MTNN_THEMA
ID MTNN_THEMA Reviewed; 217 AA.
AC Q9X0L3;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase {ECO:0000250|UniProtKB:P0AF12};
DE Short=MTA/SAH nucleosidase {ECO:0000250|UniProtKB:P0AF12};
DE Short=MTAN {ECO:0000250|UniProtKB:P0AF12};
DE EC=3.2.2.9 {ECO:0000250|UniProtKB:P0AF12};
DE AltName: Full=5'-deoxyadenosine nucleosidase {ECO:0000250|UniProtKB:P0AF12};
DE Short=DOA nucleosidase {ECO:0000250|UniProtKB:P0AF12};
DE Short=dAdo nucleosidase {ECO:0000250|UniProtKB:P0AF12};
DE AltName: Full=5'-methylthioadenosine nucleosidase {ECO:0000250|UniProtKB:P0AF12};
DE Short=MTA nucleosidase {ECO:0000250|UniProtKB:P0AF12};
DE AltName: Full=S-adenosylhomocysteine nucleosidase {ECO:0000250|UniProtKB:P0AF12};
DE Short=AdoHcy nucleosidase {ECO:0000250|UniProtKB:P0AF12};
DE Short=SAH nucleosidase {ECO:0000250|UniProtKB:P0AF12};
DE Short=SRH nucleosidase {ECO:0000250|UniProtKB:P0AF12};
GN Name=mtnN; Synonyms=mtn; OrderedLocusNames=TM_1129;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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.
CC {ECO:0000250|UniProtKB:P0AF12}.
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:0000250|UniProtKB:P0AF12};
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:0000250|UniProtKB:P0AF12};
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:0000250|UniProtKB:P0AF12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29860;
CC Evidence={ECO:0000250|UniProtKB:P0AF12};
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 {ECO:0000250|UniProtKB:P0AF12}.
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. MtnN
CC subfamily. {ECO:0000305}.
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DR EMBL; AE000512; AAD36205.1; -; Genomic_DNA.
DR PIR; F72293; F72293.
DR RefSeq; NP_228935.1; NC_000853.1.
DR RefSeq; WP_004080281.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9X0L3; -.
DR SMR; Q9X0L3; -.
DR STRING; 243274.THEMA_08700; -.
DR DNASU; 898635; -.
DR EnsemblBacteria; AAD36205; AAD36205; TM_1129.
DR KEGG; tma:TM1129; -.
DR eggNOG; COG0775; Bacteria.
DR InParanoid; Q9X0L3; -.
DR OMA; HDMDVTP; -.
DR OrthoDB; 1860206at2; -.
DR UniPathway; UPA00904; UER00871.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008782; F:adenosylhomocysteine nucleosidase activity; IBA:GO_Central.
DR GO; GO:0008930; F:methylthioadenosine nucleosidase activity; IBA:GO_Central.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IBA:GO_Central.
DR GO; GO:0009164; P:nucleoside catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1580; -; 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;
KW Reference proteome.
FT CHAIN 1..217
FT /note="5'-methylthioadenosine/S-adenosylhomocysteine
FT nucleosidase"
FT /id="PRO_0000164450"
FT ACT_SITE 11
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AF12"
FT ACT_SITE 183
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0AF12"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF12"
FT BINDING 139
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF12"
FT BINDING 159..160
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF12"
SQ SEQUENCE 217 AA; 24166 MW; CF9AE5F0F0F4AA16 CRC64;
MILVLGVFKI EVEPMLKEME VLEKGRLLKR YYQRGVVGRN EVVVSYGFIG KVEAALVTQA
FLDRFNIDAV FLTGNAGGLE GVEVGDVVIG DSYVEYDFET ALGDEGIIVS GSEDLEDKVI
AYSNREIKTG LIASGDAFVT VKEKAEEIKR RTGALCVDMD SAAVAKVCYE NEKKFLAIKT
IVDICGRETE EEFRKNYERY GFLSNLILLD VLKKCVF
