ID A0A1Q8Q7X3_9BACI Unreviewed; 233 AA.
AC A0A1Q8Q7X3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=BTO30_05570 {ECO:0000313|EMBL:OLN23430.1};
OS Domibacillus antri.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Domibacillus.
OX NCBI_TaxID=1714264 {ECO:0000313|EMBL:OLN23430.1, ECO:0000313|Proteomes:UP000185568};
RN [1] {ECO:0000313|EMBL:OLN23430.1, ECO:0000313|Proteomes:UP000185568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XD80 {ECO:0000313|EMBL:OLN23430.1,
RC ECO:0000313|Proteomes:UP000185568};
RA Verma A., Krishnamurthi S.;
RT "Domibacillus antri genome sequencing.";
RL Submitted (DEC-2016) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLN23430.1}.
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DR EMBL; MSDU01000008; OLN23430.1; -; Genomic_DNA.
DR RefSeq; WP_075397721.1; NZ_MSDU01000008.1.
DR AlphaFoldDB; A0A1Q8Q7X3; -.
DR STRING; 1714264.BTO30_05570; -.
DR OrthoDB; 9792278at2; -.
DR UniPathway; UPA00904; UER00871.
DR Proteomes; UP000185568; Unassembled WGS sequence.
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 CDD; cd09008; MTAN; 1.
DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 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 NCBIfam; TIGR01704; MTA_SAH-Nsdase; 1.
DR PANTHER; PTHR46832; 5'-METHYLTHIOADENOSINE/S-ADENOSYLHOMOCYSTEINE NUCLEOSIDASE; 1.
DR PANTHER; PTHR46832:SF1; 5'-METHYLTHIOADENOSINE_S-ADENOSYLHOMOCYSTEINE NUCLEOSIDASE; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01684};
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="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT ACT_SITE 12
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01684"
FT ACT_SITE 198
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01684"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01684"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01684"
FT BINDING 174..175
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01684"
SQ SEQUENCE 233 AA; 25050 MW; A9F37D26379C9D8F CRC64;
MKIGIIGAME EEVLILRDEM EKKEVTTIAG SEFTTGLLRG VEVVLLRSGI GKVNASMTTA
VLIHAFKPDV IINTGSAGGL SPELQVGDVV ISSEVRHHDV DVTAFGYEYG QVPQLPAAFQ
ADERLVQIAA ACAESIQEVK TVKGLIATGD SFMNDPVRVQ SIAEKFTDLQ AVEMEAAAIA
QVAYQFNVPF VIIRALSDIA GKESNISFEQ FLPKAGLHSA NLVMKMTEEL GKE
//
