MTN1_ARATH
ID MTN1_ARATH Reviewed; 267 AA.
AC Q9T0I8;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=5'-methylthioadenosine nucleosidase;
DE Short=MTA nucleosidase;
DE EC=3.2.2.16 {ECO:0000269|PubMed:18342331, ECO:0000269|PubMed:19249293};
DE AltName: Full=5'-methylthioadenosine nucleosidase 1;
DE Short=AtMTAN1 {ECO:0000303|PubMed:18342331};
DE Short=MTA nucleosidase 1;
GN Name=MTN1; Synonyms=MTAN, MTAN1; OrderedLocusNames=At4g38800;
GN ORFNames=T9A14.80;
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 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 [5]
RP ACTIVITY REGULATION, TISSUE SPECIFICITY, AND INTERACTION WITH CBL3.
RX PubMed=18945934; DOI=10.1104/pp.108.130419;
RA Oh S.I., Park J., Yoon S., Kim Y., Park S., Ryu M., Nam M.J., Ok S.H.,
RA Kim J.K., Shin J.S., Kim K.N.;
RT "The Arabidopsis calcium sensor calcineurin B-like 3 inhibits the 5'-
RT methylthioadenosine nucleosidase in a calcium-dependent manner.";
RL Plant Physiol. 148:1883-1896(2008).
RN [6]
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 [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, 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).
RN [8] {ECO:0007744|PDB:2H8G}
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH ADENINE, AND SUBUNIT.
RX PubMed=16909418; DOI=10.1002/prot.21120;
RA Park E.Y., Oh S.I., Nam M.J., Shin J.S., Kim K.N., Song H.K.;
RT "Crystal structure of 5'-methylthioadenosine nucleosidase from Arabidopsis
RT thaliana at 1.5-A resolution.";
RL Proteins 65:519-523(2006).
RN [9] {ECO:0007744|PDB:2QSU, ECO:0007744|PDB:2QTG, ECO:0007744|PDB:2QTT}
RP X-RAY CRYSTALLOGRAPHY (1.84 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP ADENINE AND THE SUBSTRATE- AND TRANSITION-STATE-ANALOGS
RP 5'-METHYLTHIOTUBERCIDIN AND FORMYCIN A, FUNCTION, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION,
RP AND SUBUNIT.
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 [10] {ECO:0007744|PDB:3LGS}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH
RP S-ADENOSYL-L-HOMOCYSTEINE AND ADENINE, AND ACTIVE SITE.
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).
CC -!- FUNCTION: Enzyme of the methionine cycle that catalyzes the
CC irreversible cleavage of the glycosidic bond in 5'-methylthioadenosine
CC (MTA) to adenine and 5'-methylthioribose (PubMed:19249293,
CC PubMed:18342331). Contributes to the maintenance of AdoMet homeostasis
CC and is required to sustain high rates of ethylene synthesis. Inactive
CC towards S-adenosylhomocysteine (SAH/AdoHcy) (PubMed:18342331,
CC PubMed:19249293). {ECO:0000269|PubMed:17144895,
CC ECO:0000269|PubMed:18342331, ECO:0000269|PubMed:19249293,
CC ECO:0000269|PubMed:20345605}.
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=3.2.2.16;
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 -!- ACTIVITY REGULATION: Inhibited by CBL3 in a calcium-dependent manner
CC (PubMed:18945934). Inhibited by 5'-methylthiotubercidin (MTT) and by
CC formycin A (FMA) (PubMed:18342331). {ECO:0000269|PubMed:18342331,
CC ECO:0000269|PubMed:18945934}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=7.1 uM for 5'-methylthioadenosine (MTA)
CC {ECO:0000269|PubMed:18342331};
CC KM=27.6 uM for 5'-methylthioadenosine (MTA)
CC {ECO:0000269|PubMed:19249293};
CC Note=kcat is 18.7 sec(-1). {ECO:0000269|PubMed:18342331};
CC pH dependence:
CC Optimum pH is 8.0. {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 (PubMed:19249293, PubMed:16909418). Interacts with
CC CBL3 in a calcium-dependent manner. {ECO:0000269|PubMed:16909418,
CC ECO:0000269|PubMed:18342331, ECO:0000269|PubMed:18945934,
CC ECO:0000269|PubMed:19249293, ECO:0000269|PubMed:20554051}.
CC -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, cauline leaves
CC and flowers. {ECO:0000269|PubMed:18945934}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC condition. Not able to grow with methylthioadenosine (MTA) as unique
CC source of sulfur. {ECO:0000269|PubMed:20345605}.
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. MtnN
CC subfamily. {ECO:0000305}.
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DR EMBL; AL035656; CAB38614.1; -; Genomic_DNA.
DR EMBL; AL161594; CAB80543.1; -; Genomic_DNA.
DR EMBL; CP002687; AEE86976.1; -; Genomic_DNA.
DR EMBL; AF370297; AAK44112.1; -; mRNA.
DR EMBL; AY142681; AAN13219.1; -; mRNA.
DR PIR; T06079; T06079.
DR RefSeq; NP_195591.1; NM_120040.4.
DR PDB; 2H8G; X-ray; 1.50 A; A/B=1-267.
DR PDB; 2QSU; X-ray; 2.00 A; A/B=1-267.
DR PDB; 2QTG; X-ray; 1.84 A; A/B=1-267.
DR PDB; 2QTT; X-ray; 1.93 A; A/B=1-267.
DR PDB; 3LGS; X-ray; 2.20 A; A/B/C/D=1-267.
DR PDBsum; 2H8G; -.
DR PDBsum; 2QSU; -.
