ID Q5F9P8_NEIG1 Unreviewed; 233 AA.
AC Q5F9P8;
DT 15-MAR-2005, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2005, sequence version 1.
DT 27-MAR-2024, entry version 111.
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=NGO_0345 {ECO:0000313|EMBL:AAW89089.1};
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231 {ECO:0000313|EMBL:AAW89089.1, ECO:0000313|Proteomes:UP000000535};
RN [1] {ECO:0000313|Proteomes:UP000000535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090 {ECO:0000313|Proteomes:UP000000535};
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) 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}.
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DR EMBL; AE004969; AAW89089.1; -; Genomic_DNA.
DR RefSeq; WP_003687752.1; NC_002946.2.
DR RefSeq; YP_207501.1; NC_002946.2.
DR AlphaFoldDB; Q5F9P8; -.
DR STRING; 242231.NGO_0345; -.
DR GeneID; 66752685; -.
DR KEGG; ngo:NGO_0345; -.
DR PATRIC; fig|242231.10.peg.421; -.
DR HOGENOM; CLU_031248_2_2_4; -.
DR UniPathway; UPA00904; UER00871.
DR Proteomes; UP000000535; 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 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:AAW89089.1};
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:UP000000535}.
FT DOMAIN 5..231
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT ACT_SITE 15
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01684"
FT ACT_SITE 201
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01684"
FT BINDING 81
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01684"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01684"
FT BINDING 177..178
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01684"
SQ SEQUENCE 233 AA; 24806 MW; AFBBD9C83675B0AF CRC64;
MSLKTVAVIG AMEQEIELLR EMMENVKAVS FGRFSAYEGE LAGKRIVLAL SGIGKVNAAV
ATAWLIRQFA PDCVINTGSA GGLGKGLKVG DVVIGTETEH HDVDVTAFGY ARGQVPQLPA
RFASDGILIE TAKRAARTFE GAEVEQGLIV SGDRFVHSSE GVAEIRKHFP EVKAVEMEAA
AIAQTCHQLE TPFVIIRAVS DSADEKADIS FEEFLKTAAA SSAKMVAEIV KSL
//
