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P47857

- PFKAM_MOUSE

UniProt

P47857 - PFKAM_MOUSE

Protein

ATP-dependent 6-phosphofructokinase, muscle type

Gene

Pfkm

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

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

    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.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 sitei471 – 4711Allosteric activator fructose 2,6-bisphosphateUniRule annotation
    Binding sitei566 – 5661Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
    Binding sitei629 – 6291Allosteric activator fructose 2,6-bisphosphateUniRule annotation
    Binding sitei655 – 6551Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
    Binding sitei735 – 7351Allosteric 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: UniProtKB
    2. ATP binding Source: UniProtKB-KW
    3. fructose binding Source: Ensembl
    4. metal ion binding Source: UniProtKB-KW
    5. phosphofructokinase activity Source: MGI
    6. protein binding Source: MGI
    7. protein homodimerization activity Source: MGI

    GO - Biological processi

    1. carbohydrate phosphorylation Source: GOC
    2. fructose 6-phosphate metabolic process Source: InterPro
    3. glucose homeostasis Source: MGI
    4. glycolytic process Source: MGI
    5. glycolytic process through fructose-6-phosphate Source: MGI
    6. muscle cell cellular homeostasis Source: Ensembl
    7. positive regulation of insulin secretion Source: MGI
    8. protein oligomerization Source: Ensembl

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    SABIO-RKP47857.
    UniPathwayiUPA00109; UER00182.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent 6-phosphofructokinase, muscle typeUniRule annotation (EC:2.7.1.11UniRule annotation)
    Short name:
    ATP-PFKUniRule annotation
    Short name:
    PFK-M
    Alternative name(s):
    6-phosphofructokinase type A
    Phosphofructo-1-kinase isozyme A
    Short name:
    PFK-A
    PhosphohexokinaseUniRule annotation
    Gene namesi
    Name:Pfkm
    Synonyms:Pfk-m, Pfka
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 15

    Organism-specific databases

    MGIiMGI:97548. Pfkm.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. 6-phosphofructokinase complex Source: InterPro
    2. apical plasma membrane Source: Ensembl
    3. cytosol Source: MGI
    4. sperm principal piece Source: MGI

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 780779ATP-dependent 6-phosphofructokinase, muscle typePRO_0000112018Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonineBy similarity
    Glycosylationi530 – 5301O-linked (GlcNAc)By similarity
    Modified residuei667 – 6671PhosphoserineBy similarity
    Modified residuei775 – 7751PhosphoserineBy similarity

    Post-translational modificationi

    GlcNAcylation decreases enzyme activity.By similarity

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP47857.
    PaxDbiP47857.
    PRIDEiP47857.

    PTM databases

    PhosphoSiteiP47857.

    Miscellaneous databases

    PMAP-CutDBP47857.

    Expressioni

    Gene expression databases

    ArrayExpressiP47857.
    BgeeiP47857.
    CleanExiMM_PFKM.
    GenevestigatoriP47857.

    Interactioni

    Subunit structurei

    Homo- and heterotetramers.

    Protein-protein interaction databases

    BioGridi202125. 2 interactions.
    IntActiP47857. 4 interactions.
    MINTiMINT-1869891.

    Structurei

    3D structure databases

    ProteinModelPortaliP47857.
    SMRiP47857. Positions 9-756.
    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 – 40111Interdomain linkerAdd
    BLAST
    Regioni402 – 780379C-terminal regulatory PFK domain 2Add
    BLAST
    Regioni528 – 5325Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
    Regioni573 – 5753Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
    Regioni661 – 6644Allosteric 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.
    InParanoidiP47857.
    KOiK00850.
    OMAiVYHMASK.
    OrthoDBiEOG7ZSHV5.
    PhylomeDBiP47857.
    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.

