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P00511 (K6PF_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
6-phosphofructokinase, muscle type

EC=2.7.1.11
Alternative name(s):
Phosphofructo-1-kinase isozyme A
Short name=PFK-A
Short name=Phosphofructokinase-M
Phosphofructokinase 1
Phosphohexokinase
Gene names
Name:PFKM
OrganismOryctolagus cuniculus (Rabbit) [Reference proteome]
Taxonomic identifier9986 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus

Protein attributes

Sequence length780 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the third step of glycolysis, the phosphorylation of fructose-6-phosphate (F6P) by ATP to generate fructose-1,6-bisphosphate (FBP) and ADP 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.

Enzyme regulation

Allosteric enzyme activated by ADP, AMP, or fructose bisphosphate and inhibited by ATP or citrate. 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.

Post-translational modification

GlcNAcylation decreases enzyme activity By similarity. HAMAP-Rule MF_00339

Sequence similarities

Belongs to the phosphofructokinase family. Two domains subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 7807796-phosphofructokinase, muscle type HAMAP-Rule MF_00339
PRO_0000112019

Regions

Repeat2 – 402401Approximate HAMAP-Rule MF_00339
Repeat403 – 780378Approximate HAMAP-Rule MF_00339
Nucleotide binding35 – 395ATP By similarity
Nucleotide binding193 – 1975ATP By similarity
Nucleotide binding210 – 22617ATP By similarity

Sites

Active site1661Proton acceptor By similarity
Metal binding2241Magnesium; via carbonyl oxygen By similarity
Binding site2011Substrate By similarity
Binding site2921Substrate By similarity
Binding site2981Substrate By similarity
Binding site3011Substrate By similarity

Amino acid modifications

Modified residue21N-acetylthreonine Ref.2
Modified residue6671Phosphoserine By similarity
Modified residue7751Phosphoserine; by PKA Ref.3
Glycosylation5301O-linked (GlcNAc) By similarity

Experimental info

Sequence conflict2691R → S AA sequence Ref.2
Sequence conflict480 – 50829Missing AA sequence Ref.2
Sequence conflict5591S → I AA sequence Ref.2
Sequence conflict5661Missing AA sequence Ref.2

Secondary structure

........................................................................................................................ 780
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P00511 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: ACDDF38C36F48EDB

FASTA78085,203
        10         20         30         40         50         60 
MTHEEHHAAR TLGVGKAIAV 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 TRSSYLNIVG LVGSIDNDFC GTDMTIGTDS 

       190        200        210        220        230        240 
ALHRITEIVD AITTTAQSHQ RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDNWE 

       250        260        270        280        290        300 
DHLCRRLSET RTRGSRLNII IVAEGAIDRN GKPITSEGVK DLVVRRLGYD TRVTVLGHVQ 

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

       370        380        390        400        410        420 
AMDEKRFDEA MKLRGRSFMN NWEVYKLLAH IRPPAPKSGS YTVAVMNVGA PAAGMNAAVR 

       430        440        450        460        470        480 
STVRIGLIQG NRVLVVHDGF EGPAKGQIEE AGWSYVGGWT GQGGSKLGSK RTLPKKSFEQ 

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

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

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

       670        680        690        700        710        720 
HMQQGGSPTP FDRNFATKMG AKAMNWMAGK IKESYRNGRI FANTPDSGCV LGMRKRALVF 

       730        740        750        760        770        780 
QPVTELQNQT DFEHRIPKEQ WWLKLRPILK ILAKYEIDLD TSEHAHLEHI SRKRSGEATV 

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References

[1]"The rabbit muscle phosphofructokinase gene. Implications for protein structure, function, and tissue specificity."
Lee C.P., Kao M.C., French B.A., Putney S.D., Chang S.H.
J. Biol. Chem. 262:4195-4199(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Muscle.
[2]"Evolution of phosphofructokinase -- gene duplication and creation of new effector sites."
Poorman R.A., Randolph A., Kemp R.G., Heinrikson R.L.
Nature 309:467-469(1984) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-780, ACETYLATION AT THR-2.
[3]"The sites of phosphorylation of rabbit brain phosphofructo-1-kinase by cyclic AMP-dependent protein kinase."
Valaitis A.P., Foe L.G., Kwiatkowska D., Latshaw S.P., Kemp R.G.
Biochim. Biophys. Acta 995:187-194(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 768-780, PHOSPHORYLATION AT SER-775.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14477 expand/collapse EMBL AC list , M14456, M14457, M14458, M14459, M14460, M14461, M14462, M14463, M14464, M14465, M14466, M14467, M14468, M14469, M14470, M14471, M14472, M14473, M14474, M14475, M14476 Genomic DNA. Translation: AAA31441.1.
PIRKIRBF. A26550.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3O8LX-ray3.20A/B1-762[»]
3O8NX-ray3.20A/B1-762[»]
ProteinModelPortalP00511.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9986.ENSOCUP00000014991.

Chemistry

ChEMBLCHEMBL1075312.

Proteomic databases

PRIDEP00511.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG0205.
HOGENOMHOG000200154.
HOVERGENHBG000976.

Enzyme and pathway databases

SABIO-RKP00511.
UniPathwayUPA00109; UER00182.

Family and domain databases

HAMAPMF_00339. Phosphofructokinase.
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

EvolutionaryTraceP00511.

Entry information

Entry nameK6PF_RABIT
AccessionPrimary (citable) accession number: P00511
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 116 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways