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A6QAB4 (PFKA_SULNB) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 51. 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:SUN_1472
OrganismSulfurovum sp. (strain NBC37-1) [Complete proteome] [HAMAP]
Taxonomic identifier387093 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaSulfurovum

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_1000059804

Regions

Nucleotide binding72 – 732ATP By similarity
Nucleotide binding102 – 1054ATP By similarity
Region127 – 1293Substrate binding By similarity
Region171 – 1733Substrate binding By similarity
Region187 – 1893Allosteric activator ADP binding By similarity
Region251 – 2544Substrate binding By similarity

Sites

Active site1291Proton acceptor By similarity
Metal binding1031Magnesium; catalytic By similarity
Binding site111ATP; via amide nitrogen By similarity
Binding site1561Allosteric activator ADP By similarity
Binding site1641Substrate; shared with dimeric partner By similarity
Binding site2241Substrate By similarity
Binding site2451Substrate; shared with dimeric partner By similarity

Sequences

Sequence LengthMass (Da)Tools
A6QAB4 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 81A4E39C4DCC0C4F

FASTA32736,227
        10         20         30         40         50         60 
MKNIAILCSG GDVSGMNAAL KRFVEYAFDQ GLTPFFVENG YEGLIDNKIS KADYSDVAGI 

        70         80         90        100        110        120 
ISIGGTKIRT SRSERFKEIS YRQIALENLR GHGIDGLIVL GGDGSFKGMQ KLSDECNDIG 

       130        140        150        160        170        180 
FIGIPSTIDN DIAGTQYCLG VDTALNAIRV AIDSIRDTAS SFGRAFVIEV MGRECGYLAL 

       190        200        210        220        230        240 
VSALTSGAEM CLIPEVPYNL EVYKEEFLEE KEQGRTYFIA VVSEALKNTE QIVRWFEEEI 

       250        260        270        280        290        300 
DIESRMTVLG HIQRGGIPTV HDRLMAFHFV TSAIDALREG TKSKVVCYDD GMFICKDIKD 

       310        320 
VAFKKYMIDE DLLALGREFE SPQHKQV 

« Hide

References

[1]"Deep-sea vent epsilon-proteobacterial genomes provide insights into emergence of pathogens."
Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K., Horikoshi K.
Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NBC37-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP009179 Genomic DNA. Translation: BAF72423.1.
RefSeqYP_001358780.1. NC_009663.1.

3D structure databases

ProteinModelPortalA6QAB4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING387093.SUN_1472.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAF72423; BAF72423; SUN_1472.
GeneID5363450.
KEGGsun:SUN_1472.
PATRIC23775955. VBISulSp49917_1499.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000248870.
KOK00850.
OMAGFGGRCV.
OrthoDBEOG644ZRM.

Enzyme and pathway databases

BioCycSSP387093:GH25-1494-MONOMER.
UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_00339. Phosphofructokinase_I_B1.
InterProIPR012003. ATP_PFK_prok.
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.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePFKA_SULNB
AccessionPrimary (citable) accession number: A6QAB4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: August 21, 2007
Last modified: July 9, 2014
This is version 51 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