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P47860

- PFKAP_RAT

UniProt

P47860 - PFKAP_RAT

Protein

ATP-dependent 6-phosphofructokinase, platelet type

Gene

Pfkp

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 117 (01 Oct 2014)
      Sequence version 2 (20 Dec 2005)
      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 sitei34 – 341ATP; via amide nitrogenUniRule annotation
    Metal bindingi128 – 1281Magnesium; catalyticUniRule annotation
    Active sitei175 – 1751Proton acceptorUniRule annotation
    Binding sitei210 – 2101Substrate; shared with dimeric partnerUniRule annotation
    Binding sitei273 – 2731SubstrateUniRule annotation
    Binding sitei301 – 3011Substrate; shared with dimeric partnerUniRule annotation
    Binding sitei481 – 4811Allosteric activator fructose 2,6-bisphosphateUniRule annotation
    Binding sitei576 – 5761Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
    Binding sitei639 – 6391Allosteric activator fructose 2,6-bisphosphateUniRule annotation
    Binding sitei665 – 6651Allosteric activator fructose 2,6-bisphosphate; shared with dimeric partnerUniRule annotation
    Binding sitei744 – 7441Allosteric activator fructose 2,6-bisphosphateUniRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi97 – 982ATPUniRule annotation
    Nucleotide bindingi127 – 1304ATPUniRule annotation

    GO - Molecular functioni

    1. 6-phosphofructokinase activity Source: UniProtKB
    2. ATP binding Source: RGD
    3. fructose-6-phosphate binding Source: RGD
    4. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. carbohydrate phosphorylation Source: GOC
    2. fructose 1,6-bisphosphate metabolic process Source: RGD
    3. fructose 6-phosphate metabolic process Source: RGD
    4. glycolytic process Source: RGD
    5. protein homotetramerization Source: RGD

    Keywords - Molecular functioni

    Kinase, Transferase

    Keywords - Biological processi

    Glycolysis

    Keywords - Ligandi

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

    Enzyme and pathway databases

    SABIO-RKP47860.
    UniPathwayiUPA00109; UER00182.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    ATP-dependent 6-phosphofructokinase, platelet typeUniRule annotation (EC:2.7.1.11UniRule annotation)
    Short name:
    ATP-PFKUniRule annotation
    Short name:
    PFK-P
    Alternative name(s):
    6-phosphofructokinase type C
    Phosphofructo-1-kinase isozyme C
    Short name:
    PFK-C
    PhosphohexokinaseUniRule annotation
    Gene namesi
    Name:Pfkp
    Synonyms:Pfkc
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Unplaced

    Organism-specific databases

    RGDi61893. Pfkp.

    Subcellular locationi

    Cytoplasm UniRule annotation

    GO - Cellular componenti

    1. 6-phosphofructokinase complex Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 788788ATP-dependent 6-phosphofructokinase, platelet typePRO_0000112027Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Modified residuei12 – 121PhosphoserineBy similarity
    Modified residuei386 – 3861PhosphoserineBy similarity
    Modified residuei395 – 3951N6-acetyllysineBy similarity
    Modified residuei486 – 4861N6-acetyllysineBy similarity
    Glycosylationi540 – 5401O-linked (GlcNAc)By similarity
    Modified residuei651 – 6511PhosphotyrosineBy similarity
    Modified residuei688 – 6881N6-acetyllysineBy similarity

    Post-translational modificationi

    GlcNAcylation decreases enzyme activity.By similarity

    Keywords - PTMi

    Acetylation, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP47860.
    PRIDEiP47860.

    2D gel databases

    World-2DPAGE0004:P47860.

    PTM databases

    PhosphoSiteiP47860.

    Expressioni

    Tissue specificityi

    Expressed at high level in neuroendocrine tissues.

    Gene expression databases

    GenevestigatoriP47860.

    Interactioni

    Subunit structurei

    Homo- and heterotetramers.UniRule annotation

    Protein-protein interaction databases

    BioGridi248822. 2 interactions.
    IntActiP47860. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP47860.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 399399N-terminal catalytic PFK domain 1Add
    BLAST
    Regioni173 – 1753Substrate bindingUniRule annotation
    Regioni217 – 2193Substrate bindingUniRule annotation
    Regioni307 – 3104Substrate bindingUniRule annotation
    Regioni400 – 41112Interdomain linkerAdd
    BLAST
    Regioni412 – 788377C-terminal regulatory PFK domain 2Add
    BLAST
    Regioni538 – 5425Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
    Regioni583 – 5853Allosteric activator fructose 2,6-bisphosphate bindingUniRule annotation
    Regioni671 – 6744Allosteric 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.
    HOGENOMiHOG000200154.
    HOVERGENiHBG000976.
    InParanoidiP47860.
    KOiK00850.
    PhylomeDBiP47860.

    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.

