MTNN_VIBCH
ID MTNN_VIBCH Reviewed; 231 AA.
AC Q9KPI8;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
DE Short=MTA/SAH nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
DE Short=MTAN {ECO:0000255|HAMAP-Rule:MF_01684};
DE EC=3.2.2.9 {ECO:0000255|HAMAP-Rule:MF_01684};
DE AltName: Full=5'-deoxyadenosine nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
DE Short=DOA nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
DE Short=dAdo nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
DE AltName: Full=5'-methylthioadenosine nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
DE Short=MTA nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
DE AltName: Full=S-adenosylhomocysteine nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
DE Short=AdoHcy nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
DE Short=SAH nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
DE Short=SRH nucleosidase {ECO:0000255|HAMAP-Rule:MF_01684};
GN Name=mtnN {ECO:0000255|HAMAP-Rule:MF_01684}; OrderedLocusNames=VC_2379;
OS Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=243277;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX PubMed=10952301; DOI=10.1038/35020000;
RA Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT cholerae.";
RL Nature 406:477-483(2000).
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:0000255|HAMAP-
CC 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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01684};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29860;
CC Evidence={ECO:0000255|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. {ECO:0000255|HAMAP-
CC Rule:MF_01684}.
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. MtnN
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01684}.
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DR EMBL; AE003852; AAF95522.1; -; Genomic_DNA.
DR PIR; A82084; A82084.
DR RefSeq; NP_232009.1; NC_002505.1.
DR RefSeq; WP_000689868.1; NZ_LT906614.1.
DR PDB; 3DP9; X-ray; 2.30 A; A/C=1-231.
DR PDBsum; 3DP9; -.
DR AlphaFoldDB; Q9KPI8; -.
DR SMR; Q9KPI8; -.
DR STRING; 243277.VC_2379; -.
DR ChEMBL; CHEMBL1250374; -.
DR DrugBank; DB07463; (3R,4S)-1-[(4-amino-5H-pyrrolo[3,2-d]pyrimidin-7-yl)methyl]-4-[(butylsulfanyl)methyl]pyrrolidin-3-ol.
DR DNASU; 2613048; -.
DR EnsemblBacteria; AAF95522; AAF95522; VC_2379.
DR GeneID; 57740987; -.
DR KEGG; vch:VC_2379; -.
DR PATRIC; fig|243277.26.peg.2265; -.
DR eggNOG; COG0775; Bacteria.
DR HOGENOM; CLU_031248_2_2_6; -.
DR OMA; DQFVHSK; -.
DR BioCyc; MetaCyc:MON-14562; -.
DR BioCyc; VCHO:VC2379-MON; -.
DR BRENDA; 3.2.2.9; 6626.
DR UniPathway; UPA00904; UER00871.
DR EvolutionaryTrace; Q9KPI8; -.
DR PRO; PR:Q9KPI8; -.
DR Proteomes; UP000000584; Chromosome 1.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008782; F:adenosylhomocysteine nucleosidase activity; IBA:GO_Central.
DR GO; GO:0008930; F:methylthioadenosine nucleosidase activity; IBA:GO_Central.
DR GO; GO:0019509; P:L-methionine salvage from methylthioadenosine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019284; P:L-methionine salvage from S-adenosylmethionine; IBA:GO_Central.
DR GO; GO:0009164; P:nucleoside catabolic process; IEA:InterPro.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Hydrolase; Methionine biosynthesis;
KW Reference proteome.
FT CHAIN 1..231
FT /note="5'-methylthioadenosine/S-adenosylhomocysteine
FT nucleosidase"
FT /id="PRO_0000359381"
FT ACT_SITE 12
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
FT ACT_SITE 198
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
FT BINDING 174..175
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01684"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:3DP9"
FT HELIX 10..17
FT /evidence="ECO:0007829|PDB:3DP9"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:3DP9"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:3DP9"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:3DP9"
FT HELIX 52..66
FT /evidence="ECO:0007829|PDB:3DP9"
FT STRAND 69..79
FT /evidence="ECO:0007829|PDB:3DP9"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:3DP9"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:3DP9"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:3DP9"
FT HELIX 123..133
FT /evidence="ECO:0007829|PDB:3DP9"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:3DP9"
FT HELIX 156..165
FT /evidence="ECO:0007829|PDB:3DP9"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:3DP9"
FT HELIX 176..186
FT /evidence="ECO:0007829|PDB:3DP9"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:3DP9"
FT HELIX 204..228
FT /evidence="ECO:0007829|PDB:3DP9"
SQ SEQUENCE 231 AA; 24525 MW; 5BEE5C1DA30A68C1 CRC64;
MKIGIIGAMQ QEVAILKDLI EDVQEVNQAG CTFYSGQIQG VDVVLLQSGI GKVSAALGTA
LLISQYAPDV VINTGSAGGF DASLNVGDVV ISSEVRHHDA DVTAFGYEIG QMAGQPAAFK
ADEKLMTVAE QALAQLPNTH AVRGLICTGD AFVCTAERQQ FIRQHFPSVV AVEMEASAIA
QTCHQFKVPF VVVRAISDVA DKESPLSFEE FLPLAAKSSS AMVLKMVELL K
