate By similarity
Binding site2451Substrate; shared with dimeric partner 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.
OMAGFGGRCV.
OrthoDBEOG644ZRM.

Enzyme and pathway databases

BioCycYPES360102:GHZU-3538-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_YERPA
AccessionPrimary (citable) accession number: Q1C297
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 11, 2006
Last modified: July 9, 2014
This is version 66 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