MTNN_MYCTU
ID MTNN_MYCTU Reviewed; 255 AA.
AC P9WJM3; L0T5N1; P67656; Q10889;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 39.
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=Rv0091; ORFNames=MTCY251.10;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(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.
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 -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. MtnN
CC subfamily. {ECO:0000305}.
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DR EMBL; AL123456; CCP42816.1; -; Genomic_DNA.
DR PIR; C70750; C70750.
DR RefSeq; NP_214605.1; NC_000962.3.
DR RefSeq; WP_003400678.1; NZ_NVQJ01000005.1.
DR AlphaFoldDB; P9WJM3; -.
DR SMR; P9WJM3; -.
DR STRING; 83332.Rv0091; -.
DR PaxDb; P9WJM3; -.
DR DNASU; 886953; -.
DR GeneID; 886953; -.
DR KEGG; mtu:Rv0091; -.
DR PATRIC; fig|83332.111.peg.105; -.
DR TubercuList; Rv0091; -.
DR eggNOG; COG0775; Bacteria.
DR OMA; DQFVHSK; -.
DR PhylomeDB; P9WJM3; -.
DR BRENDA; 3.2.2.9; 3445.
DR UniPathway; UPA00904; UER00871.
DR Proteomes; UP000001584; Chromosome.
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:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR Gene3D; 3.40.50.1580; -; 1.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Hydrolase; Methionine biosynthesis;
KW Reference proteome.
FT CHAIN 1..255
FT /note="5'-methylthioadenosine/S-adenosylhomocysteine
FT nucleosidase"
FT /id="PRO_0000164446"
FT ACT_SITE 14
FT /note="Proton acceptor"
FT /evidence="ECO:0000250|UniProtKB:P0AF12"
FT ACT_SITE 220
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P0AF12"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF12"
FT BINDING 176
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF12"
FT BINDING 196..197
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0AF12"
SQ SEQUENCE 255 AA; 27340 MW; EA80AA80B2BFEE79 CRC64;
MAVTVGVICA IPQELAYLRG VLVDAKRQQV AQILFDSGQL DAHRVVLAAA GMGKVNTGLT
ATLLADRFGC RTIVFTGVAG GLDPELCIGD IVIADRVVQH DFGLLTDERL RPYQPGHIPF
IEPTERLGYP VDPAVIDRVK HRLDGFTLAP LSTAAGGGGR QPRIYYGTIL TGDQYLHCER
TRNRLHHELG GMAVEMEGGA VAQICASFDI PWLVIRALSD LAGADSGVDF NRFVGEVAAS
SARVLLRLLP VLTAC
