MTNN_MYCTO
ID MTNN_MYCTO Reviewed; 255 AA.
AC P9WJM2; L0T5N1; P67656; Q10889;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
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=MT0100;
OS Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 1551 / Oshkosh;
RX PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT laboratory strains.";
RL J. Bacteriol. 184:5479-5490(2002).
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; AE000516; AAK44323.1; -; Genomic_DNA.
DR PIR; C70750; C70750.
DR RefSeq; WP_003400678.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WJM2; -.
DR SMR; P9WJM2; -.
DR EnsemblBacteria; AAK44323; AAK44323; MT0100.
DR KEGG; mtc:MT0100; -.
DR PATRIC; fig|83331.31.peg.105; -.
DR HOGENOM; CLU_031248_2_0_11; -.
DR UniPathway; UPA00904; UER00871.
DR Proteomes; UP000001020; Chromosome.
DR GO; GO:0008782; F:adenosylhomocysteine nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008930; F:methylthioadenosine nucleosidase activity; IEA:RHEA.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1580; -; 1.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Hydrolase; Methionine biosynthesis.
FT CHAIN 1..255
FT /note="5'-methylthioadenosine/S-adenosylhomocysteine
FT nucleosidase"
FT /id="PRO_0000427805"
FT ACT_SITE 14
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AF12"
FT ACT_SITE 220
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0AF12"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF12"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF12"
FT BINDING 196..197
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF12"
SQ SEQUENCE 255 AA; 27340 MW; EA80AA80B2BFEE79 CRC64;
MAVTVGVICA IPQELAYLRG VLVDAKRQQV AQILFDSGQL DAHRVVLAAA GMGKVNTGLT
ATLLADRFGC RTIVFTGVAG GLDPELCIGD IVIADRVVQH DFGLLTDERL RPYQPGHIPF
IEPTERLGYP VDPAVIDRVK HRLDGFTLAP LSTAAGGGGR QPRIYYGTIL TGDQYLHCER
TRNRLHHELG GMAVEMEGGA VAQICASFDI PWLVIRALSD LAGADSGVDF NRFVGEVAAS
SARVLLRLLP VLTAC
