ID E3G919_ENTLS Unreviewed; 232 AA.
AC E3G919;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 79.
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 OrderedLocusNames=Entcl_3575 {ECO:0000313|EMBL:ADO49816.1};
OS Enterobacter lignolyticus (strain SCF1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Pluralibacter.
OX NCBI_TaxID=701347 {ECO:0000313|EMBL:ADO49816.1, ECO:0000313|Proteomes:UP000006872};
RN [1] {ECO:0000313|Proteomes:UP000006872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCF1 {ECO:0000313|Proteomes:UP000006872};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Davenport K., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Chang Y.-J., Jeffries C., Kyrpides N., Ivanova N.,
RA Mikhailova N., DeAngelis K., Arkin A.P., Chivian D., Edwards B., Woo H.,
RA Hazen T.C., Woyke T.;
RT "Complete sequence of Enterobacter cloacae SCF1.";
RL Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADO49816.1, ECO:0000313|Proteomes:UP000006872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCF1 {ECO:0000313|EMBL:ADO49816.1,
RC ECO:0000313|Proteomes:UP000006872};
RX PubMed=22180812; DOI=10.4056/sigs.2104875;
RA Deangelis K.M., D'Haeseleer P., Chivian D., Fortney J.L., Khudyakov J.,
RA Simmons B., Woo H., Arkin A.P., Davenport K.W., Goodwin L., Chen A.,
RA Ivanova N., Kyrpides N.C., Mavromatis K., Woyke T., Hazen T.C.;
RT "Complete genome sequence of "Enterobacter lignolyticus" SCF1.";
RL Stand. Genomic Sci. 5:69-85(2011).
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. Thus, is required for in
CC vivo function of the radical SAM enzymes biotin synthase and lipoic
CC acid synthase, that are inhibited by 5'-deoxyadenosine accumulation.
CC {ECO:0000256|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: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 -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_01684}.
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. MtnN
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01684}.
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DR EMBL; CP002272; ADO49816.1; -; Genomic_DNA.
DR RefSeq; WP_013367541.1; NC_014618.1.
DR AlphaFoldDB; E3G919; -.
DR STRING; 701347.Entcl_3575; -.
DR KEGG; esc:Entcl_3575; -.
DR eggNOG; COG0775; Bacteria.
DR HOGENOM; CLU_031248_2_2_6; -.
DR UniPathway; UPA00904; UER00871.
DR Proteomes; UP000006872; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProt.
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:0046124; P:purine deoxyribonucleoside catabolic process; IEA:UniProtKB-UniRule.
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}; Glycosidase {ECO:0000313|EMBL:ADO49816.1};
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}; Reference proteome {ECO:0000313|Proteomes:UP000006872}.
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 197
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 152
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01684"
FT BINDING 173..174
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01684"
SQ SEQUENCE 232 AA; 24287 MW; 65886F2F6444215A CRC64;
MKIGIIGAME EEVTLLRDKI DNRQTITIGG SEIYTGQLNG ADVALLKSGI GKVAAAMGAA
LLIERCKPDV IINTGSAGGL AAELKVGDIV VSDEARYHDA DVTAFGYEYG QLPGCPAGFA
ADARLVDAAE NCIKALKLNA VRGLIVSGDA FINGSVGLAK IRHNFPQAIA VEMEATAIAH
VCHNFGVPFV VVRAISDVAD QQSHLSFDEF LAVAAKQSSL MVETLVQKLA HA
//
