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P36136

- SHB17_YEAST

UniProt

P36136 - SHB17_YEAST

Protein

Sedoheptulose 1,7-bisphosphatase

Gene

SHB17

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
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    Functioni

    Sedoheptulose 1,7-bisphosphatase involved in riboneogenesis. Dephosphorylates sedoheptulose 1,7-bisphosphate (SBP), which is converted via the non-oxidative pentose phosphate pathway to ribose-5-phosphate. Has a fructose 1,6-bisphosphatase activity in vitro, but this is probably not biologically relevant, since deletion does not affect fructose 1,6-biphosphate (FBP) levels.1 Publication

    Catalytic activityi

    Sedoheptulose 1,7-bisphosphate + H2O = sedoheptulose 7-phosphate + phosphate.2 Publications

    Kineticsi

    1. KM=34 µM for sedoheptulose 1,7-bisphosphate (SBP)2 Publications
    2. KM=0.2 mM for fructose 1,6-bisphosphate (FBP)2 Publications
    3. KM=0.7 mM for fructose 1,6-bisphosphate (in the presence of 1 mM fructose 2,6-bisphosphate)2 Publications
    4. KM=2.3 mM for fructose 1,6-bisphosphate (in the presence of 2 mM fructose 2,6-bisphosphate)2 Publications
    5. KM=1.4 mM for fructose 1-phosphate2 Publications
    6. KM=1.6 mM for glyceraldehyde 3-phosphate2 Publications
    7. KM=0.3 mM for erythrose 4-phosphate2 Publications

    Vmax=7.8 µmol/min/mg enzyme toward sedoheptulose 1,7-bisphosphate (SBP)2 Publications

    Vmax=8.7 µmol/min/mg enzyme toward fructose 1,6-bisphosphate (FBP)2 Publications

    Vmax=7.3 µmol/min/mg enzyme toward fructose 1,6-bisphosphate (in the presence of 1 mM fructose 2,6-bisphosphate)2 Publications

    Vmax=8.9 µmol/min/mg enzyme toward fructose 1,6-bisphosphate,(in the presence of 1 mM fructose 2,6-bisphosphate)2 Publications

    Vmax=7.3 µmol/min/mg enzyme toward fructose 1-phosphate2 Publications

    Vmax=1 µmol/min/mg enzyme toward glyceraldehyde 3-phosphate2 Publications

    Vmax=0.6 µmol/min/mg enzyme toward erythrose 4-phosphate2 Publications

    pH dependencei

    Optimum pH is 6.5.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei12 – 121Substrate
    Active sitei13 – 131Tele-phosphohistidine intermediate
    Binding sitei69 – 691Substrate
    Active sitei176 – 1761
    Binding sitei181 – 1811Substrate
    Binding sitei244 – 2441Substrate

    GO - Molecular functioni

    1. oxidoreductase activity Source: UniProtKB-KW
    2. sedoheptulose-bisphosphatase activity Source: SGD

    GO - Biological processi

    1. carbohydrate metabolic process Source: UniProtKB-KW
    2. dephosphorylation Source: GOC
    3. ribose phosphate biosynthetic process Source: SGD
    4. ribosome biogenesis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase, Oxidoreductase

    Keywords - Biological processi

    Carbohydrate metabolism, Ribosome biogenesis

    Enzyme and pathway databases

    BioCyciYEAST:G3O-32014-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sedoheptulose 1,7-bisphosphatase (EC:3.1.3.37)
    Gene namesi
    Name:SHB17
    Ordered Locus Names:YKR043C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XI

    Organism-specific databases

    CYGDiYKR043c.
    SGDiS000001751. SHB17.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi12 – 121R → A: Impairs catalytic activity. 1 Publication
    Mutagenesisi13 – 131H → A: Impairs catalytic activity. 1 Publication
    Mutagenesisi16 – 161T → A: Impairs catalytic activity. 1 Publication
    Mutagenesisi19 – 191S → A: Leads to reduced substrate affinity. 1 Publication
    Mutagenesisi24 – 241Y → A: Leads to low activity and reduced substrate affinity. 1 Publication
    Mutagenesisi65 – 651S → A: Leads to low activity and reduced substrate affinity. 1 Publication
    Mutagenesisi69 – 691R → A: Leads to reduced substrate affinity. 1 Publication
    Mutagenesisi99 – 991E → A: Impairs catalytic activity. 1 Publication
    Mutagenesisi102 – 1021Y → A: Impairs catalytic activity. 1 Publication
    Mutagenesisi131 – 1311W → A: Leads to reduced substrate affinity. 1 Publication
    Mutagenesisi176 – 1761H → A: Impairs catalytic activity. 1 Publication
    Mutagenesisi178 – 1781H → A: Leads to low activity and reduced substrate affinity. 1 Publication
    Mutagenesisi181 – 1811R → A: Leads to reduced substrate affinity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 271271Sedoheptulose 1,7-bisphosphatasePRO_0000203211Add
    BLAST

    Proteomic databases

    MaxQBiP36136.
    PaxDbiP36136.
    PeptideAtlasiP36136.
    PRIDEiP36136.

