(data stored in SCRATCH9089 zone)

SWISSPROT: MTNN_PASMU

ID   MTNN_PASMU              Reviewed;         229 AA.
AC   Q9CP62;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   11-DEC-2019, entry version 105.
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}; OrderedLocusNames=PM0194;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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.
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 = adenine + S-methyl-5-thio-D-
CC         ribose; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708,
CC         ChEBI:CHEBI:16895, ChEBI:CHEBI:17509; EC=3.2.2.9;
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   -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. MtnN
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01684}.
DR   EMBL; AE004439; AAK02278.1; -; Genomic_DNA.
DR   RefSeq; WP_010906521.1; NC_002663.1.
DR   SMR; Q9CP62; -.
DR   EnsemblBacteria; AAK02278; AAK02278; PM0194.
DR   GeneID; 29389154; -.
DR   KEGG; pmu:PM0194; -.
DR   eggNOG; ENOG4105DUF; Bacteria.
DR   eggNOG; COG0775; LUCA.
DR   HOGENOM; HOG000259346; -.
DR   KO; K01243; -.
DR   OMA; DQFVHSK; -.
DR   BioCyc; PMUL272843:G1FZ8-202-MONOMER; -.
DR   UniPathway; UPA00904; UER00871.
DR   Proteomes; UP000000809; 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; Q9CP62.
DR   SWISS-2DPAGE; Q9CP62.
KW   Amino-acid biosynthesis; Hydrolase; Methionine biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..229
FT                   /note="5'-methylthioadenosine/S-adenosylhomocysteine
FT                   nucleosidase"
FT                   /id="PRO_0000359320"
FT   REGION          173..174
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
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                   /note="Substrate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
FT   BINDING         152
FT                   /note="Substrate; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
SQ   SEQUENCE   229 AA;  24065 MW;  031789540DA3A585 CRC64;
     MKIGIVGAMA QEVQMLADLM QDKRVTQVAS CTIYEGMIHG KAVALLQSGI GKVAAAIGAT
     LLLEMCKPDL VINTGSAGGV ATGLNVGDIV ISDETVYHDA DVTAFGYAKG QLPACPARFQ
     SDEKLVQLAE KIAVQQQQQV KRGLICSGDS FIQGGTPLAQ IKADFPTVMA VEMEATAIAQ
     VCHAFNVPFV VVRAISDSGD GEASMSFEEF LPLAAKQSSA MVLEMIDNL
//

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