Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P30835

- PFKAL_RAT

UniProt

P30835 - PFKAL_RAT

Protein

ATP-dependent 6-phosphofructokinase, liver type

Gene

Pfkl

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 129 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.

    Catalytic activityi

    ATP + D-fructose 6-phosphate = ADP + D-fructose 1,6-bisphosphate.UniRule annotation

    Cofactori

    Magnesium.

    Enzyme regulationi

    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.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei25 – 251ATP; via amide nitrogenUniRule annotation
    Metal bindingi119 – 1191Magnesium; catalyticUniRule annotation
    Active sitei166 – 1661Proton acceptorUniRule annotation
    Binding sitei201 – 2011Substrate; shared with dimeric partnerUniRule annotation
    Binding sitei264 – 2641SubstrateUniRule annotation
    Binding sitei292 – 2921Substrate; shared with dimeric partnerUniRule annotation
    Binding sitei470 – 4701Allosteric activator fructose 2,6-bisphosphateUniRule annotation
    Binding sitei565 – 5651Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
    Binding sitei628 – 6281Allosteric activator fructose 2,6-bisphosphateUniRule annotation
    Binding sitei654 – 6541Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
    Binding sitei734 – 7341Allosteric activator fructose 2,6-bisphosphateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi88 – 892ATPUniRule annotation
    Nucleotide bindingi118 – 1214ATPUniRule annotation

    GO - Molecular functioni

    1. 6-phosphofructokinase activity Source: RGD
    2. ATP binding Source: RGD
    3. fructose-2,6-bisphosphate 2-phosphatase activity Source: RGD
    4. fructose-6-phosphate binding Source: RGD
    5. fructose binding Source: Ensembl
    6. metal ion binding Source: UniProtKB-KW
    7. monosaccharide binding Source: RGD

    GO - Biological processi

    1. carbohydrate metabolic process Source: RGD
    2. carbohydrate phosphorylation Source: GOC
    3. dephosphorylation Source: GOC
    4. fructose 1,6-bisphosphate metabolic process Source: RGD
    5. fructose 6-phosphate metabolic process Source: RGD
    6. glycolytic process Source: RGD
    7. negative regulation of insulin secretion Source: Ensembl
    8. protein homotetramerization Source: RGD
    9. response to glucose Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

    ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

    Enzyme and pathway databases

    ReactomeiREACT_225694. Glycolysis.
    SABIO-RKP30835.
    UniPathwayiUPA00109; UER00182.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent 6-phosphofructokinase, liver typeUniRule annotation (EC:2.7.1.11UniRule annotation)
    Short name:
    ATP-PFKUniRule annotation
    Short name:
    PFK-L
    Alternative name(s):
    6-phosphofructokinase type B
    Phosphofructo-1-kinase isozyme B
    Short name:
    PFK-B
    PhosphohexokinaseUniRule annotation
    Gene namesi
    Name:Pfkl
    Synonyms:Pfk-l
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 20

    Organism-specific databases

    RGDi3311. Pfkl.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. 6-phosphofructokinase complex Source: Ensembl
    2. cytosol Source: RGD

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 780779ATP-dependent 6-phosphofructokinase, liver typePRO_0000112023Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Glycosylationi529 – 5291O-linked (GlcNAc)By similarity
    Modified residuei640 – 6401PhosphotyrosineBy similarity
    Modified residuei775 – 7751PhosphoserineBy similarity

    Post-translational modificationi

    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.By similarity

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP30835.
    PRIDEiP30835.

    PTM databases

    PhosphoSiteiP30835.

    Expressioni

    Gene expression databases

    GenevestigatoriP30835.

    Interactioni

    Subunit structurei

    Homo- and heterotetramers.

    Protein-protein interaction databases

    BioGridi247769. 1 interaction.
    IntActiP30835. 1 interaction.
    MINTiMINT-4575401.
    STRINGi10116.ENSRNOP00000001625.

    Structurei

    3D structure databases

    ProteinModelPortaliP30835.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 390389N-terminal catalytic PFK domain 1Add
    BLAST
    Regioni164 – 1663Substrate bindingUniRule annotation
    Regioni208 – 2103Substrate bindingUniRule annotation
    Regioni298 – 3014Substrate bindingUniRule annotation
    Regioni391 – 40010Interdomain linker
    Regioni401 – 780380C-terminal regulatory PFK domain 2Add
    BLAST
    Regioni527 – 5315Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
    Regioni572 – 5743Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
    Regioni660 – 6634Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation

    Sequence similaritiesi

    Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade "E" sub-subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0205.
    GeneTreeiENSGT00390000013209.
    HOGENOMiHOG000200154.
    HOVERGENiHBG000976.
    InParanoidiP30835.
    KOiK00850.
    OMAiVQHGITN.
    OrthoDBiEOG7ZSHV5.
    PhylomeDBiP30835.
    TreeFamiTF300411.

