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P32179

- MET22_YEAST

UniProt

P32179 - MET22_YEAST

Protein

3'(2'),5'-bisphosphate nucleotidase

Gene

MET22

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 127 (01 Oct 2014)
      Sequence version 1 (01 Oct 1993)
      Previous versions | rss
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    Functioni

    Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine 5'- phosphate (PAP) to AMP. Regulates the flux of sulfur in the sulfur-activation pathway by converting PAPS to APS. Involved in salt tolerance. Confers resistance to lithium.

    Catalytic activityi

    Adenosine 3',5'-bisphosphate + H2O = adenosine 5'-phosphate + phosphate.

    Cofactori

    Magnesium.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi72 – 721Magnesium 1
    Binding sitei72 – 721SubstrateBy similarity
    Metal bindingi142 – 1421Magnesium 1
    Metal bindingi142 – 1421Magnesium 2
    Metal bindingi144 – 1441Magnesium 1; via carbonyl oxygen
    Metal bindingi145 – 1451Magnesium 2
    Metal bindingi294 – 2941Magnesium 2
    Binding sitei294 – 2941SubstrateBy similarity

    GO - Molecular functioni

    1. 3'(2'),5'-bisphosphate nucleotidase activity Source: SGD
    2. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. dephosphorylation Source: GOC
    2. hyperosmotic salinity response Source: SGD
    3. methionine biosynthetic process Source: SGD
    4. phosphatidylinositol phosphorylation Source: InterPro
    5. sulfate assimilation Source: SGD

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Stress response

    Keywords - Ligandi

    Lithium, Magnesium, Metal-binding

    Enzyme and pathway databases

    BioCyciYEAST:YOL064C-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3'(2'),5'-bisphosphate nucleotidase (EC:3.1.3.7)
    Alternative name(s):
    3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase
    DPNPase
    Halotolerance protein HAL2
    Methionine-requiring protein 22
    Gene namesi
    Name:MET22
    Synonyms:HAL2
    Ordered Locus Names:YOL064C
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    CYGDiYOL064c.
    SGDiS000005425. MET22.

    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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 3573573'(2'),5'-bisphosphate nucleotidasePRO_0000142537Add
    BLAST

    Proteomic databases

    MaxQBiP32179.
    PaxDbiP32179.
    PeptideAtlasiP32179.

    Expressioni

    Inductioni

    By salt stress.

    Gene expression databases

    GenevestigatoriP32179.

    Interactioni

    Protein-protein interaction databases

    BioGridi34337. 140 interactions.
    DIPiDIP-4072N.
    IntActiP32179. 1 interaction.
    MINTiMINT-506588.
    STRINGi4932.YOL064C.

    Structurei

    Secondary structure

    1
    357
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi4 – 3027
    Turni31 – 344
    Beta strandi35 – 384
    Beta strandi44 – 463
    Helixi47 – 6317
    Beta strandi69 – 724
    Helixi80 – 10021
    Beta strandi111 – 1133
    Helixi118 – 1269
    Beta strandi134 – 14512
    Helixi147 – 1515
    Beta strandi157 – 1648
    Beta strandi167 – 1759
    Helixi180 – 1834
    Turni189 – 1946
    Beta strandi196 – 2016
    Turni202 – 2043
    Beta strandi206 – 2105
    Turni211 – 2133
    Beta strandi218 – 2203
    Helixi228 – 2303
    Beta strandi232 – 2354
    Turni239 – 2413
    Helixi244 – 25310
    Beta strandi258 – 2614
    Helixi266 – 2738
    Beta strandi277 – 2815
    Helixi292 – 2943
    Helixi296 – 3049
    Beta strandi308 – 3103
    Beta strandi312 – 3143
    Beta strandi322 – 3254
    Beta strandi327 – 3293
    Beta strandi331 – 3355
    Helixi338 – 35316

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1K9YX-ray1.90A1-357[»]
    1K9ZX-ray1.50A1-357[»]
    1KA0X-ray1.80A1-357[»]
    1KA1X-ray1.30A1-357[»]
    1QGXX-ray1.60A1-357[»]
    ProteinModelPortaliP32179.
    SMRiP32179. Positions 2-355.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP32179.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni144 – 1474Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the inositol monophosphatase family.Curated

    Phylogenomic databases

    eggNOGiCOG1218.
    KOiK01082.
    OMAiGRFWCLD.
    OrthoDBiEOG7VB2R7.

    Family and domain databases

    InterProiIPR006239. Bisphos_HAL2.
    IPR020583. Inositol_monoP_metal-BS.
    IPR000760. Inositol_monophosphatase.
    IPR020550. Inositol_monophosphatase_CS.
    [Graphical view]
    PANTHERiPTHR20854. PTHR20854. 1 hit.
    PfamiPF00459. Inositol_P. 1 hit.
    [Graphical view]
    PRINTSiPR00377. IMPHPHTASES.
    TIGRFAMsiTIGR01330. bisphos_HAL2. 1 hit.
    PROSITEiPS00629. IMP_1. 1 hit.
    PS00630. IMP_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P32179-1 [UniParc]FASTAAdd to Basket

