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Protein

5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase 1

Gene

MTN1

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Enzyme of the methionine cycle that catalyzes the irreversible cleavage of the glycosidic bond in 5'-methylthioadenosine (MTA) to adenine and 5'-methylthioribose. Contributes to the maintenance of AdoMet homeostasis and is required to sustain high rates of ethylene synthesis. Inactive towards S-adenosylhomocysteine (SAH/AdoHcy).3 Publications

Catalytic activityi

S-adenosyl-L-homocysteine + H2O = S-(5-deoxy-D-ribos-5-yl)-L-homocysteine + adenine.
S-methyl-5'-thioadenosine + H2O = S-methyl-5-thio-D-ribose + adenine.

Enzyme regulationi

Inhibited by CBL3 in a calcium-dependent manner.1 Publication

Kineticsi

  1. KM=7.1 µM for 5'-methylthioadenosine (MTA)1 Publication

    pH dependencei

    Optimum pH is 8.0.1 Publication

    Pathwayi: L-methionine biosynthesis via salvage pathway

    This protein is involved in step 1 of the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route).
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase 1 (MTN1), 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase 2 (MTN2)
    2. Methylthioribose kinase (MTK)
    This subpathway is part of the pathway L-methionine biosynthesis via salvage pathway, which is itself part of Amino-acid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-thioadenosine (hydrolase route), the pathway L-methionine biosynthesis via salvage pathway and in Amino-acid biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei38 – 381Proton acceptorBy similarity
    Binding sitei181 – 1811Substrate; via carbonyl oxygen2 Publications
    Active sitei225 – 2251Proton donorCurated

    GO - Molecular functioni

    GO - Biological processi

    • L-methionine biosynthetic process from methylthioadenosine Source: TAIR
    • nucleoside metabolic process Source: InterPro
    • reproduction Source: TAIR
    • vasculature development Source: TAIR
    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Amino-acid biosynthesis, Methionine biosynthesis

    Enzyme and pathway databases

    BioCyciARA:AT4G38800-MONOMER.
    BRENDAi2.4.2.28. 399.
    3.2.2.9. 399.
    UniPathwayiUPA00904; UER00871.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase 1 (EC:3.2.2.9)
    Short name:
    AtMTN1
    Alternative name(s):
    5'-methylthioadenosine nucleosidase
    Short name:
    MTA nucleosidase
    MTA/SAH nucleosidase 1
    Short name:
    AtMTAN1
    S-adenosylhomocysteine nucleosidase
    Short name:
    AdoHcy nucleosidase
    Short name:
    SAH nucleosidase
    Short name:
    SRH nucleosidase
    Gene namesi
    Name:MTN1
    Synonyms:MTAN, MTAN1
    Ordered Locus Names:At4g38800
    ORF Names:T9A14.80
    OrganismiArabidopsis thaliana (Mouse-ear cress)
    Taxonomic identifieri3702 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
    Proteomesi
    • UP000006548 Componenti: Chromosome 4

    Organism-specific databases

    TAIRiAT4G38800.

    Subcellular locationi

    GO - Cellular componenti

    • cytosol Source: TAIR
    • plasma membrane Source: TAIR
    Complete GO annotation...

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype under normal growth condition. Not able to grow with methylthioadenosine (MTA) as unique source of sulfur.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2672675'-methylthioadenosine/S-adenosylhomocysteine nucleosidase 1PRO_0000401373Add
    BLAST

    Proteomic databases

    PaxDbiQ9T0I8.
    PRIDEiQ9T0I8.

    PTM databases

    iPTMnetiQ9T0I8.

    Expressioni

    Tissue specificityi

    Expressed in roots, leaves, stems, cauline leaves and flowers.1 Publication

    Gene expression databases

    GenevisibleiQ9T0I8. AT.

    Interactioni

    Subunit structurei

    Homodimer. Interacts with CBL3 in a calcium-dependent manner.4 Publications

    Protein-protein interaction databases

    BioGridi15315. 3 interactions.
    IntActiQ9T0I8. 2 interactions.
    STRINGi3702.AT4G38800.1.

    Structurei

    Secondary structure

    1
    267
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi28 – 325Combined sources
    Helixi36 – 4510Combined sources
    Beta strandi63 – 697Combined sources
    Beta strandi72 – 787Combined sources
    Turni83 – 853Combined sources
    Beta strandi86 – 883Combined sources
    Helixi92 – 10615Combined sources
    Beta strandi109 – 11911Combined sources
    Helixi121 – 1233Combined sources
    Beta strandi130 – 14011Combined sources
    Helixi148 – 1536Combined sources
    Helixi162 – 1687Combined sources
    Beta strandi171 – 1777Combined sources
    Helixi185 – 1939Combined sources
    Beta strandi197 – 2026Combined sources
    Helixi203 – 21210Combined sources
    Beta strandi217 – 22610Combined sources
    Beta strandi229 – 2313Combined sources
    Helixi233 – 25927Combined sources
    Helixi264 – 2663Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2H8GX-ray1.50A/B1-267[»]
    2QSUX-ray2.00A/B1-267[»]
    2QTGX-ray1.84A/B1-267[»]
    2QTTX-ray1.93A/B1-267[»]
    3LGSX-ray2.20A/B/C/D1-267[»]
    ProteinModelPortaliQ9T0I8.
    SMRiQ9T0I8. Positions 22-267.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9T0I8.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni116 – 1183Substrate binding
    Regioni199 – 2024Substrate binding

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG410IEX0. Eukaryota.
    ENOG4111IXC. LUCA.
    HOGENOMiHOG000241650.
    KOiK01244.
    OMAiMYGIGAR.
    PhylomeDBiQ9T0I8.

    Family and domain databases

    Gene3Di3.40.50.1580. 1 hit.
    InterProiIPR018017. Nucleoside_phosphorylase.
    IPR000845. Nucleoside_phosphorylase_d.
    [Graphical view]
    PANTHERiPTHR21234. PTHR21234. 1 hit.
    PfamiPF01048. PNP_UDP_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53167. SSF53167. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9T0I8-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAPHGDGLSD IEEPEVDAQS EILRPISSVV FVIAMQAEAL PLVNKFGLSE
    60 70 80 90 100
    TTDSPLGKGL PWVLYHGVHK DLRINVVCPG RDAALGIDSV GTVPASLITF
    110 120 130 140 150
    ASIQALKPDI IINAGTCGGF KVKGANIGDV FLVSDVVFHD RRIPIPMFDL
    160 170 180 190 200
    YGVGLRQAFS TPNLLKELNL KIGRLSTGDS LDMSTQDETL IIANDATLKD
    210 220 230 240 250
    MEGAAVAYVA DLLKIPVVFL KAVTDLVDGD KPTAEEFLQN LTVVTAALEG
    260
    TATKVINFIN GRNLSDL
    Length:267
    Mass (Da):28,451
    Last modified:May 1, 2000 - v1
    Checksum:iE7F8A113441AA012
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL035656 Genomic DNA. Translation: CAB38614.1.
    AL161594 Genomic DNA. Translation: CAB80543.1.
    CP002687 Genomic DNA. Translation: AEE86976.1.
    AF370297 mRNA. Translation: AAK44112.1.
    AY142681 mRNA. Translation: AAN13219.1.
    PIRiT06079.
    RefSeqiNP_195591.1. NM_120040.3.
    UniGeneiAt.2827.
    At.31148.

    Genome annotation databases

    EnsemblPlantsiAT4G38800.1; AT4G38800.1; AT4G38800.
    GeneIDi830035.
    GrameneiAT4G38800.1; AT4G38800.1; AT4G38800.
    KEGGiath:AT4G38800.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AL035656 Genomic DNA. Translation: CAB38614.1.
    AL161594 Genomic DNA. Translation: CAB80543.1.
    CP002687 Genomic DNA. Translation: AEE86976.1.
    AF370297 mRNA. Translation: AAK44112.1.
    AY142681 mRNA. Translation: AAN13219.1.
    PIRiT06079.
    RefSeqiNP_195591.1. NM_120040.3.
    UniGeneiAt.2827.
    At.31148.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2H8GX-ray1.50A/B1-267[»]
    2QSUX-ray2.00A/B1-267[»]
    2QTGX-ray1.84A/B1-267[»]
    2QTTX-ray1.93A/B1-267[»]
    3LGSX-ray2.20A/B/C/D1-267[»]
    ProteinModelPortaliQ9T0I8.
    SMRiQ9T0I8. Positions 22-267.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi15315. 3 interactions.
    IntActiQ9T0I8. 2 interactions.
    STRINGi3702.AT4G38800.1.

    PTM databases

    iPTMnetiQ9T0I8.

    Proteomic databases

    PaxDbiQ9T0I8.
    PRIDEiQ9T0I8.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblPlantsiAT4G38800.1; AT4G38800.1; AT4G38800.
    GeneIDi830035.
    GrameneiAT4G38800.1; AT4G38800.1; AT4G38800.
    KEGGiath:AT4G38800.

    Organism-specific databases

    TAIRiAT4G38800.

    Phylogenomic databases

    eggNOGiENOG410IEX0. Eukaryota.
    ENOG4111IXC. LUCA.
    HOGENOMiHOG000241650.
    KOiK01244.
    OMAiMYGIGAR.
    PhylomeDBiQ9T0I8.

    Enzyme and pathway databases

    UniPathwayiUPA00904; UER00871.
    BioCyciARA:AT4G38800-MONOMER.
    BRENDAi2.4.2.28. 399.
    3.2.2.9. 399.

    Miscellaneous databases

    EvolutionaryTraceiQ9T0I8.
    PROiQ9T0I8.

    Gene expression databases

    GenevisibleiQ9T0I8. AT.

    Family and domain databases

    Gene3Di3.40.50.1580. 1 hit.
    InterProiIPR018017. Nucleoside_phosphorylase.
    IPR000845. Nucleoside_phosphorylase_d.
    [Graphical view]
    PANTHERiPTHR21234. PTHR21234. 1 hit.
    PfamiPF01048. PNP_UDP_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53167. SSF53167. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana."
      Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T., Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B., Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M., de Simone V., Obermaier B.
      , Mache R., Mueller M., Kreis M., Delseny M., Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D., Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J., Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B., Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J., Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R., Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M., Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P., Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S., Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C., Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J., Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S., Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A., Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M., Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D., Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E., Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S., Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R., Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M., Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E., Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P., Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K., Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K., de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K., Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M., Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G., Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K., Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K., Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W., Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H., Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B., Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J., Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K., O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N., Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A., Martienssen R., McCombie W.R.
      Nature 402:769-777(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Columbia.
    2. The Arabidopsis Information Resource (TAIR)
      Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
      Cited for: GENOME REANNOTATION.
      Strain: cv. Columbia.
    3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
      Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
      , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
      Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: cv. Columbia.
    4. "The role of methionine recycling for ethylene synthesis in Arabidopsis."
      Buerstenbinder K., Rzewuski G., Wirtz M., Hell R., Sauter M.
      Plant J. 49:238-249(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    5. "The Arabidopsis calcium sensor calcineurin B-like 3 inhibits the 5'-methylthioadenosine nucleosidase in a calcium-dependent manner."
      Oh S.I., Park J., Yoon S., Kim Y., Park S., Ryu M., Nam M.J., Ok S.H., Kim J.K., Shin J.S., Kim K.N.
      Plant Physiol. 148:1883-1896(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, TISSUE SPECIFICITY, INTERACTION WITH CBL3.
    6. "Inhibition of 5'-methylthioadenosine metabolism in the Yang cycle alters polyamine levels, and impairs seedling growth and reproduction in Arabidopsis."
      Buerstenbinder K., Waduwara I., Schoor S., Moffatt B.A., Wirtz M., Minocha S.C., Oppermann Y., Bouchereau A., Hell R., Sauter M.
      Plant J. 62:977-988(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    7. "Crystal structure of 5'-methylthioadenosine nucleosidase from Arabidopsis thaliana at 1.5-A resolution."
      Park E.Y., Oh S.I., Nam M.J., Shin J.S., Kim K.N., Song H.K.
      Proteins 65:519-523(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.
    8. "Molecular determinants of substrate specificity in plant 5'-methylthioadenosine nucleosidases."
      Siu K.K., Lee J.E., Sufrin J.R., Moffatt B.A., McMillan M., Cornell K.A., Isom C., Howell P.L.
      J. Mol. Biol. 378:112-128(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS, FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
    9. "Mechanism of substrate specificity in 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidases."
      Siu K.K., Asmus K., Zhang A.N., Horvatin C., Li S., Liu T., Moffatt B., Woods V.L. Jr., Howell P.L.
      J. Struct. Biol. 173:86-98(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH SUBSTRATE.

    Entry informationi

    Entry nameiMTN1_ARATH
    AccessioniPrimary (citable) accession number: Q9T0I8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 30, 2010
    Last sequence update: May 1, 2000
    Last modified: February 17, 2016
    This is version 90 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Arabidopsis thaliana
      Arabidopsis thaliana: entries and gene names
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.