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MTNN_BUCA5
ID   MTNN_BUCA5              Reviewed;         232 AA.
AC   B8D909;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-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=BUAP5A_207;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain 5A).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=563178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=5A;
RX   PubMed=19150844; DOI=10.1126/science.1167140;
RA   Moran N.A., McLaughlin H.J., Sorek R.;
RT   "The dynamics and time scale of ongoing genomic erosion in symbiotic
RT   bacteria.";
RL   Science 323:379-382(2009).
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. Thus, is required for in
CC       vivo function of the radical SAM enzymes biotin synthase and lipoic
CC       acid synthase, that are inhibited by 5'-deoxyadenosine accumulation.
CC       {ECO:0000255|HAMAP-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   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-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; CP001161; ACL30580.1; -; Genomic_DNA.
DR   RefSeq; WP_009874168.1; NC_011833.1.
DR   AlphaFoldDB; B8D909; -.
DR   SMR; B8D909; -.
DR   KEGG; bap:BUAP5A_207; -.
DR   HOGENOM; CLU_031248_2_2_6; -.
DR   OMA; DQFVHSK; -.
DR   OrthoDB; 1860206at2; -.
DR   UniPathway; UPA00904; UER00871.
DR   Proteomes; UP000006904; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:0046124; P:purine deoxyribonucleoside catabolic process; IEA:UniProtKB-UniRule.
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..232
FT                   /note="5'-methylthioadenosine/S-adenosylhomocysteine
FT                   nucleosidase"
FT                   /id="PRO_1000187414"
FT   ACT_SITE        12
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
FT   ACT_SITE        197
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         152
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
FT   BINDING         173..174
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
SQ   SEQUENCE   232 AA;  26266 MW;  F109382AA7C767BB CRC64;
     MKIGIIGAIN QETERLKKII HFYIEKKINT YKIYIGKFKS HDVFLIKSGI GKVSASIATM
     ILIDLYKPDT IINSGSAGSL QSFLKIGDII IPKKTCYYDV DLTNFGYTRG QIPGYPKEFT
     VNEKICNFFK KNADKYQLKY IKGLILSGDT FVRENESIKI LKKQFPSAIA VEMESSAIAQ
     VCYKFNIPLI IIKSISDASD NNATVNFKEN IDIVSYQLSK FVKIILENLI DM
 
 
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