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Q0IIG5 (PFKAM_BOVIN) 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, muscle type

Short name=ATP-PFK
Short name=PFK-M
EC=2.7.1.11
Alternative name(s):
6-phosphofructokinase type A
Phosphofructo-1-kinase isozyme A
Short name=PFK-A
Phosphohexokinase
Gene names
Name:PFKM
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length779 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

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_03184

Catalytic activity

ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate. HAMAP-Rule MF_03184

Cofactor

Magnesium By similarity. HAMAP-Rule MF_03184

Enzyme regulation

Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate By similarity. HAMAP-Rule MF_03184

Pathway

Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4. HAMAP-Rule MF_03184

Subunit structure

Homo- and heterotetramers By similarity. HAMAP-Rule MF_03184

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_03184.

Post-translational modification

GlcNAcylation decreases enzyme activity By similarity. HAMAP-Rule MF_03184

Sequence similarities

Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 779778ATP-dependent 6-phosphofructokinase, muscle type HAMAP-Rule MF_03184
PRO_0000284438

Regions

Nucleotide binding87 – 882ATP By similarity
Nucleotide binding117 – 1204ATP By similarity
Region2 – 389388N-terminal catalytic PFK domain 1 HAMAP-Rule MF_03184
Region163 – 1653Substrate binding By similarity
Region207 – 2093Substrate binding By similarity
Region297 – 3004Substrate binding By similarity
Region390 – 40011Interdomain linker HAMAP-Rule MF_03184
Region401 – 779379C-terminal regulatory PFK domain 2 HAMAP-Rule MF_03184
Region527 – 5315Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region572 – 5743Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region660 – 6634Allosteric activator fructose 2,6-bisphosphate binding By similarity

Sites

Active site1651Proton acceptor By similarity
Metal binding1181Magnesium; catalytic By similarity
Binding site241ATP; via amide nitrogen By similarity
Binding site2001Substrate; shared with dimeric partner By similarity
Binding site2631Substrate By similarity
Binding site2911Substrate; shared with dimeric partner By similarity
Binding site4701Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site5651Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site6281Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site6541Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site7341Allosteric activator fructose 2,6-bisphosphate By similarity

Amino acid modifications

Modified residue21N-acetylthreonine By similarity
Modified residue6661Phosphoserine By similarity
Modified residue7741Phosphoserine By similarity
Glycosylation5291O-linked (GlcNAc) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0IIG5 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: BBA2D207ADD079EE

FASTA77985,294
        10         20         30         40         50         60 
MTHEHHAAKT LGIGKAIAVL TSGGDAQGMN AAVRAVVRVG IYTGARVFFV HEGYQGLVDG 

        70         80         90        100        110        120 
GDNIREATWE SVSMMLQLGG TVIGSARCKD FREREGRLRA AHNLVKRGIT NLCVIGGDGS 

       130        140        150        160        170        180 
LTGADTFRSE WSDLLSDLQK SGKITAEEAT KSSYLNIVGL VGSIDNDFCG TDMTIGTDSA 

       190        200        210        220        230        240 
LHRIIEIVDA ITTTAQSHQR TFVLEVMGRH CGYLALVTSL SCGADWVFIP ECPPDDDWEE 

       250        260        270        280        290        300 
HLCRRLSETR NRGSRLNIII VAEGAIDKNG KPITSEDIKN LVVKRLGYDT RVTVLGHVQR 

       310        320        330        340        350        360 
GGTPSAFDRI LGSRMGVEAV MALLEGTPDT PACVVSLSGN QAVRLPLMEC VQVTKDVTRA 

       370        380        390        400        410        420 
MDERRFDEAL KLRGRSFMNN WEVYKLLAHV RPPKSKSGSH TVAVMNVGAP AAGMNAAVRS 

       430        440        450        460        470        480 
TVRIGLIQGN RMLVVHDGFE GLAKGQIEEA GWSYVGGWTG QGGSKLGTKR TLPKKSFEQI 

       490        500        510        520        530        540 
SANITKFNIQ GLVIIGGFEA YTGGLELMEG RKQYDELCIP FVVIPATVSN NVPGSDFSVG 

       550        560        570        580        590        600 
ADTALNTICM TCDRIKQSAA GTKRRVFIIE TMGGYCGYLA TMAGLAAGAD AAYIFEDPFT 

       610        620        630        640        650        660 
IRDLQVNVEH LVQKMKTTVK RGLVLRNEKC NENYTTDFIF NLYSEEGKGI FDSRKNVLGH 

       670        680        690        700        710        720 
MQQGGSPTPF DRNFATKMGA KAMNWMSGKI KESYRNGRIF ANSPDSGCVL GMRKRALVFQ 

       730        740        750        760        770 
PVTELKEQTD FEHRIPKEQW WLKLRPILKI LAKYEIDLDT SEHAHLEHIS RKRSGEANV 

« Hide

References

[1]NIH - Mammalian Gene Collection (MGC) project
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Basal ganglia.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC122655 mRNA. Translation: AAI22656.1.
RefSeqNP_001068736.1. NM_001075268.1.
UniGeneBt.61411.

3D structure databases

ProteinModelPortalQ0IIG5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000000358.

Proteomic databases

PaxDbQ0IIG5.
PRIDEQ0IIG5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000000359; ENSBTAP00000000359; ENSBTAG00000000286.
GeneID506544.
KEGGbta:506544.

Organism-specific databases

CTD5213.

Phylogenomic databases

eggNOGCOG0205.
GeneTreeENSGT00390000013209.
HOGENOMHOG000200154.
HOVERGENHBG000976.
InParanoidQ0IIG5.
KOK00850.
OMAVYHMASK.
OrthoDBEOG7ZSHV5.
TreeFamTF300411.

Enzyme and pathway databases

UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_03184. Phosphofructokinase_I_E.
InterProIPR009161. 6-phosphofructokinase_euk.
IPR022953. Phosphofructokinase.
IPR015912. Phosphofructokinase_CS.
IPR000023. Phosphofructokinase_dom.
[Graphical view]
PfamPF00365. PFK. 2 hits.
[Graphical view]
PIRSFPIRSF000533. ATP_PFK_euk. 1 hit.
PRINTSPR00476. PHFRCTKINASE.
SUPFAMSSF53784. SSF53784. 2 hits.
TIGRFAMsTIGR02478. 6PF1K_euk. 1 hit.
PROSITEPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio20867650.

Entry information

Entry namePFKAM_BOVIN
AccessionPrimary (citable) accession number: Q0IIG5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: October 3, 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 programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways