ID MTNN_SHEHH Reviewed; 230 AA. AC B0TIS5; DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 02-SEP-2026, entry version 86. DE RecName: Full=5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE Short=MTA/SAH nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE Short=MTAN {ECO:0000255|HAMAP-Rule:MF_01684}; DE EC=3.2.2.9 {ECO:0000255|HAMAP-Rule:MF_01684}; DE AltName: Full=5'-deoxyadenosine nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE Short=DOA nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE Short=dAdo nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE AltName: Full=5'-methylthioadenosine nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE Short=MTA nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE AltName: Full=S-adenosylhomocysteine nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE Short=AdoHcy nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE Short=SAH nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; DE Short=SRH nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684}; GN Name=mtnN {ECO:0000255|HAMAP-Rule:MF_01684}; GN OrderedLocusNames=Shal_1051; OS Shewanella halifaxensis (strain HAW-EB4). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Alteromonadales; Shewanellaceae; Shewanella. OX NCBI_TaxID=458817; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HAW-EB4; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C., RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Zhao J.-S., Richardson P.; RT "Complete sequence of Shewanella halifaxensis HAW-EB4."; RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the irreversible cleavage of the glycosidic bond in CC both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine CC (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'- CC methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves CC 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine CC (SAM) enzymes, into 5-deoxyribose and adenine. {ECO:0000255|HAMAP- CC Rule:MF_01684}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-adenosyl-L-homocysteine + H2O = S-(5-deoxy-D-ribos-5-yl)-L- CC homocysteine + adenine; 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:0000255|HAMAP-Rule:MF_01684}; CC -!- CATALYTIC ACTIVITY: CC Reaction=S-methyl-5'-thioadenosine + H2O = 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:0000255|HAMAP-Rule:MF_01684}; 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:0000255|HAMAP-Rule:MF_01684}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29860; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01684}; 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. {ECO:0000255|HAMAP- CC Rule:MF_01684}. CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. MtnN CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01684}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000931; ABZ75620.1; -; Genomic_DNA. DR RefSeq; WP_012276167.1; NC_010334.1. DR AlphaFoldDB; B0TIS5; -. DR SMR; B0TIS5; -. DR STRING; 458817.Shal_1051; -. DR KEGG; shl:Shal_1051; -. DR eggNOG; COG0775; Bacteria. DR HOGENOM; CLU_031248_2_2_6; -. DR OrthoDB; 9792278at2; -. DR UniPathway; UPA00904; UER00871. DR Proteomes; UP000001317; Chromosome. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0008782; F:adenosylhomocysteine nucleosidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0008930; F:methylthioadenosine nucleosidase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009164; P:nucleoside catabolic process; IEA:InterPro. DR CDD; cd09008; MTAN; 1. DR FunFam; 3.40.50.1580:FF:000001; MTA/SAH nucleosidase family protein; 1. DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1. DR HAMAP; MF_01684; Salvage_MtnN; 1. DR InterPro; IPR010049; MTA_SAH_Nsdase. DR InterPro; IPR000845; Nucleoside_phosphorylase_d. DR InterPro; IPR035994; Nucleoside_phosphorylase_sf. DR NCBIfam; TIGR01704; MTA_SAH-Nsdase; 1. DR NCBIfam; NF004079; PRK05584.1; 1. DR PANTHER; PTHR46832; 5'-METHYLTHIOADENOSINE/S-ADENOSYLHOMOCYSTEINE NUCLEOSIDASE; 1. DR PANTHER; PTHR46832:SF1; 5'-METHYLTHIOADENOSINE_S-ADENOSYLHOMOCYSTEINE NUCLEOSIDASE; 1. DR Pfam; PF01048; PNP_UDP_1; 1. DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Hydrolase; Methionine biosynthesis; KW Reference proteome. FT CHAIN 1..230 FT /note="5'-methylthioadenosine/S-adenosylhomocysteine FT nucleosidase" FT /id="PRO_0000359345" FT ACT_SITE 12 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01684" FT ACT_SITE 198 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01684" FT BINDING 78 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01684" FT BINDING 153 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01684" FT BINDING 174..175 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01684" SQ SEQUENCE 230 AA; 24128 MW; E5D880A90C1706C4 CRC64; MKIGIIGAME PEVAHLVESM ENPSSTTIAG IEFVAGQLAG KDVIVTRSGI GKVTASIATT LLIEKYAPDV IINTGSAGGF ADELAIGDIV ISSEVRHHDV DVTAFGYEIG QMAQQPAAFI PDAKLVAAAQ KAVASLGEVK AIEGLICTGD SFICDPVRTK TMLENFPTMA ACEMEGAAIA QVCHQFGVPF VVIRSLSDNA NNDSPVDFDE YIVKAGHHSA LMVIALLKQL //