(data stored in SCRATCH zone)

SWISSPROT: E6V3F8_VARPE

ID   E6V3F8_VARPE            Unreviewed;       255 AA.
AC   E6V3F8;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 55.
DE   RecName: Full=5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase {ECO:0000256|SAAS:SAAS00064819};
DE            EC=3.2.2.9 {ECO:0000256|SAAS:SAAS00064821};
GN   OrderedLocusNames=Varpa_0426 {ECO:0000313|EMBL:ADU34648.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34648.1, ECO:0000313|Proteomes:UP000008917};
RN   [1] {ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P.,
RA   Han J.-I.G., Woyke T.;
RT   "Complete sequence of Variovorax paradoxus EPS.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU34648.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34648.1,
RC   ECO:0000313|Proteomes:UP000008917};
RX   PubMed=24158554;
RA   Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA   Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT   "Genome of the Root-Associated Plant Growth-Promoting Bacterium
RT   Variovorax paradoxus Strain EPS.";
RL   Genome Announc. 1:e00843-13(2013).
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}.
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DR   EMBL; CP002417; ADU34648.1; -; Genomic_DNA.
DR   RefSeq; WP_013538894.1; NC_014931.1.
DR   STRING; 595537.Varpa_0426; -.
DR   EnsemblBacteria; ADU34648; ADU34648; Varpa_0426.
DR   GeneID; 29716792; -.
DR   KEGG; vpe:Varpa_0426; -.
DR   eggNOG; ENOG4105DUF; Bacteria.
DR   eggNOG; COG0775; LUCA.
DR   HOGENOM; HOG000259346; -.
DR   KO; K01243; -.
DR   OMA; DQFVHSK; -.
DR   OrthoDB; 1860206at2; -.
DR   BioCyc; VPAR595537:G1GQO-428-MONOMER; -.
DR   UniPathway; UPA00904; UER00871.
DR   Proteomes; UP000008917; 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   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; E6V3F8.
DR   SWISS-2DPAGE; E6V3F8.
KW   Amino-acid biosynthesis {ECO:0000256|SAAS:SAAS00448580};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008917};
KW   Glycosidase {ECO:0000313|EMBL:ADU34648.1};
KW   Hydrolase {ECO:0000256|SAAS:SAAS00064825,
KW   ECO:0000313|EMBL:ADU34648.1};
KW   Methionine biosynthesis {ECO:0000256|SAAS:SAAS00448567};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008917}.
FT   DOMAIN        4    244       PNP_UDP_1. {ECO:0000259|Pfam:PF01048}.
SQ   SEQUENCE   255 AA;  26874 MW;  ED690B1AA732CFD2 CRC64;
     MAAPIAIVAA MHEELKALLA QMPDEQRVRV AGRDFWVGHL QGQPVVAVLS RIGKVAAAIT
     ATVLLERFGV RAIVFSGVAG GLAPGVNVGD VVVATELLQH DMDASPLFPK YEVPLMGLSH
     FATDAAISEA LAAVAEETLR DPVALVGQGA VDEFGLHSPK VHRGLLISGD RFVSTAAESE
     TLRRHLPKAL AVEMEGAAVA QVCHDYGVPF AAMRTISDRA DDEAHGDFAR FVAEVASRYS
     LALVGAWLAT LPAVD
//

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