ID A0A8B0GLG6_9LACT Unreviewed; 229 AA. AC A0A8B0GLG6; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 19-JAN-2022, entry version 2. DE RecName: Full=5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase {ECO:0000256|HAMAP-Rule:MF_01684}; DE Short=MTA/SAH nucleosidase {ECO:0000256|HAMAP-Rule:MF_01684}; DE Short=MTAN {ECO:0000256|HAMAP-Rule:MF_01684}; DE EC=3.2.2.9 {ECO:0000256|HAMAP-Rule:MF_01684}; DE AltName: Full=5'-deoxyadenosine nucleosidase {ECO:0000256|HAMAP-Rule:MF_01684}; DE Short=DOA nucleosidase {ECO:0000256|HAMAP-Rule:MF_01684}; DE Short=dAdo nucleosidase {ECO:0000256|HAMAP-Rule:MF_01684}; DE AltName: Full=5'-methylthioadenosine nucleosidase {ECO:0000256|HAMAP-Rule:MF_01684}; DE Short=MTA nucleosidase {ECO:0000256|HAMAP-Rule:MF_01684}; DE AltName: Full=S-adenosylhomocysteine nucleosidase {ECO:0000256|HAMAP-Rule:MF_01684}; DE Short=AdoHcy nucleosidase {ECO:0000256|HAMAP-Rule:MF_01684}; DE Short=SAH nucleosidase {ECO:0000256|HAMAP-Rule:MF_01684}; DE Short=SRH nucleosidase {ECO:0000256|HAMAP-Rule:MF_01684}; GN Name=mtnN {ECO:0000256|HAMAP-Rule:MF_01684}; GN ORFNames=J7S27_03325 {ECO:0000313|EMBL:QTU83567.1}; OS Carnobacteriaceae bacterium zg-C25. OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Carnobacteriaceae; OC unclassified Carnobacteriaceae. OX NCBI_TaxID=2821731 {ECO:0000313|EMBL:QTU83567.1}; RN [1] {ECO:0000313|EMBL:QTU83567.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=Zg-C25 {ECO:0000313|EMBL:QTU83567.1}; RA Zhang G.; RT "Novel species in family Carnobacteriaceae."; RL Submitted (APR-2021) to the EMBL/GenBank/DDBJ databases. 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:0000256|HAMAP- CC 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:0000256|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:0000256|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:0000256|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. CC {ECO:0000256|ARBA:ARBA00004945, ECO:0000256|HAMAP-Rule:MF_01684}. CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. MtnN CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01684}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP072828; QTU83567.1; -; Genomic_DNA. DR UniPathway; UPA00904; UER00871. DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:UniProtKB-KW. DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW. 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; KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP- KW Rule:MF_01684}; Glycosidase {ECO:0000313|EMBL:QTU83567.1}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01684}; KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167, ECO:0000256|HAMAP- KW Rule:MF_01684}. FT DOMAIN 2..226 FT /note="PNP_UDP_1" FT /evidence="ECO:0000259|Pfam:PF01048" FT REGION 173..174 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01684" FT ACT_SITE 12 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01684" FT ACT_SITE 197 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01684" FT BINDING 78 FT /note="Substrate; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01684" FT BINDING 152 FT /note="Substrate; via amide nitrogen and carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01684" SQ SEQUENCE 229 AA; 25006 MW; C68ADB1A34D7B02C CRC64; MKIGIIGAMA QETKLLLEQM VDVTTEVKHH LTFYSGTLQN REVVLVQSGI GKVASAIATT LLVTHFSIDY VINTGSAGSL NPNLHIGNVV ISNQVAYHDV EATAFGYQHG QVPQMPLYYV ADERLINAAT KALNTIQSTR FVGEIVSSDS FIAEKSKIED IKEHFPNALC TEMEGASIAQ ACHILNVPFI VIRAISDNAN EEAHMTFDEF IILAGETSAK MVMNMLTHL //