DR PDBsum; 2QTG; -.
DR PDBsum; 2QTT; -.
DR PDBsum; 3LGS; -.
DR AlphaFoldDB; Q9T0I8; -.
DR SMR; Q9T0I8; -.
DR BioGRID; 15315; 5.
DR IntAct; Q9T0I8; 2.
DR STRING; 3702.AT4G38800.1; -.
DR iPTMnet; Q9T0I8; -.
DR PaxDb; Q9T0I8; -.
DR PRIDE; Q9T0I8; -.
DR ProteomicsDB; 250984; -.
DR EnsemblPlants; AT4G38800.1; AT4G38800.1; AT4G38800.
DR GeneID; 830035; -.
DR Gramene; AT4G38800.1; AT4G38800.1; AT4G38800.
DR KEGG; ath:AT4G38800; -.
DR Araport; AT4G38800; -.
DR TAIR; locus:2141806; AT4G38800.
DR eggNOG; ENOG502QTZK; Eukaryota.
DR HOGENOM; CLU_067435_0_0_1; -.
DR OMA; KDKGACI; -.
DR OrthoDB; 1260657at2759; -.
DR PhylomeDB; Q9T0I8; -.
DR BioCyc; ARA:AT4G38800-MON; -.
DR BRENDA; 2.4.2.28; 399.
DR BRENDA; 3.2.2.9; 399.
DR UniPathway; UPA00904; UER00871.
DR EvolutionaryTrace; Q9T0I8; -.
DR PRO; PR:Q9T0I8; -.
DR Proteomes; UP000006548; Chromosome 4.
DR ExpressionAtlas; Q9T0I8; baseline and differential.
DR Genevisible; Q9T0I8; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA:TAIR.
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; Amino-acid biosynthesis; Hydrolase; Methionine biosynthesis;
KW Reference proteome.
FT CHAIN 1..267
FT /note="5'-methylthioadenosine nucleosidase"
FT /id="PRO_0000401373"
FT ACT_SITE 38
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:20554051"
FT ACT_SITE 225
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:20554051"
FT BINDING 116
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000305|PubMed:18342331,
FT ECO:0000305|PubMed:20554051, ECO:0007744|PDB:2QTT,
FT ECO:0007744|PDB:3LGS"
FT BINDING 199..202
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000305|PubMed:18342331,
FT ECO:0000305|PubMed:20554051, ECO:0007744|PDB:2QTT,
FT ECO:0007744|PDB:3LGS"
FT BINDING 199
FT /ligand="adenine"
FT /ligand_id="ChEBI:CHEBI:16708"
FT /evidence="ECO:0000269|PubMed:16909418,
FT ECO:0000269|PubMed:20554051, ECO:0007744|PDB:2H8G,
FT ECO:0007744|PDB:3LGS"
FT BINDING 225
FT /ligand="adenine"
FT /ligand_id="ChEBI:CHEBI:16708"
FT /evidence="ECO:0000269|PubMed:16909418,
FT ECO:0000269|PubMed:18342331, ECO:0000305|PubMed:20554051,
FT ECO:0007744|PDB:2H8G, ECO:0007744|PDB:2QTT,
FT ECO:0007744|PDB:3LGS"
FT BINDING 225
FT /ligand="S-methyl-5'-thioadenosine"
FT /ligand_id="ChEBI:CHEBI:17509"
FT /evidence="ECO:0000305|PubMed:18342331,
FT ECO:0000305|PubMed:20554051, ECO:0007744|PDB:2QTT,
FT ECO:0007744|PDB:3LGS"
FT STRAND 28..32
FT /evidence="ECO:0007829|PDB:2H8G"
FT HELIX 36..45
FT /evidence="ECO:0007829|PDB:2H8G"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:2H8G"
FT STRAND 72..78
FT /evidence="ECO:0007829|PDB:2H8G"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:2H8G"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2QSU"
FT HELIX 92..106
FT /evidence="ECO:0007829|PDB:2H8G"
FT STRAND 109..119
FT /evidence="ECO:0007829|PDB:2H8G"
FT HELIX 121..123
FT /evidence="ECO:0007829|PDB:2H8G"
FT STRAND 130..140
FT /evidence="ECO:0007829|PDB:2H8G"
FT HELIX 148..153
FT /evidence="ECO:0007829|PDB:2H8G"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:2H8G"
FT STRAND 171..177
FT /evidence="ECO:0007829|PDB:2H8G"
FT HELIX 185..193
FT /evidence="ECO:0007829|PDB:2H8G"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:2H8G"
FT HELIX 203..212
FT /evidence="ECO:0007829|PDB:2H8G"
FT STRAND 217..226
FT /evidence="ECO:0007829|PDB:2H8G"
FT STRAND 229..231
FT /evidence="ECO:0007829|PDB:2H8G"
FT HELIX 233..259
FT /evidence="ECO:0007829|PDB:2H8G"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:2H8G"
SQ SEQUENCE 267 AA; 28451 MW; E7F8A113441AA012 CRC64;
MAPHGDGLSD IEEPEVDAQS EILRPISSVV FVIAMQAEAL PLVNKFGLSE TTDSPLGKGL
PWVLYHGVHK DLRINVVCPG RDAALGIDSV GTVPASLITF ASIQALKPDI IINAGTCGGF
KVKGANIGDV FLVSDVVFHD RRIPIPMFDL YGVGLRQAFS TPNLLKELNL KIGRLSTGDS
LDMSTQDETL IIANDATLKD MEGAAVAYVA DLLKIPVVFL KAVTDLVDGD KPTAEEFLQN
LTVVTAALEG TATKVINFIN GRNLSDL