    Expressioni

    Inductioni

    Expression is correlated with levels of ribosomal proteins, thus periodic SHB17 expression coincides with the peak demand for ribose phosphate that occurs during ribosome synthesis.1 Publication

    Gene expression databases

    GenevestigatoriP36136.

    Interactioni

    Subunit structurei

    Homodimer.2 Publications

    Protein-protein interaction databases

    BioGridi34175. 19 interactions.
    DIPiDIP-4847N.
    IntActiP36136. 1 interaction.
    MINTiMINT-567834.
    STRINGi4932.YKR043C.

    Structurei

    Secondary structure

    1
    271
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 126
    Helixi17 – 215
    Beta strandi26 – 283
    Helixi34 – 4815
    Helixi49 – 513
    Helixi56 – 583
    Beta strandi59 – 646
    Helixi68 – 7710
    Turni78 – 803
    Helixi83 – 875
    Beta strandi89 – 935
    Helixi95 – 973
    Helixi103 – 1053
    Helixi110 – 11910
    Beta strandi124 – 1263
    Helixi130 – 1334
    Helixi141 – 16424
    Beta strandi170 – 1756
    Helixi177 – 18711
    Beta strandi191 – 1955
    Helixi199 – 2024
    Beta strandi219 – 2235
    Beta strandi237 – 2437
    Beta strandi249 – 2535
    Turni254 – 2574
    Helixi262 – 2643

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3F3KX-ray1.75A/B2-263[»]
    3LG2X-ray2.60A/B/C/D1-271[»]
    3LL4X-ray2.49A/B1-271[»]
    3OI7X-ray2.40A/B/C/D1-271[»]
    ProteinModelPortaliP36136.
    SMRiP36136. Positions 2-263.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP36136.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni24 – 252Substrate binding
    Regioni99 – 1024Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG0406.
    HOGENOMiHOG000221683.
    KOiK15634.
    OMAiGCENGES.
    OrthoDBiEOG7N9068.

    Family and domain databases

    Gene3Di3.40.50.1240. 1 hit.
    InterProiIPR013078. His_Pase_superF_clade-1.
    IPR029033. His_PPase_superfam.
    [Graphical view]
    PfamiPF00300. His_Phos_1. 1 hit.
    [Graphical view]
    SMARTiSM00855. PGAM. 1 hit.
    [Graphical view]
    SUPFAMiSSF53254. SSF53254. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P36136-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPSLTPRCII VRHGQTEWSK SGQYTGLTDL PLTPYGEGQM LRTGESVFRN    50
    NQFLNPDNIT YIFTSPRLRA RQTVDLVLKP LSDEQRAKIR VVVDDDLREW 100
    EYGDYEGMLT REIIELRKSR GLDKERPWNI WRDGCENGET TQQIGLRLSR 150
    AIARIQNLHR KHQSEGRASD IMVFAHGHAL RYFAAIWFGL GVQKKCETIE 200
    EIQNVKSYDD DTVPYVKLES YRHLVDNPCF LLDAGGIGVL SYAHHNIDEP 250
    ALELAGPFVS PPEEESQHGD V 271
    Length:271
    Mass (Da):31,022
    Last modified:June 1, 1994 - v1
    Checksum:iFF934DE2F5145C40
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z28268 Genomic DNA. Translation: CAA82119.1.
    BK006944 Genomic DNA. Translation: DAA09195.1.
    PIRiS38115.
    RefSeqiNP_012969.1. NM_001179833.1.

    Genome annotation databases

    EnsemblFungiiYKR043C; YKR043C; YKR043C.
    GeneIDi853917.
    KEGGisce:YKR043C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z28268 Genomic DNA. Translation: CAA82119.1 .
    BK006944 Genomic DNA. Translation: DAA09195.1 .
    PIRi S38115.
    RefSeqi NP_012969.1. NM_001179833.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3F3K X-ray 1.75 A/B 2-263 [» ]
    3LG2 X-ray 2.60 A/B/C/D 1-271 [» ]
    3LL4 X-ray 2.49 A/B 1-271 [» ]
    3OI7 X-ray 2.40 A/B/C/D 1-271 [» ]
    ProteinModelPortali P36136.
    SMRi P36136. Positions 2-263.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34175. 19 interactions.
    DIPi DIP-4847N.
    IntActi P36136. 1 interaction.
    MINTi MINT-567834.
    STRINGi 4932.YKR043C.