    P47857-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTHEEHHAAK TLGIGKAIAV LTSGGDAQGM NAAVRAVVRV GIFTGARVFF    50
    VHEGYQGLVD GGEHIREATW ESVSMMLQLG GTVIGSARCK DFREREGRLR 100
    AAHNLVKRGI TNLCVIGGDG SLTGADTFRS EWSDLLNDLQ KDGKITAEEA 150
    TKSSYLNIVG LVGSIDNDFC GTDMTIGTDS ALHRIVEIVD AITTTAQSHQ 200
    RTFVLEVMGR HCGYLALVTS LSCGADWVFI PECPPDDDWE EHLCRRLSET 250
    RTRGSRLNII IVAEGAIDKN GKPITSEDIK NLVVKRLGYD TRVTVLGHVQ 300
    RGGTPSAFDR ILGSRMGVEA VMALLEGTPD TPACVVSLSG NQAVRLPLME 350
    CVQVTKDVTK AMDEKRFDEA IKLRGRSFMN NWEVYKLLAH VRPPVSKGGL 400
    HTVAVMNVGA PAAGMNAAVR STVRIGLIQG NRVLVVHDGF EGLAKGQIEE 450
    AGWSYVGGWT GQGGSKLGTK RTLPKKNLEQ ISANITKFNI QGLVIIGGFE 500
    AYTGGLELME GRKQFDELCI PFVVIPATVS NNVPGSDFSI GADTALNTIC 550
    TTCDRIKQSA AGTKRRVFII ETMGGYCGYL ATMAGLAAGA DAAYIFEEPF 600
    TIRDLQVNVE HLVQKMKTTV KRGLVLRNEK CNENYTTDFI FNLYSEEGKG 650
    IFDSRKNVLG HMQQGGSPTP FDRNFATKMG AKAMNWMSGK IKESYRNGRI 700
    FANTPDSGCV LGMRKRALVF QPVTELKDQT DFEHRIPKEQ WWLKLRPILK 750
    ILAKYEIDLD TSDHAHLEHI SRKRSGEAAV 780
    Length:780
    Mass (Da):85,269
    Last modified:January 23, 2007 - v3
    Checksum:i7917C7AC108B25C7
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF249894 mRNA. Translation: AAF63762.1.
    AK002711 mRNA. Translation: BAB22303.1.
    AK049773 mRNA. Translation: BAC33913.1.
    D21864 Genomic DNA. Translation: BAA21892.1.
    D21865 mRNA. Translation: BAA21012.1.
    CCDSiCCDS27786.1.
    PIRiS53317.
    RefSeqiNP_001156959.1. NM_001163487.1.
    NP_001156960.1. NM_001163488.1.
    NP_067489.3. NM_021514.4.
    XP_006520665.1. XM_006520602.1.
    UniGeneiMm.272582.

    Genome annotation databases

    EnsembliENSMUST00000051226; ENSMUSP00000059801; ENSMUSG00000033065.
    ENSMUST00000163507; ENSMUSP00000132803; ENSMUSG00000033065.
    GeneIDi18642.
    KEGGimmu:18642.
    UCSCiuc007xlv.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF249894 mRNA. Translation: AAF63762.1 .
    AK002711 mRNA. Translation: BAB22303.1 .
    AK049773 mRNA. Translation: BAC33913.1 .
    D21864 Genomic DNA. Translation: BAA21892.1 .
    D21865 mRNA. Translation: BAA21012.1 .
    CCDSi CCDS27786.1.
    PIRi S53317.
    RefSeqi NP_001156959.1. NM_001163487.1.
    NP_001156960.1. NM_001163488.1.
    NP_067489.3. NM_021514.4.
    XP_006520665.1. XM_006520602.1.
    UniGenei Mm.272582.

    3D structure databases

    ProteinModelPortali P47857.
    SMRi P47857. Positions 9-756.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 202125. 2 interactions.
    IntActi P47857. 4 interactions.
    MINTi MINT-1869891.

    PTM databases

    PhosphoSitei P47857.

    Proteomic databases

    MaxQBi P47857.
    PaxDbi P47857.
    PRIDEi P47857.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000051226 ; ENSMUSP00000059801 ; ENSMUSG00000033065 .
    ENSMUST00000163507 ; ENSMUSP00000132803 ; ENSMUSG00000033065 .
    GeneIDi 18642.
    KEGGi mmu:18642.
    UCSCi uc007xlv.2. mouse.

    Organism-specific databases

    CTDi 5213.
    MGIi MGI:97548. Pfkm.

    Phylogenomic databases

    eggNOGi COG0205.
    GeneTreei ENSGT00390000013209.
    HOGENOMi HOG000200154.
    HOVERGENi HBG000976.
    InParanoidi P47857.
    KOi K00850.
    OMAi VYHMASK.
    OrthoDBi EOG7ZSHV5.
    PhylomeDBi P47857.
    TreeFami TF300411.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00182 .
    SABIO-RK P47857.

    Miscellaneous databases

    ChiTaRSi PFKM. mouse.
    NextBioi 294630.
    PMAP-CutDB P47857.
    PROi P47857.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P47857.
    Bgeei P47857.
    CleanExi MM_PFKM.
    Genevestigatori P47857.

    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. "Genomic organization, 5'flanking region and tissue-specific expression of mouse phosphofructokinase C gene."
      Gunasekera D., Kemp R.G.
      Gene 260:103-112(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: Swiss.
      Tissue: Brain.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Kidney and Spinal cord.
    3. "Expression of mouse phosphofructokinase-M gene alternative transcripts: evidence for the conserved two-promoter system."
      Nakajima H., Noguchi T., Hamaguchi T., Tomita K., Hanafusa T., Kono N., Tanaka T., Kuwajima M., Matsuzawa Y.
      Biochem. J. 303:449-453(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-212 AND 259-345.
      Strain: ICR.
    4. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 367-374, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.

    Entry informationi

    Entry nameiPFKAM_MOUSE
    AccessioniPrimary (citable) accession number: P47857
    Secondary accession number(s): O35513, Q543L1, Q9JK94
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 141 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, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3