    Family and domain databases

    HAMAPiMF_03184. Phosphofructokinase_I_E.
    InterProiIPR009161. 6-phosphofructokinase_euk.
    IPR022953. Phosphofructokinase.
    IPR015912. Phosphofructokinase_CS.
    IPR000023. Phosphofructokinase_dom.
    [Graphical view]
    PfamiPF00365. PFK. 2 hits.
    [Graphical view]
    PIRSFiPIRSF000533. ATP_PFK_euk. 1 hit.
    PRINTSiPR00476. PHFRCTKINASE.
    SUPFAMiSSF53784. SSF53784. 2 hits.
    TIGRFAMsiTIGR02478. 6PF1K_euk. 1 hit.
    PROSITEiPS00433. PHOSPHOFRUCTOKINASE. 2 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P30835-1 [UniParc]FASTAAdd to Basket

    « Hide

    MATVDLEKLR MSGAGKAIGV LTSGGDAQGM NAAVRAVTRM GIYVGAKVFL    50
    IYEGYEGLVE GGENIKPANW LSVSNIIQLG GTIIGSARCK AFTTREGRLA 100
    AAYNLLQHGI TNLCVIGGDG SLTGANIFRN EWGSLLEELV KEGKISESTA 150
    QNYAHLSIAG LVGSIDNDFC GTDMTIGTDS ALHRIMEVID AITTTAQSHQ 200
    RTFVLEVMGR HCGYLALVSA LASGADWLFI PEAPPEDGWE NFMCERLGET 250
    RSRGSRLNII IIAEGAIDRH GKPISSSYVK DLVVQRLGFD TRVTVLGHVQ 300
    RGGTPSAFDR VLSSKMGMEA VMALLEATPD TPACVVSLSG NQSVRLPLME 350
    CVQVTKDVQK AMDEKRFDEA IQLRGRSFEN NWKIYKLLAH QKVSKEKSNF 400
    SLAILNVGAP AAGMNAAVRS AVRTGISEGH TVYVVHDGFE GLAKGQVQEV 450
    GWHDVAGWLG RGGSMLGTKR TLPKPHLEAI VENLRTYNIH ALLVIGGFEA 500
    YEGVLQLVEA RGRYEELCIV MCVIPATISN NVPGTDFSLG SDTAVNAAME 550
    SCDRIKQSAS GTKRRVFIVE TMGGYCGYLA TVTGIAVGAD AAYVFEDPFN 600
    IHDLKANVEH MTEKMKTDIQ RGLVLRNEKC HEHYTTEFLY NLYSSEGRGV 650
    FDCRTNVLGH LQQGGAPTPF DRNYGTKLGV KAMLWMSEKL RDVYRKGRVF 700
    ANAPDSACVI GLRKKVVAFS SVTELKKETD FEHRMPREQW WLNLRLMLKM 750
    LAHYRISMAD YVSGELEHVT RRTLSIDKGF 780
    Length:780
    Mass (Da):85,339
    Last modified:January 23, 2007 - v3
    Checksum:i7F6FCFB076D6A0F1
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58865 mRNA. Translation: CAA41674.1.
    PIRiS19689.
    RefSeqiNP_037322.1. NM_013190.4.
    UniGeneiRn.4212.

    Genome annotation databases

    EnsembliENSRNOT00000001625; ENSRNOP00000001625; ENSRNOG00000001214.
    GeneIDi25741.
    KEGGirno:25741.
    UCSCiRGD:3311. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58865 mRNA. Translation: CAA41674.1 .
    PIRi S19689.
    RefSeqi NP_037322.1. NM_013190.4.
    UniGenei Rn.4212.

    3D structure databases

    ProteinModelPortali P30835.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 247769. 1 interaction.
    IntActi P30835. 1 interaction.
    MINTi MINT-4575401.
    STRINGi 10116.ENSRNOP00000001625.

    PTM databases

    PhosphoSitei P30835.

    Proteomic databases

    PaxDbi P30835.
    PRIDEi P30835.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000001625 ; ENSRNOP00000001625 ; ENSRNOG00000001214 .
    GeneIDi 25741.
    KEGGi rno:25741.
    UCSCi RGD:3311. rat.

    Organism-specific databases

    CTDi 5211.
    RGDi 3311. Pfkl.

    Phylogenomic databases

    eggNOGi COG0205.
    GeneTreei ENSGT00390000013209.
    HOGENOMi HOG000200154.
    HOVERGENi HBG000976.
    InParanoidi P30835.
    KOi K00850.
    OMAi VQHGITN.
    OrthoDBi EOG7ZSHV5.
    PhylomeDBi P30835.
    TreeFami TF300411.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00182 .
    Reactomei REACT_225694. Glycolysis.
    SABIO-RK P30835.

    Miscellaneous databases

    NextBioi 607897.
    PROi P30835.

    Gene expression databases

    Genevestigatori P30835.

    Family and domain databases

    HAMAPi MF_03184. Phosphofructokinase_I_E.
    InterProi IPR009161. 6-phosphofructokinase_euk.
    IPR022953. Phosphofructokinase.
    IPR015912. Phosphofructokinase_CS.
    IPR000023. Phosphofructokinase_dom.
    [Graphical view ]
    Pfami PF00365. PFK. 2 hits.
    [Graphical view ]
    PIRSFi PIRSF000533. ATP_PFK_euk. 1 hit.
    PRINTSi PR00476. PHFRCTKINASE.
    SUPFAMi SSF53784. SSF53784. 2 hits.
    TIGRFAMsi TIGR02478. 6PF1K_euk. 1 hit.
    PROSITEi PS00433. PHOSPHOFRUCTOKINASE. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.

    Entry informationi

    Entry nameiPFKAL_RAT
    AccessioniPrimary (citable) accession number: P30835
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 129 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3