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Q5R7V5 (K6PL_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 56. 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:
6-phosphofructokinase, liver type

EC=2.7.1.11
Alternative name(s):
Phosphofructo-1-kinase isozyme B
Short name=PFK-B
Phosphofructokinase 1
Phosphohexokinase
Gene names
Name:PFKL
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

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 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 By similarity. HAMAP-Rule MF_00339

Enzyme regulation

Allosteric enzyme activated by ADP, AMP, or fructose bisphosphate and inhibited by ATP or citrate. GlcNAcylation by OGT overcomes allosteric regulation By similarity. 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 By similarity. HAMAP-Rule MF_00339

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_00339

Sequence similarities

Belongs to the phosphofructokinase family. Two domains subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 7807796-phosphofructokinase, liver type HAMAP-Rule MF_00339
PRO_0000284441

Regions

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-acetylalanine By similarity
Modified residue6401Phosphotyrosine By similarity
Modified residue7751Phosphoserine By similarity
Glycosylation5291O-linked (GlcNAc) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R7V5 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: 38904F427763072E

FASTA78085,067
        10         20         30         40         50         60 
MAAVDLEKLR ASGAGKAIGV LTSGGDAQGM NAAVRAVTRM GIYVGAKVFL IHEGYEGLVE 

        70         80         90        100        110        120 
GGENIKQANW LSVSNIIQLG GTVIGSARCK AFTTREGRRA AAYNLVQHGI TNLCVIGGDG 

       130        140        150        160        170        180 
SLTGANIFRS EWGSLLEELV AEGKISETMA RTYSHLNIAG LVGSIDNDFC GTDMTIGTDS 

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

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

       310        320        330        340        350        360 
RGGTPSAFDR VLSSKMAMEA VMALLEATHD TPACVVTLSG NQSVRLPLME CVQMTKEVQK 

       370        380        390        400        410        420 
AMDDKRFDEA IQLRGGSFEN NWNIYKLLAH QKPPKEKSNF SLAILNVGAP AAGMNAAVRS 

       430        440        450        460        470        480 
AVRTGISHGH TVYVVHDGFE GLAKGQVQEV GWHDVAGWLG RGGSMLGTKR TLPKGQLESI 

       490        500        510        520        530        540 
VENIRIYGIH ALLVVGGFEA YEGVLQLVEA RGRYEELCIV MCVIPATISN NVPGTDFSLG 

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

       610        620        630        640        650        660 
IHDLKVNVEH MTEKMKTDIQ RGLVLRNEKC HDYYTTEFLY NLYSSEGKGV FDCRTNVLGH 

       670        680        690        700        710        720 
LQQGGAPTPF DRNYGTKLGV KAMLWLSEKL RDVYRKGRVF ANAPDSACVI GLKKKAVAFS 

       730        740        750        760        770        780 
PVTELKKDTD FEHRMPREQW WLSLRLMLKM LAQYRISMAA YVSGELEHVT RRTLSMDKGF 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR860004 mRNA. Translation: CAH92155.1.
RefSeqNP_001126263.1. NM_001132791.1.

3D structure databases

ProteinModelPortalQ5R7V5.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5R7V5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100173235.
KEGGpon:100173235.

Organism-specific databases

CTD5211.

Phylogenomic databases

HOVERGENHBG000976.
InParanoidQ5R7V5.
KOK00850.

Enzyme and pathway databases

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...

Entry information

Entry nameK6PL_PONAB
AccessionPrimary (citable) accession number: Q5R7V5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: December 21, 2004
Last modified: April 16, 2014
This is version 56 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