MTNN_VIBC3
ID MTNN_VIBC3 Reviewed; 231 AA.
AC A5F5R2; C3M4A2;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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}; Synonyms=pfs;
GN OrderedLocusNames=VC0395_A1957, VC395_2494;
OS Vibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 /
OS O395).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=345073;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RA Heidelberg J.;
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39541 / Classical Ogawa 395 / O395;
RX PubMed=19115014; DOI=10.1371/journal.pone.0004053;
RA Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J.,
RA Wang W., Wang J., Qian W., Li D., Wang L.;
RT "A recalibrated molecular clock and independent origins for the cholera
RT pandemic clones.";
RL PLoS ONE 3:E4053-E4053(2008).
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; CP000627; ABQ19861.1; -; Genomic_DNA.
DR EMBL; CP001235; ACP10484.1; -; Genomic_DNA.
DR RefSeq; WP_000689868.1; NZ_JAACZH010000008.1.
DR PDB; 4WKB; X-ray; 1.37 A; A/B=1-231.
DR PDB; 4X24; X-ray; 1.50 A; A/B=1-231.
DR PDBsum; 4WKB; -.
DR PDBsum; 4X24; -.
DR AlphaFoldDB; A5F5R2; -.
DR SMR; A5F5R2; -.
DR STRING; 345073.VC395_2494; -.
DR EnsemblBacteria; ABQ19861; ABQ19861; VC0395_A1957.
DR GeneID; 57740987; -.
DR KEGG; vco:VC0395_A1957; -.
DR KEGG; vcr:VC395_2494; -.
DR PATRIC; fig|345073.21.peg.2398; -.
DR eggNOG; COG0775; Bacteria.
DR HOGENOM; CLU_031248_2_2_6; -.
DR OMA; DQFVHSK; -.
DR BRENDA; 3.2.2.16; 6626.
DR BRENDA; 3.2.2.9; 6626.
DR UniPathway; UPA00904; UER00871.
DR Proteomes; UP000000249; Chromosome 2.
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 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.
FT CHAIN 1..231
FT /note="5'-methylthioadenosine/S-adenosylhomocysteine
FT nucleosidase"
FT /id="PRO_0000359382"
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 2..9
FT /evidence="ECO:0007829|PDB:4WKB"
FT HELIX 10..19
FT /evidence="ECO:0007829|PDB:4WKB"
FT STRAND 21..28
FT /evidence="ECO:0007829|PDB:4WKB"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:4WKB"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:4WKB"
FT HELIX 52..66
FT /evidence="ECO:0007829|PDB:4WKB"
FT STRAND 69..79
FT /evidence="ECO:0007829|PDB:4WKB"
FT STRAND 89..97
FT /evidence="ECO:0007829|PDB:4WKB"
FT HELIX 103..105
FT /evidence="ECO:0007829|PDB:4WKB"
FT STRAND 117..120
FT /evidence="ECO:0007829|PDB:4X24"
FT HELIX 123..134
FT /evidence="ECO:0007829|PDB:4WKB"
FT STRAND 141..148
FT /evidence="ECO:0007829|PDB:4WKB"
FT HELIX 156..165
FT /evidence="ECO:0007829|PDB:4WKB"
FT STRAND 169..175
FT /evidence="ECO:0007829|PDB:4WKB"
FT HELIX 176..186
FT /evidence="ECO:0007829|PDB:4WKB"
FT STRAND 190..198
FT /evidence="ECO:0007829|PDB:4WKB"
FT HELIX 204..231
FT /evidence="ECO:0007829|PDB:4WKB"
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
