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P30835 (PFKAL_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 127. 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, liver type

Short name=ATP-PFK
Short name=PFK-L
EC=2.7.1.11
Alternative name(s):
6-phosphofructokinase type B
Phosphofructo-1-kinase isozyme B
Short name=PFK-B
Phosphohexokinase
Gene names
Name:Pfkl
Synonyms:Pfk-l
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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. 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. GlcNAcylation by OGT overcomes allosteric regulation 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 at Ser-529 by OGT decreases enzyme activity, leading to redirect glucose flux through the oxidative pentose phosphate pathway. Glycosylation is stimulated by both hypoxia and glucose deprivation 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.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentCytoplasm
   LigandATP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
Glycoprotein
Phosphoprotein
   Technical termAllosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcarbohydrate metabolic process

Inferred from direct assay PubMed 1834654. Source: RGD

carbohydrate phosphorylation

Inferred from direct assay PubMed 14342527PubMed 156182PubMed 1834654PubMed 2931076PubMed 4273555PubMed 6240262PubMed 6446905PubMed 6458283. Source: GOC

dephosphorylation

Traceable author statement PubMed 12482582. Source: GOC

fructose 1,6-bisphosphate metabolic process

Inferred from direct assay PubMed 2931076PubMed 4273555. Source: RGD

fructose 6-phosphate metabolic process

Inferred from direct assay PubMed 14342527PubMed 156182PubMed 2931076PubMed 4273555PubMed 6240262PubMed 6446905PubMed 6458283. Source: RGD

glycolytic process

Inferred from direct assay PubMed 2931076PubMed 4273555PubMed 4353083PubMed 6458283. Source: RGD

negative regulation of insulin secretion

Inferred from electronic annotation. Source: Ensembl

protein homotetramerization

Inferred from direct assay PubMed 2931076. Source: RGD

response to glucose

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_component6-phosphofructokinase complex

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from direct assay PubMed 1834654PubMed 6240262. Source: RGD

   Molecular_function6-phosphofructokinase activity

Inferred from direct assay PubMed 14342527PubMed 156182PubMed 1834654PubMed 2931076PubMed 4273555PubMed 6240262PubMed 6446905PubMed 6458283. Source: RGD

ATP binding

Inferred from direct assay PubMed 14342527PubMed 156182PubMed 2931076PubMed 6446905PubMed 6458283. Source: RGD

fructose binding

Inferred from electronic annotation. Source: Ensembl

fructose-2,6-bisphosphate 2-phosphatase activity

Traceable author statement PubMed 12482582. Source: RGD

fructose-6-phosphate binding

Inferred from direct assay PubMed 2931076PubMed 4273555. Source: RGD

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

monosaccharide binding

Inferred from direct assay PubMed 14342527PubMed 156182PubMed 6446905PubMed 6458283. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 780779ATP-dependent 6-phosphofructokinase, liver type HAMAP-Rule MF_03184
PRO_0000112023

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 – 40010Interdomain linker HAMAP-Rule MF_03184
Region401 – 780380C-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 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 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-acetylalanine By similarity
Modified residue6401Phosphotyrosine By similarity
Modified residue7751Phosphoserine By similarity
Glycosylation5291O-linked (GlcNAc) By similarity

Sequences

Sequence LengthMass (Da)Tools
P30835 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 7F6FCFB076D6A0F1

FASTA78085,339
        10         20         30         40         50         60 
MATVDLEKLR MSGAGKAIGV LTSGGDAQGM NAAVRAVTRM GIYVGAKVFL IYEGYEGLVE 

        70         80         90        100        110        120 
GGENIKPANW LSVSNIIQLG GTIIGSARCK AFTTREGRLA AAYNLLQHGI TNLCVIGGDG 

       130        140        150        160        170        180 
SLTGANIFRN EWGSLLEELV KEGKISESTA QNYAHLSIAG LVGSIDNDFC GTDMTIGTDS 

       190        200        210        220        230        240 
ALHRIMEVID AITTTAQSHQ RTFVLEVMGR HCGYLALVSA LASGADWLFI PEAPPEDGWE 

       250        260        270        280        290        300 
NFMCERLGET RSRGSRLNII IIAEGAIDRH GKPISSSYVK DLVVQRLGFD TRVTVLGHVQ 

       310        320        330        340        350        360 
RGGTPSAFDR VLSSKMGMEA VMALLEATPD TPACVVSLSG NQSVRLPLME CVQVTKDVQK 

       370        380        390        400        410        420 
AMDEKRFDEA IQLRGRSFEN NWKIYKLLAH QKVSKEKSNF SLAILNVGAP AAGMNAAVRS 

       430        440        450        460        470        480 
AVRTGISEGH TVYVVHDGFE GLAKGQVQEV GWHDVAGWLG RGGSMLGTKR TLPKPHLEAI 

       490        500        510        520        530        540 
VENLRTYNIH ALLVIGGFEA YEGVLQLVEA RGRYEELCIV MCVIPATISN NVPGTDFSLG 

       550        560        570        580        590        600 
SDTAVNAAME SCDRIKQSAS GTKRRVFIVE TMGGYCGYLA TVTGIAVGAD AAYVFEDPFN 

       610        620        630        640        650        660 
IHDLKANVEH MTEKMKTDIQ RGLVLRNEKC HEHYTTEFLY NLYSSEGRGV FDCRTNVLGH 

       670        680        690        700        710        720 
LQQGGAPTPF DRNYGTKLGV KAMLWMSEKL RDVYRKGRVF ANAPDSACVI GLRKKVVAFS 

       730        740        750        760        770        780 
SVTELKKETD FEHRMPREQW WLNLRLMLKM LAHYRISMAD YVSGELEHVT RRTLSIDKGF 

« Hide

References

[1]"Rat-liver-type phosphofructokinase mRNA. Structure, tissue distribution and regulation."
Hotta K., Nakajima H., Yamasaki T., Hamaguchi T., Kuwajima M., Noguchi T., Tanaka T., Kono N., Tarui S.
Eur. J. Biochem. 202:293-298(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: Sprague-Dawley.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X58865 mRNA. Translation: CAA41674.1.
PIRS19689.
RefSeqNP_037322.1. NM_013190.4.
UniGeneRn.4212.

3D structure databases

ProteinModelPortalP30835.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid247769. 1 interaction.
IntActP30835. 1 interaction.
MINTMINT-4575401.
STRING10116.ENSRNOP00000001625.

PTM databases

PhosphoSiteP30835.

Proteomic databases

PaxDbP30835.
PRIDEP30835.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000001625; ENSRNOP00000001625; ENSRNOG00000001214.
GeneID25741.
KEGGrno:25741.
UCSCRGD:3311. rat.

Organism-specific databases

CTD5211.
RGD3311. Pfkl.

Phylogenomic databases

eggNOGCOG0205.
GeneTreeENSGT00390000013209.
HOGENOMHOG000200154.
HOVERGENHBG000976.
InParanoidP30835.
KOK00850.
OMAVQHGITN.
OrthoDBEOG7ZSHV5.
PhylomeDBP30835.
TreeFamTF300411.

Enzyme and pathway databases

SABIO-RKP30835.
UniPathwayUPA00109; UER00182.

Gene expression databases

GenevestigatorP30835.

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

NextBio607897.
PROP30835.

Entry information

Entry namePFKAL_RAT
AccessionPrimary (citable) accession number: P30835
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 127 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

PATHWAY comments

Index of metabolic and biosynthesis pathways