MTN2_ARATH
ID MTN2_ARATH Reviewed; 254 AA.
AC Q7XA67; Q9SW50;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase;
DE Short=MTA/SAH nucleosidase;
DE EC=3.2.2.9 {ECO:0000269|PubMed:18342331, ECO:0000269|PubMed:19249293};
DE AltName: Full=5'-methylthioadenosine nucleosidase 2;
DE Short=AtMTAN2 {ECO:0000303|PubMed:18342331};
DE Short=MTA nucleosidase 2;
DE AltName: Full=S-adenosylhomocysteine nucleosidase;
DE Short=AdoHcy nucleosidase;
DE Short=SAH nucleosidase;
DE Short=SRH nucleosidase;
GN Name=MTN2; Synonyms=MTAN2; OrderedLocusNames=At4g34840; ORFNames=T11I11.80;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10617198; DOI=10.1038/47134;
RA Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA Martienssen R., McCombie W.R.;
RT "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL Nature 402:769-777(1999).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION.
RX PubMed=17144895; DOI=10.1111/j.1365-313x.2006.02942.x;
RA Buerstenbinder K., Rzewuski G., Wirtz M., Hell R., Sauter M.;
RT "The role of methionine recycling for ethylene synthesis in Arabidopsis.";
RL Plant J. 49:238-249(2007).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RX PubMed=18342331; DOI=10.1016/j.jmb.2008.01.088;
RA Siu K.K., Lee J.E., Sufrin J.R., Moffatt B.A., McMillan M., Cornell K.A.,
RA Isom C., Howell P.L.;
RT "Molecular determinants of substrate specificity in plant 5'-
RT methylthioadenosine nucleosidases.";
RL J. Mol. Biol. 378:112-128(2008).
RN [7]
RP FUNCTION.
RX PubMed=20554051; DOI=10.1016/j.jsb.2010.06.006;
RA Siu K.K., Asmus K., Zhang A.N., Horvatin C., Li S., Liu T., Moffatt B.,
RA Woods V.L. Jr., Howell P.L.;
RT "Mechanism of substrate specificity in 5'-methylthioadenosine/S-
RT adenosylhomocysteine nucleosidases.";
RL J. Struct. Biol. 173:86-98(2011).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=20345605; DOI=10.1111/j.1365-313x.2010.04211.x;
RA Buerstenbinder K., Waduwara I., Schoor S., Moffatt B.A., Wirtz M.,
RA Minocha S.C., Oppermann Y., Bouchereau A., Hell R., Sauter M.;
RT "Inhibition of 5'-methylthioadenosine metabolism in the Yang cycle alters
RT polyamine levels, and impairs seedling growth and reproduction in
RT Arabidopsis.";
RL Plant J. 62:977-988(2010).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [10] {ECO:0007744|PDB:3BSF}
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH ADENINE, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE SPECIFICITY,
RP AND SUBUNIT.
RX PubMed=19249293; DOI=10.1016/j.bbrc.2009.02.106;
RA Park E.Y., Choi W.S., Oh S.I., Kim K.N., Shin J.S., Song H.K.;
RT "Biochemical and structural characterization of 5'-methylthioadenosine
RT nucleosidases from Arabidopsis thaliana.";
RL Biochem. Biophys. Res. Commun. 381:619-624(2009).
CC -!- FUNCTION: Enzyme of the methionine cycle that catalyzes the
CC irreversible cleavage of the glycosidic bond in 5'-methylthioadenosine
CC (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to a lesser extent, to
CC adenine and the corresponding thioribose, 5'-methylthioribose and S-
CC ribosylhomocysteine, respectively (PubMed:18342331, PubMed:19249293).
CC Contributes to the maintenance of AdoMet homeostasis and is required to
CC sustain high rates of ethylene synthesis. {ECO:0000269|PubMed:17144895,
CC ECO:0000269|PubMed:18342331, ECO:0000269|PubMed:19249293,
CC ECO:0000269|PubMed:20345605, ECO:0000269|PubMed:20554051}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-methyl-5'-thioadenosine = 5-(methylsulfanyl)-D-ribose
CC + adenine; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16708, ChEBI:CHEBI:17509, ChEBI:CHEBI:78440; EC=3.2.2.9;
CC Evidence={ECO:0000269|PubMed:18342331, ECO:0000269|PubMed:19249293};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13618;
CC Evidence={ECO:0000305|PubMed:18342331, ECO:0000305|PubMed:19249293};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-adenosyl-L-homocysteine = adenine + S-(5-deoxy-D-
CC ribos-5-yl)-L-homocysteine; Xref=Rhea:RHEA:17805, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16708, ChEBI:CHEBI:57856, ChEBI:CHEBI:58195; EC=3.2.2.9;
CC Evidence={ECO:0000269|PubMed:18342331, ECO:0000269|PubMed:19249293};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17806;
CC Evidence={ECO:0000305|PubMed:18342331, ECO:0000305|PubMed:19249293};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5'-deoxyadenosine + H2O = 5-deoxy-D-ribose + adenine;
CC Xref=Rhea:RHEA:29859, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708,
CC ChEBI:CHEBI:17319, ChEBI:CHEBI:149540; EC=3.2.2.9;
CC Evidence={ECO:0000269|PubMed:18342331, ECO:0000269|PubMed:19249293};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29860;
CC Evidence={ECO:0000305|PubMed:18342331, ECO:0000305|PubMed:19249293};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.4 uM for 5'-methylthioadenosine (MTA)
CC {ECO:0000269|PubMed:18342331};
CC KM=33.4 uM for 5'-methylthioadenosine (MTA)
CC {ECO:0000269|PubMed:19249293};
CC KM=200.9 uM for S-adenosyl-L-homocysteine (SAH)
CC {ECO:0000269|PubMed:19249293};
CC Note=kcat is 2.0 sec(-1) with MTA as substrate.
CC {ECO:0000269|PubMed:18342331};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:18342331};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via salvage
CC pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from S-methyl-5'-
CC thioadenosine (hydrolase route): step 1/2.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19249293}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype.
CC {ECO:0000269|PubMed:20345605}.
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. MtnN
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB45445.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAB80201.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AL079347; CAB45445.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL161586; CAB80201.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002687; AEE86427.1; -; Genomic_DNA.
DR EMBL; BT010195; AAQ22664.1; -; mRNA.
DR EMBL; AK229730; BAF01568.1; -; mRNA.
DR PIR; T10230; T10230.
DR RefSeq; NP_195210.2; NM_119650.4.
DR PDB; 3BSF; X-ray; 2.90 A; A/B=1-254.
DR PDBsum; 3BSF; -.
DR AlphaFoldDB; Q7XA67; -.
DR SMR; Q7XA67; -.
DR BioGRID; 14918; 2.
DR STRING; 3702.AT4G34840.1; -.
DR iPTMnet; Q7XA67; -.
DR PaxDb; Q7XA67; -.
DR PRIDE; Q7XA67; -.
DR DNASU; 829636; -.
DR EnsemblPlants; AT4G34840.1; AT4G34840.1; AT4G34840.
DR GeneID; 829636; -.
DR Gramene; AT4G34840.1; AT4G34840.1; AT4G34840.
DR KEGG; ath:AT4G34840; -.
DR Araport; AT4G34840; -.
DR TAIR; locus:2116925; AT4G34840.
DR eggNOG; ENOG502QTZK; Eukaryota.
DR HOGENOM; CLU_067435_0_0_1; -.
DR OrthoDB; 1260657at2759; -.
DR PhylomeDB; Q7XA67; -.
DR BioCyc; ARA:AT4G34840-MON; -.
DR BRENDA; 2.4.2.28; 399.
DR BRENDA; 3.2.2.9; 399.
DR UniPathway; UPA00904; UER00871.
DR EvolutionaryTrace; Q7XA67; -.
DR PRO; PR:Q7XA67; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q7XA67; baseline and differential.
DR Genevisible; Q7XA67; AT.
DR GO; GO:0008782; F:adenosylhomocysteine nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008930; F:methylthioadenosine nucleosidase activity; IDA:TAIR.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IDA:TAIR.
DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR GO; GO:0010087; P:phloem or xylem histogenesis; IGI:TAIR.
DR GO; GO:0000003; P:reproduction; IGI:TAIR.
DR Gene3D; 3.40.50.1580; -; 1.
DR InterPro; IPR044580; MTAN.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR PANTHER; PTHR46994; PTHR46994; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Amino-acid biosynthesis; Hydrolase;
KW Methionine biosynthesis; Reference proteome.
FT CHAIN 1..254
FT /note="5'-methylthioadenosine/S-adenosylhomocysteine
FT nucleosidase"
FT /id="PRO_0000401374"
FT ACT_SITE 25
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q9T0I8"
FT ACT_SITE 212
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:Q9T0I8"
FT BINDING 103
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000250|UniProtKB:Q9T0I8"
FT BINDING 186..189
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000250|UniProtKB:Q9T0I8"
FT BINDING 186
FT /ligand="adenine"
FT /ligand_id="ChEBI:CHEBI:16708"
FT /evidence="ECO:0000269|PubMed:19249293"
FT BINDING 212
FT /ligand="adenine"
FT /ligand_id="ChEBI:CHEBI:16708"
FT /evidence="ECO:0000269|PubMed:19249293"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:3BSF"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:3BSF"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:3BSF"
FT STRAND 50..56
FT /evidence="ECO:0007829|PDB:3BSF"
FT STRAND 59..65
FT /evidence="ECO:0007829|PDB:3BSF"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:3BSF"
FT HELIX 79..91
FT /evidence="ECO:0007829|PDB:3BSF"
FT STRAND 96..106
FT /evidence="ECO:0007829|PDB:3BSF"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:3BSF"
FT STRAND 117..127
FT /evidence="ECO:0007829|PDB:3BSF"
FT HELIX 135..140
FT /evidence="ECO:0007829|PDB:3BSF"
FT HELIX 149..154
FT /evidence="ECO:0007829|PDB:3BSF"
FT STRAND 158..164
FT /evidence="ECO:0007829|PDB:3BSF"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:3BSF"
FT STRAND 184..189
FT /evidence="ECO:0007829|PDB:3BSF"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:3BSF"
FT STRAND 204..213
FT /evidence="ECO:0007829|PDB:3BSF"
FT TURN 214..217
FT /evidence="ECO:0007829|PDB:3BSF"
FT TURN 221..225
FT /evidence="ECO:0007829|PDB:3BSF"
FT HELIX 227..246
FT /evidence="ECO:0007829|PDB:3BSF"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:3BSF"
SQ SEQUENCE 254 AA; 27462 MW; E7AA475AA0BAD10C CRC64;
MEGVMGQVEK RPISTIVFIV AMQKEAQPLI NRLRLVEEVN TPFPKEVTWI MFKGMYKDLN
INIVCPGKDS TLGVESVGTV PASLVTYASI LAIQPDLIIN AGTAGGFKAK GACISDVYVV
STVAFHDRRI PVPVLDIYGV GMRNTFPTPN LIKELNLKVG RLSTGDSMDM SPHDEESITA
NDATVKDMEG AAVAYVADIF KVPTILIKGV TDIVDGNRPT SEEFLENLAA VTAKLDESLT
KVIDFISGKC LSDL
