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)

P09201

- F16P_YEAST

UniProt

P09201 - F16P_YEAST

Protein

Fructose-1,6-bisphosphatase

Gene

FBP1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 2 (23 Jan 2007)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

    D-fructose 1,6-bisphosphate + H2O = D-fructose 6-phosphate + phosphate.

    Cofactori

    Binds 3 magnesium ions per subunit.By similarity

    Enzyme regulationi

    Subject to complex allosteric regulation. The enzyme can assume an active R-state, or an inactive T-state. Intermediate conformations may exist. AMP acts as allosteric inhibitor. AMP binding affects the turnover of bound substrate and not the affinity for substrate By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi79 – 791Magnesium 1By similarity
    Metal bindingi108 – 1081Magnesium 1By similarity
    Metal bindingi108 – 1081Magnesium 2By similarity
    Metal bindingi128 – 1281Magnesium 2By similarity
    Metal bindingi128 – 1281Magnesium 3By similarity
    Metal bindingi130 – 1301Magnesium 2; via carbonyl oxygenBy similarity
    Metal bindingi131 – 1311Magnesium 3By similarity
    Binding sitei222 – 2221SubstrateBy similarity
    Binding sitei256 – 2561SubstrateBy similarity
    Binding sitei276 – 2761SubstrateBy similarity
    Binding sitei286 – 2861SubstrateBy similarity
    Metal bindingi292 – 2921Magnesium 3By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi38 – 425AMPBy similarity
    Nucleotide bindingi122 – 1232AMPBy similarity

    GO - Molecular functioni

    1. fructose 1,6-bisphosphate 1-phosphatase activity Source: SGD
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. dephosphorylation Source: GOC
    2. gluconeogenesis Source: SGD
    3. reactive oxygen species metabolic process Source: SGD

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism

    Keywords - Ligandi

    Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciYEAST:YLR377C-MONOMER.
    UniPathwayiUPA00138.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fructose-1,6-bisphosphatase (EC:3.1.3.11)
    Short name:
    FBPase
    Alternative name(s):
    D-fructose-1,6-bisphosphate 1-phosphohydrolase
    Gene namesi
    Name:FBP1
    Ordered Locus Names:YLR377C
    ORF Names:L8039.18
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XII

    Organism-specific databases

    SGDiS000004369. FBP1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: SGD
    2. periplasmic space Source: SGD

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 348347Fructose-1,6-bisphosphatasePRO_0000200511Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei12 – 121Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    PaxDbiP09201.
    PeptideAtlasiP09201.

    Expressioni

    Gene expression databases

    GenevestigatoriP09201.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    BioGridi31636. 65 interactions.
    DIPiDIP-3986N.
    IntActiP09201. 6 interactions.
    MINTiMINT-562945.
    STRINGi4932.YLR377C.

    Structurei

    3D structure databases

    ProteinModelPortaliP09201.
    SMRiP09201. Positions 17-342.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni131 – 1344Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the FBPase class 1 family.Curated

    Phylogenomic databases

    eggNOGiCOG0158.
    GeneTreeiENSGT00390000015513.
    HOGENOMiHOG000191265.
    KOiK03841.
    OMAiSSFTTCV.
    OrthoDBiEOG77HDQH.

    Family and domain databases

    HAMAPiMF_01855. FBPase_class1.
    InterProiIPR000146. FBPase_class-1/SBPase.
    IPR028343. FBPtase.
    IPR020548. Fructose_bisphosphatase_AS.
    [Graphical view]
    PANTHERiPTHR11556. PTHR11556. 1 hit.
    PfamiPF00316. FBPase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF500210. FBPtase. 1 hit.
    PIRSF000904. FBPtase_SBPase. 1 hit.
    PRINTSiPR00115. F16BPHPHTASE.
    PROSITEiPS00124. FBPASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P09201-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPTLVNGPRR DSTEGFDTDI ITLPRFIIEH QKQFKNATGD FTLVLNALQF    50
    AFKFVSHTIR RAELVNLVGL AGASNFTGDQ QKKLDVLGDE IFINAMRASG 100
    IIKVLVSEEQ EDLIVFPTNT GSYAVCCDPI DGSSNLDAGV SVGTIASIFR 150
    LLPDSSGTIN DVLRCGKEMV AACYAMYGSS THLVLTLGDG VDGFTLDTNL 200
    GEFILTHPNL RIPPQKAIYS INEGNTLYWN ETIRTFIEKV KQPQADNNNK 250
    PFSARYVGSM VADVHRTFLY GGLFAYPCDK KSPNGKLRLL YEAFPMAFLM 300
    EQAGGKAVND RGERILDLVP SHIHDKSSIW LGSSGEIDKF LDHIGKSQ 348
    Length:348
    Mass (Da):38,263
    Last modified:January 23, 2007 - v2
    Checksum:iBCFC0984A086094B
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti278 – 2781C → D AA sequence (PubMed:3008716)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00754 Genomic DNA. Translation: CAA68723.1.
    J03207 Genomic DNA. Translation: AAA34603.1.
    U19103 Genomic DNA. Translation: AAB67579.1.
    AY692816 Genomic DNA. Translation: AAT92835.1.
    BK006945 Genomic DNA. Translation: DAA09679.1.
    PIRiS01127. PABY.
    RefSeqiNP_013481.3. NM_001182266.3.

