MTNN_STAAM
ID MTNN_STAAM Reviewed; 228 AA.
AC Q99TQ0;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
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'-deoxyadenosine nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
DE Short=DOA nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
DE Short=dAdo nucleosidase {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=SAV1599;
OS Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158878;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mu50 / ATCC 700699;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(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. Also cleaves
CC 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine
CC (SAM) enzymes, into 5-deoxyribose and adenine. {ECO:0000255|HAMAP-
CC 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 = 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:0000255|HAMAP-Rule:MF_01684};
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:0000255|HAMAP-Rule:MF_01684};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29860;
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}.
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DR EMBL; BA000017; BAB57761.1; -; Genomic_DNA.
DR RefSeq; WP_000579275.1; NC_002758.2.
DR PDB; 3BL6; X-ray; 1.70 A; A=1-228.
DR PDB; 4GMH; X-ray; 2.00 A; A=1-228.
DR PDBsum; 3BL6; -.
DR PDBsum; 4GMH; -.
DR AlphaFoldDB; Q99TQ0; -.
DR SMR; Q99TQ0; -.
DR World-2DPAGE; 0002:Q99TQ0; -.
DR PaxDb; Q99TQ0; -.
DR EnsemblBacteria; BAB57761; BAB57761; SAV1599.
DR KEGG; sav:SAV1599; -.
DR HOGENOM; CLU_031248_2_2_9; -.
DR OMA; DQFVHSK; -.
DR PhylomeDB; Q99TQ0; -.
DR BioCyc; SAUR158878:SAV_RS08595-MON; -.
DR BRENDA; 3.2.2.16; 3352.
DR BRENDA; 3.2.2.9; 3352.
DR UniPathway; UPA00904; UER00871.
DR EvolutionaryTrace; Q99TQ0; -.
DR Proteomes; UP000002481; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Hydrolase; Methionine biosynthesis.
FT CHAIN 1..228
FT /note="5'-methylthioadenosine/S-adenosylhomocysteine
FT nucleosidase"
FT /id="PRO_0000359369"
FT ACT_SITE 11
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
FT ACT_SITE 196
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
FT BINDING 172..173
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
FT STRAND 1..8
FT /evidence="ECO:0007829|PDB:3BL6"
FT HELIX 9..16
FT /evidence="ECO:0007829|PDB:3BL6"
FT STRAND 20..27
FT /evidence="ECO:0007829|PDB:3BL6"
FT STRAND 30..37
FT /evidence="ECO:0007829|PDB:3BL6"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:3BL6"
FT HELIX 51..65
FT /evidence="ECO:0007829|PDB:3BL6"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:3BL6"
FT STRAND 74..78
FT /evidence="ECO:0007829|PDB:3BL6"
FT STRAND 88..98
FT /evidence="ECO:0007829|PDB:3BL6"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:3BL6"
FT STRAND 116..119
FT /evidence="ECO:0007829|PDB:3BL6"
FT HELIX 122..134
FT /evidence="ECO:0007829|PDB:3BL6"
FT STRAND 139..146
FT /evidence="ECO:0007829|PDB:3BL6"
FT HELIX 154..163
FT /evidence="ECO:0007829|PDB:3BL6"
FT STRAND 167..173
FT /evidence="ECO:0007829|PDB:3BL6"
FT HELIX 174..184
FT /evidence="ECO:0007829|PDB:3BL6"
FT STRAND 188..196
FT /evidence="ECO:0007829|PDB:3BL6"
FT HELIX 202..225
FT /evidence="ECO:0007829|PDB:3BL6"
SQ SEQUENCE 228 AA; 24534 MW; C756E9386E9B19DD CRC64;
MIGIIGAMEE EVTILKNKLT QLSEISVAHV KFYTGILKDR EVVITQSGIG KVNAAISTTL
LINKFKPDVI INTGSAGALD ESLNVGDVLI SDDVKYHDAD ATAFGYEYGQ IPQMPVAFQS
SKPLIEKVSQ VVQQQQLTAK VGLIVSGDSF IGSVEQRQKI KKAFPNAMAV EMEATAIAQT
CYQFNVPFVV VRAVSDLANG EAEMSFEAFL EKAAVSSSQT VEALVSQL
