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P00511 (PFKAM_RABIT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 119. 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:
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
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 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.

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 Ref.2
Chain2 – 780779ATP-dependent 6-phosphofructokinase, muscle type HAMAP-Rule MF_03184
PRO_0000112019

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 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.
[4]"The crystal structures of eukaryotic phosphofructokinases from baker's yeast and rabbit skeletal muscle."
Banaszak K., Mechin I., Obmolova G., Oldham M., Chang S.H., Ruiz T., Radermacher M., Kopperschlager G., Rypniewski W.
J. Mol. Biol. 407:284-297(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 194-959.

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_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

EvolutionaryTraceP00511.

Entry information

Entry namePFKAM_RABIT
AccessionPrimary (citable) accession number: P00511
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 119 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