(data stored in ACNUC7421 zone)

SWISSPROT: MTNN_SHISS

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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