    Genome annotation databases

    EnsemblFungiiYLR377C; YLR377C; YLR377C.
    GeneIDi851092.
    KEGGisce:YLR377C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y00754 Genomic DNA. Translation: CAA68723.1 .
    J03207 Genomic DNA. Translation: AAA34603.1 .
    U19103 Genomic DNA. Translation: AAB67579.1 .
    AY692816 Genomic DNA. Translation: AAT92835.1 .
    BK006945 Genomic DNA. Translation: DAA09679.1 .
    PIRi S01127. PABY.
    RefSeqi NP_013481.3. NM_001182266.3.

    3D structure databases

    ProteinModelPortali P09201.
    SMRi P09201. Positions 17-342.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 31636. 65 interactions.
    DIPi DIP-3986N.
    IntActi P09201. 6 interactions.
    MINTi MINT-562945.
    STRINGi 4932.YLR377C.

    Proteomic databases

    PaxDbi P09201.
    PeptideAtlasi P09201.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YLR377C ; YLR377C ; YLR377C .
    GeneIDi 851092.
    KEGGi sce:YLR377C.

    Organism-specific databases

    SGDi S000004369. FBP1.

    Phylogenomic databases

    eggNOGi COG0158.
    GeneTreei ENSGT00390000015513.
    HOGENOMi HOG000191265.
    KOi K03841.
    OMAi SSFTTCV.
    OrthoDBi EOG77HDQH.

    Enzyme and pathway databases

    UniPathwayi UPA00138 .
    BioCyci YEAST:YLR377C-MONOMER.

    Miscellaneous databases

    NextBioi 967768.
    PROi P09201.

    Gene expression databases

    Genevestigatori P09201.

    Family and domain databases

    HAMAPi MF_01855. FBPase_class1.
    InterProi IPR000146. FBPase_class-1/SBPase.
    IPR028343. FBPtase.
    IPR020548. Fructose_bisphosphatase_AS.
    [Graphical view ]
    PANTHERi PTHR11556. PTHR11556. 1 hit.
    Pfami PF00316. FBPase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF500210. FBPtase. 1 hit.
    PIRSF000904. FBPtase_SBPase. 1 hit.
    PRINTSi PR00115. F16BPHPHTASE.
    PROSITEi PS00124. FBPASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the gene for fructose-1,6-bisphosphatase from Saccharomyces cerevisiae and Schizosaccharomyces pombe. Sequence, protein homology, and expression during growth on glucose."
      Rogers D.T., Hiller E., Mitsock L., Orr E.
      J. Biol. Chem. 263:6051-6057(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Isolation and primary structure of the gene encoding fructose-1,6-bisphosphatase from Saccharomyces cerevisiae."
      Entian K.-D., Vogel R.F., Rose M., Hofmann L., Mecke D.
      FEBS Lett. 236:195-200(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XII."
      Johnston M., Hillier L.W., Riles L., Albermann K., Andre B., Ansorge W., Benes V., Brueckner M., Delius H., Dubois E., Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U., Heumann K., Heuss-Neitzel D., Hilbert H.
      , Hilger F., Kleine K., Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T., Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E., Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M., Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C., Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M., Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H., Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A., Hani J., Hoheisel J.D.
      Nature 387:87-90(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    4. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    6. "Amino acid sequence homology among fructose-1,6-bisphosphatases."
      Marcus F., Gontero B., Harrsch P.B., Rittenhouse J.
      Biochem. Biophys. Res. Commun. 135:374-381(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-16; 83-97; 256-280; 289-306 AND 327-346.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "Global analysis of Cdk1 substrate phosphorylation sites provides insights into evolution."
      Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.
      Science 325:1682-1686(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiF16P_YEAST
    AccessioniPrimary (citable) accession number: P09201
    Secondary accession number(s): D6VZ13
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 134 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 589 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families
    3. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    4. Yeast chromosome XII
      Yeast (Saccharomyces cerevisiae) chromosome XII: entries and gene names

    External Data

    Dasty 3