MTNN_TREPA
ID MTNN_TREPA Reviewed; 269 AA.
AC P96122; O83200;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase {ECO:0000250|UniProtKB:P0AF12};
DE Short=MTA/SAH nucleosidase {ECO:0000250|UniProtKB:P0AF12};
DE Short=MTAN {ECO:0000250|UniProtKB:P0AF12};
DE EC=3.2.2.9 {ECO:0000250|UniProtKB:P0AF12};
DE AltName: Full=5'-deoxyadenosine nucleosidase {ECO:0000250|UniProtKB:P0AF12};
DE Short=DOA nucleosidase {ECO:0000250|UniProtKB:P0AF12};
DE Short=dAdo nucleosidase {ECO:0000250|UniProtKB:P0AF12};
DE AltName: Full=5'-methylthioadenosine nucleosidase {ECO:0000250|UniProtKB:P0AF12};
DE Short=MTA nucleosidase {ECO:0000250|UniProtKB:P0AF12};
DE AltName: Full=S-adenosylhomocysteine nucleosidase {ECO:0000250|UniProtKB:P0AF12};
DE Short=AdoHcy nucleosidase {ECO:0000250|UniProtKB:P0AF12};
DE Short=SAH nucleosidase {ECO:0000250|UniProtKB:P0AF12};
DE Short=SRH nucleosidase {ECO:0000250|UniProtKB:P0AF12};
GN Name=mtnN; Synonyms=mtn; OrderedLocusNames=TP_0170;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9332349; DOI=10.1016/s0378-1119(97)00234-5;
RA Hardham J.M., Stamm L.V., Porcella S.F., Frye J.G., Barnes N.Y.,
RA Howell J.K., Mueller S.L., Radolf J.D., Weinstock G.M., Norris S.J.;
RT "Identification and transcriptional analysis of a Treponema pallidum operon
RT encoding a putative ABC transport system, an iron-activated repressor
RT protein homolog, and a glycolytic pathway enzyme homolog.";
RL Gene 197:47-64(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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.
CC {ECO:0000250|UniProtKB:P0AF12}.
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:0000250|UniProtKB:P0AF12};
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:0000250|UniProtKB:P0AF12};
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:0000250|UniProtKB:P0AF12};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29860;
CC Evidence={ECO:0000250|UniProtKB:P0AF12};
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:0000250|UniProtKB:P0AF12}.
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. MtnN
CC subfamily. {ECO:0000305}.
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DR EMBL; U55214; AAC45731.1; -; Genomic_DNA.
DR EMBL; AE000520; AAC65159.1; -; Genomic_DNA.
DR PIR; G71357; G71357.
DR RefSeq; WP_010881617.1; NC_021490.2.
DR AlphaFoldDB; P96122; -.
DR SMR; P96122; -.
DR IntAct; P96122; 3.
DR STRING; 243276.TPANIC_0170; -.
DR EnsemblBacteria; AAC65159; AAC65159; TP_0170.
DR GeneID; 57878712; -.
DR KEGG; tpa:TP_0170; -.
DR eggNOG; COG0775; Bacteria.
DR HOGENOM; CLU_031248_2_0_12; -.
DR OMA; DQFVHSK; -.
DR OrthoDB; 1860206at2; -.
DR UniPathway; UPA00904; UER00871.
DR Proteomes; UP000000811; Chromosome.
DR GO; GO:0008782; F:adenosylhomocysteine nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008930; F:methylthioadenosine nucleosidase activity; IEA:InterPro.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR GO; GO:0009164; P:nucleoside catabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1580; -; 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; Hydrolase; Methionine biosynthesis;
KW Reference proteome.
FT CHAIN 1..269
FT /note="5'-methylthioadenosine/S-adenosylhomocysteine
FT nucleosidase"
FT /id="PRO_0000164451"
FT ACT_SITE 12
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AF12"
FT ACT_SITE 218
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0AF12"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF12"
FT BINDING 174
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF12"
FT BINDING 194..195
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF12"
FT CONFLICT 242..269
FT /note="ALLTLRVLERLSALRTSVVASLFPMVVV -> SPFDVACS (in Ref. 1;
FT AAC45731)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 269 AA; 28666 MW; 20F16DEADFA2E2E6 CRC64;
MTVGVFAALG EEVARVRECL GGVGTERAGL TFYVVSVGAL QVVYVCGGVG KVNAALCTQL
LISEFGARVL INTGIAGALD ERLCVFDVLV SVDAVQHDVD VTAFGYQKGR IPRMDSVEWT
ANTALRYLVR EAFDLCTRDP EWTEGACALS GSGDPPSRVS RLVEGRVASG DLFVSDAQTR
ARIIREFGAH GVEMEGAAFA HVASVNGVPF VIIRCISDGA GAEQDVSMSY KEFSTRAARR
SALLTLRVLE RLSALRTSVV ASLFPMVVV
