(data stored in SCRATCH zone)

SWISSPROT: B2UHE9_RALPJ

ID   B2UHE9_RALPJ            Unreviewed;       279 AA.
AC   B2UHE9;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 76.
DE   RecName: Full=5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase {ECO:0000256|SAAS:SAAS00064819};
DE            EC=3.2.2.9 {ECO:0000256|SAAS:SAAS00064821};
GN   OrderedLocusNames=Rpic_3891 {ECO:0000313|EMBL:ACD29000.1};
OS   Ralstonia pickettii (strain 12J).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=402626 {ECO:0000313|EMBL:ACD29000.1, ECO:0000313|Proteomes:UP000002566};
RN   [1] {ECO:0000313|Proteomes:UP000002566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12J {ECO:0000313|Proteomes:UP000002566};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T.,
RA   Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT   "Complete sequence of chromosome 2 of Ralstonia pickettii 12J.";
RL   Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
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:0000256|SAAS:SAAS00064815}.
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,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16708, ChEBI:CHEBI:57856,
CC         ChEBI:CHEBI:58195; EC=3.2.2.9;
CC         Evidence={ECO:0000256|SAAS:SAAS01116305};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + S-methyl-5'-thioadenosine = adenine + S-methyl-5-
CC         thio-D-ribose; Xref=Rhea:RHEA:13617, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16708, ChEBI:CHEBI:16895, ChEBI:CHEBI:17509;
CC         EC=3.2.2.9; Evidence={ECO:0000256|SAAS:SAAS01116302};
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:0000256|SAAS:SAAS00064800}.
CC   -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. MtnN
CC       subfamily. {ECO:0000256|SAAS:SAAS00561432}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001069; ACD29000.1; -; Genomic_DNA.
DR   STRING; 402626.Rpic_3891; -.
DR   EnsemblBacteria; ACD29000; ACD29000; Rpic_3891.
DR   KEGG; rpi:Rpic_3891; -.
DR   eggNOG; ENOG4105DUF; Bacteria.
DR   eggNOG; COG0775; LUCA.
DR   HOGENOM; HOG000259346; -.
DR   KO; K01243; -.
DR   OMA; DQFVHSK; -.
DR   BioCyc; RPIC402626:GH94-3896-MONOMER; -.
DR   UniPathway; UPA00904; UER00871.
DR   Proteomes; UP000002566; Chromosome 2.
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   Gene3D; 3.40.50.1580; -; 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   3: Inferred from homology;
DR   PRODOM; B2UHE9.
DR   SWISS-2DPAGE; B2UHE9.
KW   Amino-acid biosynthesis {ECO:0000256|SAAS:SAAS00448580};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002566};
KW   Glycosidase {ECO:0000313|EMBL:ACD29000.1};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00064825,
KW   ECO:0000313|EMBL:ACD29000.1};
KW   Methionine biosynthesis {ECO:0000256|SAAS:SAAS00448567};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002566}.
FT   DOMAIN       29    271       PNP_UDP_1. {ECO:0000259|Pfam:PF01048}.
SQ   SEQUENCE   279 AA;  29045 MW;  2668D3197DCB8148 CRC64;
     MTSFDVSTLQ TGAAFCMNTP SSQPNARGPI GIVAALHEEI NELLTWLSDA QCIHIGSRDF
     WTGELDGQTV VVVLSRVGKV AAASTTAVLI TQFNVRAVVF AGVAGALAPG VAVGDVVVSE
     ELLQHDVDAS PLFPRWEIPL TGMARFPADA ALASGLLESA GAVLADPHAL LGPDVMRAFG
     IAAPQAHRGL IVSGDRFVCT SAESAVLRTA LPDALAVEME GAAVAQVCHE WGVPFAAIRT
     ISDRADDAAS VDFAQFITQV DSRYAVAILR KWLSTAAGA
//

If you have problems or comments...

PBIL Back to PBIL home page