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MTNN_LISMC
ID   MTNN_LISMC              Reviewed;         233 AA.
AC   C1KVE1;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   03-AUG-2022, entry version 65.
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}; OrderedLocusNames=Lm4b_01504;
OS   Listeria monocytogenes serotype 4b (strain CLIP80459).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=568819;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIP80459;
RX   PubMed=22530965; DOI=10.1186/1471-2164-13-144;
RA   Hain T., Ghai R., Billion A., Kuenne C.T., Steinweg C., Izar B.,
RA   Mohamed W., Mraheil M., Domann E., Schaffrath S., Karst U., Goesmann A.,
RA   Oehm S., Puhler A., Merkl R., Vorwerk S., Glaser P., Garrido P.,
RA   Rusniok C., Buchrieser C., Goebel W., Chakraborty T.;
RT   "Comparative genomics and transcriptomics of lineages I, II, and III
RT   strains of Listeria monocytogenes.";
RL   BMC Genomics 13:144-144(2012).
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=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:0000255|HAMAP-Rule:MF_01684};
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: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}.
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DR   EMBL; FM242711; CAS05266.1; -; Genomic_DNA.
DR   RefSeq; WP_003725969.1; NC_012488.1.
DR   AlphaFoldDB; C1KVE1; -.
DR   SMR; C1KVE1; -.
DR   KEGG; lmc:Lm4b_01504; -.
DR   HOGENOM; CLU_031248_2_2_9; -.
DR   OMA; DQFVHSK; -.
DR   BioCyc; LMON568819:LM4B_RS07500-MON; -.
DR   UniPathway; UPA00904; UER00871.
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:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IEA:UniProtKB-UniRule.
DR   GO; GO:0009164; P:nucleoside catabolic process; IEA:InterPro.
DR   Gene3D; 3.40.50.1580; -; 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   Pfam; PF01048; PNP_UDP_1; 1.
DR   SUPFAM; SSF53167; SSF53167; 1.
DR   TIGRFAMs; TIGR01704; MTA/SAH-Nsdase; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis; Hydrolase; Methionine biosynthesis.
FT   CHAIN           1..233
FT                   /note="5'-methylthioadenosine/S-adenosylhomocysteine
FT                   nucleosidase"
FT                   /id="PRO_1000215914"
FT   ACT_SITE        12
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
FT   ACT_SITE        201
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         156
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
FT   BINDING         177..178
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
SQ   SEQUENCE   233 AA;  25305 MW;  9FC7901465F903F2 CRC64;
     MTIGIIGAME EEVELLKNSM PSVEEIVIGG AKFYVGEIAG KEVVLLESGI GKVNAALGTT
     LMADRFKPEV IINTGSAGGM AEGLAVGDVI ISDRLAYGDV DVTEFGYTYG QVPRMPAFYQ
     GDAVLLKKAE TIYREYFAAS ENKAVYGLVV TNDSFIMRPD QHETIRTFFP DVKAVEMEAA
     AIAQVAYQFD IPFLIIRAIS DLANQEATIS FDEFIHLAAK QSATCIIELL KTI
 
 
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