(data stored in ACNUC7421 zone)

SWISSPROT: MTNN_ECO57

ID   MTNN_ECO57              Reviewed;         232 AA.
AC   P0AF14; P24247;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   05-JUL-2017, entry version 84.
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=Z0170, ECs0163;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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   -!- SUBUNIT: Homodimer. {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; AE005174; AAG54463.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33586.1; -; Genomic_DNA.
DR   PIR; C85500; C85500.
DR   PIR; C90649; C90649.
DR   RefSeq; NP_308190.1; NC_002695.1.
DR   RefSeq; WP_000689844.1; NZ_MWVM01000012.1.
DR   PDB; 3DF9; X-ray; 1.95 A; A/B=1-232.
DR   PDBsum; 3DF9; -.
DR   ProteinModelPortal; P0AF14; -.
DR   SMR; P0AF14; -.
DR   STRING; 155864.Z0170; -.
DR   ChEMBL; CHEMBL1250346; -.
DR   EnsemblBacteria; AAG54463; AAG54463; Z0170.
DR   EnsemblBacteria; BAB33586; BAB33586; BAB33586.
DR   GeneID; 913817; -.
DR   KEGG; ece:Z0170; -.
DR   KEGG; ecs:ECs0163; -.
DR   PATRIC; fig|386585.9.peg.263; -.
DR   eggNOG; ENOG4105DUF; Bacteria.
DR   eggNOG; COG0775; LUCA.
DR   HOGENOM; HOG000259346; -.
DR   KO; K01243; -.
DR   BRENDA; 3.2.2.16; 2026.
DR   BRENDA; 3.2.2.9; 2026.
DR   UniPathway; UPA00904; UER00871.
DR   EvolutionaryTrace; P0AF14; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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   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   1: Evidence at protein level;
DR   PRODOM; P0AF14.
DR   SWISS-2DPAGE; P0AF14.
KW   3D-structure; Amino-acid biosynthesis; Complete proteome; Hydrolase;
KW   Methionine biosynthesis.
FT   CHAIN         1    232       5'-methylthioadenosine/S-
FT                                adenosylhomocysteine nucleosidase.
FT                                /FTId=PRO_0000164440.
FT   REGION      173    174       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    197    197       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     152    152       Substrate; via amide nitrogen and
FT                                carbonyl oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01684}.
FT   STRAND        2      9       {ECO:0000244|PDB:3DF9}.
FT   HELIX        10     18       {ECO:0000244|PDB:3DF9}.
FT   STRAND       21     28       {ECO:0000244|PDB:3DF9}.
FT   STRAND       31     38       {ECO:0000244|PDB:3DF9}.
FT   STRAND       41     47       {ECO:0000244|PDB:3DF9}.
FT   HELIX        52     66       {ECO:0000244|PDB:3DF9}.
FT   STRAND       69     79       {ECO:0000244|PDB:3DF9}.
FT   STRAND       89     99       {ECO:0000244|PDB:3DF9}.
FT   HELIX       103    105       {ECO:0000244|PDB:3DF9}.
FT   STRAND      117    120       {ECO:0000244|PDB:3DF9}.
FT   HELIX       123    136       {ECO:0000244|PDB:3DF9}.
FT   STRAND      140    147       {ECO:0000244|PDB:3DF9}.
FT   HELIX       155    164       {ECO:0000244|PDB:3DF9}.
FT   STRAND      168    174       {ECO:0000244|PDB:3DF9}.
FT   HELIX       175    184       {ECO:0000244|PDB:3DF9}.
FT   STRAND      189    197       {ECO:0000244|PDB:3DF9}.
FT   HELIX       203    231       {ECO:0000244|PDB:3DF9}.
SQ   SEQUENCE   232 AA;  24354 MW;  9B1FF9BEC39D4F2C CRC64;
     MKIGIIGAME EEVTLLRDKI ENRQTISLGG CEIYTGQLNG TEVALLKSGI GKVAAALGAT
     LLLEHCKPDV IINTGSAGGL APTLKVGDIV VSDEARYHDA DVTAFGYEYG QLPGCPAGFK
     ADDKLIAAAE ACIAELNLNA VRGLIVSGDA FINGSVGLAK IRHNFPQAIA VEMEATAIAH
     VCHNFNVPFV VVRAISDVAD QQSHLSFDEF LAVAAKQSSL MVESLVQKLA HG
//

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