(data stored in ACNUC7421 zone)

SWISSPROT: MTNN_PSEHT

ID   MTNN_PSEHT              Reviewed;         235 AA.
AC   Q3ILJ7;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   05-JUL-2017, entry version 81.
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'-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};
GN   OrderedLocusNames=PSHAa0547;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
CC   -!- FUNCTION: Catalyzes the irreversible cleavage of the glycosidic
CC       bond in both 5'-methylthioadenosine (MTA) and S-
CC       adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding
CC       thioribose, 5'-methylthioribose and S-ribosylhomocysteine,
CC       respectively. {ECO:0000255|HAMAP-Rule:MF_01684}.
CC   -!- CATALYTIC ACTIVITY: S-adenosyl-L-homocysteine + H(2)O = S-(5-
CC       deoxy-D-ribos-5-yl)-L-homocysteine + adenine. {ECO:0000255|HAMAP-
CC       Rule:MF_01684}.
CC   -!- CATALYTIC ACTIVITY: S-methyl-5'-thioadenosine + H(2)O = S-methyl-
CC       5-thio-D-ribose + adenine. {ECO:0000255|HAMAP-Rule:MF_01684}.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via
CC       salvage pathway; S-methyl-5-thio-alpha-D-ribose 1-phosphate from
CC       S-methyl-5'-thioadenosine (hydrolase route): step 1/2.
CC       {ECO:0000255|HAMAP-Rule:MF_01684}.
CC   -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. MtnN
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01684}.
DR   EMBL; CR954246; CAI85635.1; -; Genomic_DNA.
DR   RefSeq; WP_011327248.1; NC_007481.1.
DR   ProteinModelPortal; Q3ILJ7; -.
DR   SMR; Q3ILJ7; -.
DR   STRING; 326442.PSHAa0547; -.
DR   EnsemblBacteria; CAI85635; CAI85635; PSHAa0547.
DR   GeneID; 32566998; -.
DR   KEGG; pha:PSHAa0547; -.
DR   eggNOG; ENOG4105DUF; Bacteria.
DR   eggNOG; COG0775; LUCA.
DR   HOGENOM; HOG000259346; -.
DR   KO; K01243; -.
DR   OMA; DQFVHSK; -.
DR   OrthoDB; POG091H06D2; -.
DR   UniPathway; UPA00904; UER00871.
DR   Proteomes; UP000006843; Chromosome I.
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   HAMAP; MF_01684; Salvage_MtnN; 1.
DR   InterPro; IPR010049; MTA_SAH_Nsdase.
DR   InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   SUPFAM; SSF53167; SSF53167; 1.
DR   TIGRFAMs; TIGR01704; MTA/SAH-Nsdase; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q3ILJ7.
DR   SWISS-2DPAGE; Q3ILJ7.
KW   Amino-acid biosynthesis; Complete proteome; Hydrolase;
KW   Methionine biosynthesis; Reference proteome.
FT   CHAIN         1    235       5'-methylthioadenosine/S-
FT                                adenosylhomocysteine nucleosidase.
FT                                /FTId=PRO_0000359324.
FT   REGION      174    175       Substrate binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_01684}.
FT   ACT_SITE     12     12       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01684}.
FT   ACT_SITE    198    198       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01684}.
FT   BINDING      78     78       Substrate; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01684}.
FT   BINDING     153    153       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01684}.
SQ   SEQUENCE   235 AA;  24883 MW;  C8B49E447504C7FB CRC64;
     MNVGIIGAME PEVKILREAM QNPQTLTKAG FTFYTGELAG NTVTLVQSGI GKVASTIATT
     LLIDNFAPDC VINTGSAGGF DPSLNVGDVV ISSEVRHHDV DVTAFGYEIG QVPQMPAGFA
     AHPKLVAAAE QTIAQISDVK TLVGLICTGD IFMCDPIRIE KARSDFPTML AVEMEGASIA
     QTCHTLNTPF VVIRSMSDIA GKESPQSFEE YLETASINSS KMVVALLEKL TAVSL
//

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