    Proteomic databases

    MaxQBi P36136.
    PaxDbi P36136.
    PeptideAtlasi P36136.
    PRIDEi P36136.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YKR043C ; YKR043C ; YKR043C .
    GeneIDi 853917.
    KEGGi sce:YKR043C.

    Organism-specific databases

    CYGDi YKR043c.
    SGDi S000001751. SHB17.

    Phylogenomic databases

    eggNOGi COG0406.
    HOGENOMi HOG000221683.
    KOi K15634.
    OMAi GCENGES.
    OrthoDBi EOG7N9068.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-32014-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P36136.
    NextBioi 975261.

    Gene expression databases

    Genevestigatori P36136.

    Family and domain databases

    Gene3Di 3.40.50.1240. 1 hit.
    InterProi IPR013078. His_Pase_superF_clade-1.
    IPR029033. His_PPase_superfam.
    [Graphical view ]
    Pfami PF00300. His_Phos_1. 1 hit.
    [Graphical view ]
    SMARTi SM00855. PGAM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53254. SSF53254. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Complete DNA sequence of yeast chromosome XI."
      Dujon B., Alexandraki D., Andre B., Ansorge W., Baladron V., Ballesta J.P.G., Banrevi A., Bolle P.-A., Bolotin-Fukuhara M., Bossier P., Bou G., Boyer J., Buitrago M.J., Cheret G., Colleaux L., Daignan-Fornier B., del Rey F., Dion C.
      , Domdey H., Duesterhoeft A., Duesterhus S., Entian K.-D., Erfle H., Esteban P.F., Feldmann H., Fernandes L., Fobo G.M., Fritz C., Fukuhara H., Gabel C., Gaillon L., Garcia-Cantalejo J.M., Garcia-Ramirez J.J., Gent M.E., Ghazvini M., Goffeau A., Gonzalez A., Grothues D., Guerreiro P., Hegemann J.H., Hewitt N., Hilger F., Hollenberg C.P., Horaitis O., Indge K.J., Jacquier A., James C.M., Jauniaux J.-C., Jimenez A., Keuchel H., Kirchrath L., Kleine K., Koetter P., Legrain P., Liebl S., Louis E.J., Maia e Silva A., Marck C., Monnier A.-L., Moestl D., Mueller S., Obermaier B., Oliver S.G., Pallier C., Pascolo S., Pfeiffer F., Philippsen P., Planta R.J., Pohl F.M., Pohl T.M., Poehlmann R., Portetelle D., Purnelle B., Puzos V., Ramezani Rad M., Rasmussen S.W., Remacha M.A., Revuelta J.L., Richard G.-F., Rieger M., Rodrigues-Pousada C., Rose M., Rupp T., Santos M.A., Schwager C., Sensen C., Skala J., Soares H., Sor F., Stegemann J., Tettelin H., Thierry A., Tzermia M., Urrestarazu L.A., van Dyck L., van Vliet-Reedijk J.C., Valens M., Vandenbol M., Vilela C., Vissers S., von Wettstein D., Voss H., Wiemann S., Xu G., Zimmermann J., Haasemann M., Becker I., Mewes H.-W.
      Nature 369:371-378(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    2. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    3. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    4. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    5. "Structure and activity of the metal-independent fructose-1,6-bisphosphatase YK23 from Saccharomyces cerevisiae."
      Kuznetsova E., Xu L., Singer A., Brown G., Dong A., Flick R., Cui H., Cuff M., Joachimiak A., Savchenko A., Yakunin A.F.
      J. Biol. Chem. 285:21049-21059(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH FBP, SUBUNIT, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ARG-12; HIS-13; THR-16; SER-19; TYR-24; SER-65; ARG-69; GLU-99; TYR-102; TRP-131; HIS-176; HIS-178 AND ARG-181.
    6. Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) IN COMPLEX WITH SBP, SUBUNIT, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION.

    Entry informationi

    Entry nameiSHB17_YEAST
    AccessioniPrimary (citable) accession number: P36136
    Secondary accession number(s): D6VXA5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Present with 11500 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    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 XI
      Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

    External Data

    Dasty 3