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ID MTNN_SHISS Reviewed; 232 AA.
AC Q3Z5J8;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 08-MAY-2019, entry version 84.
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'-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=SSON_0171;
OS Shigella sonnei (strain Ss046).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300269;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ss046;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA Qiang B., Hou Y., Yu J., Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic
RT agents of bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
CC -!- FUNCTION: Catalyzes the irreversible cleavage of the glycosidic
CC bond in both 5'-methylthioadenosine (MTA) and S-
CC adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding
CC thioribose, 5'-methylthioribose and S-ribosylhomocysteine,
CC respectively. {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,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:58195; EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01684};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + S-methyl-5'-thioadenosine = adenine + S-methyl-5-
CC thio-D-ribose; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16708, ChEBI:CHEBI:16895, ChEBI:CHEBI:17509;
CC EC=3.2.2.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01684};
CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via
CC salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from
CC S-methyl-5'-thioadenosine (hydrolase route): step 1/2.
CC {ECO:0000255|HAMAP-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}.
DR EMBL; CP000038; AAZ86964.1; -; Genomic_DNA.
DR SMR; Q3Z5J8; -.
DR EnsemblBacteria; AAZ86964; AAZ86964; SSON_0171.
DR KEGG; ssn:SSON_0171; -.
DR HOGENOM; HOG000259346; -.
DR KO; K01243; -.
DR OMA; DQFVHSK; -.
DR BioCyc; SSON300269:G1GL2-198-MONOMER; -.
DR UniPathway; UPA00904; UER00871.
DR Proteomes; UP000002529; Chromosome.
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;
DR PRODOM; Q3Z5J8.
DR SWISS-2DPAGE; Q3Z5J8.
KW Amino-acid biosynthesis; Complete proteome; Hydrolase;
KW Methionine biosynthesis.
FT CHAIN 1 232 5'-methylthioadenosine/S-
FT adenosylhomocysteine nucleosidase.
FT /FTId=PRO_0000359360.
FT REGION 173 174 Substrate binding. {ECO:0000255|HAMAP-
FT Rule:MF_01684}.
FT ACT_SITE 12 12 Proton acceptor. {ECO:0000255|HAMAP-
FT Rule:MF_01684}.
FT ACT_SITE 197 197 Proton donor. {ECO:0000255|HAMAP-
FT Rule:MF_01684}.
FT BINDING 78 78 Substrate; via amide nitrogen.
FT {ECO:0000255|HAMAP-Rule:MF_01684}.
FT BINDING 152 152 Substrate; via amide nitrogen and
FT carbonyl oxygen. {ECO:0000255|HAMAP-
FT Rule:MF_01684}.
SQ SEQUENCE 232 AA; 24354 MW; 9B1FF9BEC39D4F2C CRC64;
MKIGIIGAME EEVTLLRDKI ENRQTISLGG CEIYTGQLNG TEVALLKSGI GKVAAALGAT
LLLEHCKPDV IINTGSAGGL APTLKVGDIV VSDEARYHDA DVTAFGYEYG QLPGCPAGFK
ADDKLIAAAE ACIAELNLNA VRGLIVSGDA FINGSVGLAK IRHNFPQAIA VEMEATAIAH
VCHNFNVPFV VVRAISDVAD QQSHLSFDEF LAVAAKQSSL MVESLVQKLA HG
//
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