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Q2HYU2 (PFKAM_PIG) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 50. 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
OrganismSus scrofa (Pig) [Reference proteome]
Taxonomic identifier9823 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaSuinaSuidaeSus

Protein attributes

Sequence length780 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 – 780779ATP-dependent 6-phosphofructokinase, muscle type HAMAP-Rule MF_03184
PRO_0000289804

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 – 40111Interdomain linker HAMAP-Rule MF_03184
Region402 – 780379C-terminal regulatory PFK domain 2 HAMAP-Rule MF_03184
Region528 – 5325Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region573 – 5753Allosteric activator fructose 2,6-bisphosphate binding By similarity
Region661 – 6644Allosteric 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 site4711Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site5661Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site6291Allosteric activator fructose 2,6-bisphosphate By similarity
Binding site6551Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partner By similarity
Binding site7351Allosteric activator fructose 2,6-bisphosphate By similarity

Amino acid modifications

Modified residue21N-acetylthreonine By similarity
Modified residue6671Phosphoserine By similarity
Modified residue7751Phosphoserine By similarity
Glycosylation5301O-linked (GlcNAc) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2HYU2 [UniParc].

Last modified March 7, 2006. Version 1.
Checksum: C9E127CBFF6005B9

FASTA78085,327
        10         20         30         40         50         60 
MTHEEHHAAK SLGVGKAIAV LTSGGDAQGM NAAVRAVVRV GIYTGARVFF VHEGYQGLVD 

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

       130        140        150        160        170        180 
SLTGADTFRS EWGDLLNDLQ KAGKITAEEA NKSSYLNIVG LVGSIDNDFC GTDMTIGTDS 

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

       250        260        270        280        290        300 
EHLCRRLSET RTRGSRLNII IVAEGAIDKN GQLITSENIK DLVVKRLGYD TRVTVLGHVQ 

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

       370        380        390        400        410        420 
AMNEKRFDEA MKLRGRSFMN NWEVYKLLAH VRPPVTKSGS YTVAVMNVGA PTAGMNAAVR 

       430        440        450        460        470        480 
STVRIGLIQG NRVLVVHDGF EGLAKGQIEE AGWSYVGGWT GQGGSKLGTK RTLPKKSFEQ 

       490        500        510        520        530        540 
ISANITKFNI QGLVIIGGFE AYTGGLELME GRKQYDELCI PFVVIPATVS NNVPGSDFSV 

       550        560        570        580        590        600 
GADTALNTIC MTCDRIKQSA AGTKRRVFII ETMGGYCGYL ATMAGLAAGA DAAYIFEEPF 

       610        620        630        640        650        660 
TIRDLQVNVE HLVQKMKTTV KRGLVLRNEK CNENYTTDFI FNLYSEEGKG IFDSRKNVLG 

       670        680        690        700        710        720 
HMQQGGSPTP LDRNFATKMG AKAMNWMSGK IKESYRNGRI FANTPDSGCV LGMRKRALVF 

       730        740        750        760        770        780 
QPVTELKEQT DFEHRIPKEQ WWLKLRPILK ILAKYEIDLD TSEHAHLEHI TRKRSGEATI 

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References

[1]"Cloning and characterization of porcine phosphofructokinase, muscle (PFKM)."
Wang J., Deng C.Y., Xiong Y.Z.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ363336 mRNA. Translation: ABC94908.1.
RefSeqNP_001038015.1. NM_001044550.1.
UniGeneSsc.4741.

3D structure databases

ProteinModelPortalQ2HYU2.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ2HYU2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID733601.
KEGGssc:733601.

Organism-specific databases

CTD5213.

Phylogenomic databases

HOVERGENHBG000976.
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...

Entry information

Entry namePFKAM_PIG
AccessionPrimary (citable) accession number: Q2HYU2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: March 7, 2006
Last modified: July 9, 2014
This is version 50 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