    P47860-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSDQDSSTSS TSFPKYLEHL SGDGKAIGVL TSGGDAQGMN AAVRAVVRMG    50
    IYTGAKVYFI YEGYQGMVDG GSNIVEAKWE CVSSILQVGG TIIGSARCQA 100
    FRSREGRLKA ACNLVRLGIT NLCVIGGDGS LTGANLFRKE WSGLLEELAK 150
    NGEIDSDTVK KHAYLNVVGM VGSIDNDFCG TDMTIGTDSA LHRIIEVVDA 200
    IMTTAQSHQR TFVLEVMGRH CGYLALVSAL ACGADWVFLP ESPPEEGWEE 250
    EMCLKLSENR ARKKRLNIII VSEGAIDTQN KPITSEKIKE LVVTNLGFDT 300
    RVTILGHVQR GGTPSAFDRI LASRMGVEAV LALLEATPET PACVVSLRGN 350
    QAVRLPLMEC VQMTQDVQKA MDERRFDEAV KLRGRSFEGN LNTYKRLAIK 400
    EPDDKIPKSN CNVAIINVGA PAAGMNAAVR SAVRVGIAEG HKMFAIYDGF 450
    DGLANGQIKE IGWGDVGGWT GQGGSILGTK RTLPGKYLEK IAEQMHSKNI 500
    NALLIIGGFE AYLGLLELAA ARNKHEAFCV PMVMVPATVS NNVPGSDFSI 550
    GADTALNTIT DTCDRIKQSA SGTKRRVFII ETMGGYCGYL ANMGGLAAGA 600
    DAAYIFEEQF DIRDLQSNVM HLTEKMKTSI QRGLVLRNEN CSVNYTTDFI 650
    YQLYSEEGKG VFDCRKNVLG HMQQGGAPSP FDRNFGTKIS AKAMEWISAK 700
    LKGSHGTGKK FVSDDSICVL GIQKRDLLFK PVAELRKATD FEHRIPKQQW 750
    WLKLRPIMKI LAKYEASYDM SDVGKLEPVH NHGELSAI 788
    Length:788
    Mass (Da):85,720
    Last modified:December 20, 2005 - v2
    Checksum:i16FEB963C3297CA6
    GO

    Sequence cautioni

    The sequence AAA17757.1 differs from that shown. Reason: Frameshift at position 27.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti35 – 362DA → ES in AAA17757. (PubMed:8106374)Curated
    Sequence conflicti51 – 511I → M in AAA17757. (PubMed:8106374)Curated
    Sequence conflicti56 – 561K → Q in AAA17757. (PubMed:8106374)Curated
    Sequence conflicti111 – 1111A → T in AAA17757. (PubMed:8106374)Curated
    Sequence conflicti220 – 2201H → Y in AAA17757. (PubMed:8106374)Curated
    Sequence conflicti600 – 6001A → R in AAA17757. (PubMed:8106374)Curated
    Sequence conflicti755 – 7551R → L in AAA17757. (PubMed:8106374)Curated
    Sequence conflicti758 – 7581M → S in AAA17757. (PubMed:8106374)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC088847 mRNA. Translation: AAH88847.1.
    L25387 mRNA. Translation: AAA17757.1. Frameshift.
    PIRiA53047.
    RefSeqiNP_996729.1. NM_206847.1.
    UniGeneiRn.2278.

    Genome annotation databases

    GeneIDi60416.
    KEGGirno:60416.
    UCSCiRGD:61893. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    BC088847 mRNA. Translation: AAH88847.1 .
    L25387 mRNA. Translation: AAA17757.1 . Frameshift.
    PIRi A53047.
    RefSeqi NP_996729.1. NM_206847.1.
    UniGenei Rn.2278.

    3D structure databases

    ProteinModelPortali P47860.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 248822. 2 interactions.
    IntActi P47860. 2 interactions.

    PTM databases

    PhosphoSitei P47860.

    2D gel databases

    World-2DPAGE 0004:P47860.

    Proteomic databases

    PaxDbi P47860.
    PRIDEi P47860.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 60416.
    KEGGi rno:60416.
    UCSCi RGD:61893. rat.

    Organism-specific databases

    CTDi 5214.
    RGDi 61893. Pfkp.

    Phylogenomic databases

    eggNOGi COG0205.
    HOGENOMi HOG000200154.
    HOVERGENi HBG000976.
    InParanoidi P47860.
    KOi K00850.
    PhylomeDBi P47860.

    Enzyme and pathway databases

    UniPathwayi UPA00109 ; UER00182 .
    SABIO-RK P47860.

    Miscellaneous databases

    NextBioi 612122.

    Gene expression databases

    Genevestigatori P47860.

    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. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    2. "Structure, distribution, and functional expression of the phosphofructokinase C isozyme."
      Gekakis N., Johnson R.C., Jerkins A., Mains R.E., Sul H.S.
      J. Biol. Chem. 269:3348-3355(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 3-788.
      Tissue: Hypothalamus.

    Entry informationi

    Entry nameiPFKAP_RAT
    AccessioniPrimary (citable) accession number: P47860
    Secondary accession number(s): Q5HZX8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1996
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 117 of the entry and version 2 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