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P52784 (PFKAM_CANFA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 102. 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
Synonyms:M-PFK
OrganismCanis familiaris (Dog) (Canis lupus familiaris) [Reference proteome]
Taxonomic identifier9615 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCarnivoraCaniformiaCanidaeCanis

Protein attributes

Sequence length782 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.

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 – 782781ATP-dependent 6-phosphofructokinase, muscle type HAMAP-Rule MF_03184
PRO_0000112014

Regions

Nucleotide binding88 – 892ATP By similarity
Nucleotide binding118 – 1214ATP By similarity
Region2 – 390389N-terminal catalytic PFK domain 1 HAMAP-Rule MF_03184
Region164 – 1663Substrate binding By similarity
Region208 – 2103Substrate binding By similarity
Region298 – 3014Substrate binding By similarity
Region391 – 40313Interdomain linker HAMAP-Rule MF_03184
Region404 – 782379C-terminal regulatory PFK domain 2 HAMAP-Rule MF_03184
Region530 – 5345Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region575 – 5773Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region663 – 6664Allosteric activator fructose 2,6-bisphosphate binding By similarity

Sites

Active site1661Proton acceptor By similarity
Metal binding1191Magnesium; catalytic By similarity
Binding site251ATP; via amide nitrogen By similarity
Binding site2011Substrate; shared with dimeric partner By similarity
Binding site2641Substrate By similarity
Binding site2921Substrate; shared with dimeric partner By similarity
Binding site4731Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site5681Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site6311Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site6571Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site7371Allosteric activator fructose 2,6-bisphosphate By similarity

Amino acid modifications

Modified residue21N-acetylthreonine By similarity
Modified residue6691Phosphoserine By similarity
Modified residue7771Phosphoserine By similarity
Glycosylation5321O-linked (GlcNAc) By similarity

Sequences

Sequence LengthMass (Da)Tools
P52784 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 7C28514057CFE1C9

FASTA78285,561
        10         20         30         40         50         60 
MTHEEHHAAK TLGIGKAIAV LTSGGDAQGM NAAVRAVVRV GIFTGARVFF VHEGYQGLVD 

        70         80         90        100        110        120 
GGDHIREATW ESVSMMLQLG GTVIGSARCK DFREREGRLR AAHNLVKRGI TNLCVIGGDG 

       130        140        150        160        170        180 
SLTGADTFRS EWSDLLSDLQ KAGKITAEEA TKSSYLNIVG LVGSIDNDFC GTDMTIGTDS 

       190        200        210        220        230        240 
ALHRIIEIVD AITTTAQSHQ RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDDWE 

       250        260        270        280        290        300 
EHLCRRLSET RTRGSRLNII IVAEGAIDKN GKPITSEEIK ELVVKRLGYD TRVTVLGHVQ 

       310        320        330        340        350        360 
RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NQAVRLPLME CVQVTKDVTK 

       370        380        390        400        410        420 
AMNDRKFDEA MKLRGRSFMN NWEVYKLLAH IRPPVSKTSA TMHTVAVMNV GAPAAGMNAA 

       430        440        450        460        470        480 
VRSTVRIGLI QGNRVLVVHD GFEGLAKGQI EEAGWSYVGG WTGQGGSKLG TKRTLPKKSF 

       490        500        510        520        530        540 
EQISANITKF NIQGLIIIGG FEAYTGGLEL MEGRKQFDEL CIPFVVIPAT VSNNVPGSDF 

       550        560        570        580        590        600 
SVGADTALNT ICTTCDRIKQ SAAGTKRRVF IIETMGGYCG YLATMAGLAA GADAAYIFEE 

       610        620        630        640        650        660 
PFTIRDLQAN VEHLVQKMKT TVKRGLVLRN EKCNENYTTD FIFNLYSEEG KGIFDSRKNV 

       670        680        690        700        710        720 
LGHMQQGGSP TPFDRNFATK MGAKAMNWMS GKIKESYRNG RIFANTPDSG CVLGMRKRAL 

       730        740        750        760        770        780 
VFQPVTELKD QTDFDHRIPK EQWWLKLRPI LKILAKYEID LDTTEHAHLE HISRKRSGET 


SI 

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References

[1]"A cDNA encoding canine muscle-type phosphofructokinase."
Smith B.F., Henthorn P.S., Rajpurohit Y., Stedman H., Wolfe J.H., Patterson D.F., Giger U.
Gene 168:275-276(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Skeletal muscle.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U25183 mRNA. Translation: AAC48615.1.
RefSeqNP_001003199.1. NM_001003199.1.
UniGeneCfa.3710.

3D structure databases

ProteinModelPortalP52784.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9615.ENSCAFP00000013277.

Proteomic databases

PaxDbP52784.
PRIDEP52784.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSCAFT00000046392; ENSCAFP00000037674; ENSCAFG00000009035.
GeneID403849.
KEGGcfa:403849.

Organism-specific databases

CTD5213.

Phylogenomic databases

eggNOGCOG0205.
GeneTreeENSGT00390000013209.
HOGENOMHOG000200154.
HOVERGENHBG000976.
InParanoidP52784.
KOK00850.

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

NextBio20817343.

Entry information

Entry namePFKAM_CANFA
AccessionPrimary (citable) accession number: P52784
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 102 of the entry and version 2 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