    « Hide

    MALERELLVA TQAVRKASLL TKRIQSEVIS HKDSTTITKN DNSPVTTGDY    50
    AAQTIIINAI KSNFPDDKVV GEESSSGLSD AFVSGILNEI KANDEVYNKN 100
    YKKDDFLFTN DQFPLKSLED VRQIIDFGNY EGGRKGRFWC LDPIDGTKGF 150
    LRGEQFAVCL ALIVDGVVQL GCIGCPNLVL SSYGAQDLKG HESFGYIFRA 200
    VRGLGAFYSP SSDAESWTKI HVRHLKDTKD MITLEGVEKG HSSHDEQTAI 250
    KNKLNISKSL HLDSQAKYCL LALGLADVYL RLPIKLSYQE KIWDHAAGNV 300
    IVHEAGGIHT DAMEDVPLDF GNGRTLATKG VIASSGPREL HDLVVSTSCD 350
    VIQSRNA 357
    Length:357
    Mass (Da):39,149
    Last modified:October 1, 1993 - v1
    Checksum:iAB2E5F90B285702B
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti40 – 401N → S in strain: Montrache.
    Natural varianti61 – 611K → M in strain: Montrache.
    Natural varianti63 – 631N → S in strain: Montrache.
    Natural varianti308 – 3081I → V in strain: Montrache.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X72847 Genomic DNA. Translation: CAA51361.1.
    AY500154 Genomic DNA. Translation: AAR89916.1.
    Z74806 Genomic DNA. Translation: CAA99074.1.
    BK006948 Genomic DNA. Translation: DAA10719.1.
    PIRiS35318.
    RefSeqiNP_014577.1. NM_001183319.1.

    Genome annotation databases

    EnsemblFungiiYOL064C; YOL064C; YOL064C.
    GeneIDi854090.
    KEGGisce:YOL064C.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X72847 Genomic DNA. Translation: CAA51361.1 .
    AY500154 Genomic DNA. Translation: AAR89916.1 .
    Z74806 Genomic DNA. Translation: CAA99074.1 .
    BK006948 Genomic DNA. Translation: DAA10719.1 .
    PIRi S35318.
    RefSeqi NP_014577.1. NM_001183319.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1K9Y X-ray 1.90 A 1-357 [» ]
    1K9Z X-ray 1.50 A 1-357 [» ]
    1KA0 X-ray 1.80 A 1-357 [» ]
    1KA1 X-ray 1.30 A 1-357 [» ]
    1QGX X-ray 1.60 A 1-357 [» ]
    ProteinModelPortali P32179.
    SMRi P32179. Positions 2-355.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34337. 140 interactions.
    DIPi DIP-4072N.
    IntActi P32179. 1 interaction.
    MINTi MINT-506588.
    STRINGi 4932.YOL064C.

    Chemistry

    DrugBanki DB00131. Adenosine monophosphate.

    Proteomic databases

    MaxQBi P32179.
    PaxDbi P32179.
    PeptideAtlasi P32179.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOL064C ; YOL064C ; YOL064C .
    GeneIDi 854090.
    KEGGi sce:YOL064C.

    Organism-specific databases

    CYGDi YOL064c.
    SGDi S000005425. MET22.

    Phylogenomic databases

    eggNOGi COG1218.
    KOi K01082.
    OMAi GRFWCLD.
    OrthoDBi EOG7VB2R7.

    Enzyme and pathway databases

    BioCyci YEAST:YOL064C-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei P32179.
    NextBioi 975743.

    Gene expression databases

    Genevestigatori P32179.

    Family and domain databases

    InterProi IPR006239. Bisphos_HAL2.
    IPR020583. Inositol_monoP_metal-BS.
    IPR000760. Inositol_monophosphatase.
    IPR020550. Inositol_monophosphatase_CS.
    [Graphical view ]
    PANTHERi PTHR20854. PTHR20854. 1 hit.
    Pfami PF00459. Inositol_P. 1 hit.
    [Graphical view ]
    PRINTSi PR00377. IMPHPHTASES.
    TIGRFAMsi TIGR01330. bisphos_HAL2. 1 hit.
    PROSITEi PS00629. IMP_1. 1 hit.
    PS00630. IMP_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Salt tolerance and methionine biosynthesis in Saccharomyces cerevisiae involve a putative phosphatase gene."
      Glaeser H.-U., Thomas D., Gaxiola R., Montrichard F., Surdin-Kerjan Y., Serrano R.
      EMBO J. 12:3105-3110(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Cloning of HAL2 gene from Saccharomyces cerevisiae Montrache."
      Thanananta N., Apisitwanich S., Peyachoknagul S.
      Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: Montrache.
    3. "Sequence analysis of a 33.2 kb segment from the left arm of yeast chromosome XV reveals eight known genes and ten new open reading frames including homologues of ABC transporters, inositol phosphatases and human expressed sequence tags."
      Tzermia M., Katsoulou C., Alexandraki D.
      Yeast 13:583-589(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "X-ray structure of yeast Hal2p, a major target of lithium and sodium toxicity, and identification of framework interactions determining cation sensitivity."
      Albert A., Yenush L., Gil-Mascarell M.R., Rodriguez P.L., Patel S., Martinez-Ripoll M., Blundell T.L., Serrano R.
      J. Mol. Biol. 295:927-938(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS AND AMP.

    Entry informationi

    Entry nameiMET22_YEAST
    AccessioniPrimary (citable) accession number: P32179
    Secondary accession number(s): D6W203, Q6RFY5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1993
    Last sequence update: October 1, 1993
    Last modified: October 1, 2014
    This is version 127 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 7330 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 XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3