ID   Q0SMS0_BORAP            Unreviewed;       264 AA.
AC   Q0SMS0;
DT   05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2006, sequence version 1.
DT   02-SEP-2026, entry version 117.
DE   RecName: Full=adenosylhomocysteine nucleosidase {ECO:0000256|ARBA:ARBA00011974};
DE            EC=3.2.2.9 {ECO:0000256|ARBA:ARBA00011974};
GN   Name=mtnN {ECO:0000313|EMBL:AEL69808.1};
GN   OrderedLocusNames=BafPKo_0604 {ECO:0000313|EMBL:AEL69808.1};
OS   Borreliella afzelii (strain PKo) (Borrelia afzelii).
OC   Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia; Spirochaetales;
OC   Borreliaceae; Borreliella.
OX   NCBI_TaxID=390236 {ECO:0000313|EMBL:AEL69808.1, ECO:0000313|Proteomes:UP000005216};
RN   [1] {ECO:0000313|EMBL:AEL69808.1, ECO:0000313|Proteomes:UP000005216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PKo {ECO:0000313|EMBL:AEL69808.1,
RC   ECO:0000313|Proteomes:UP000005216};
RX   PubMed=22123755; DOI=10.1128/JB.05951-11;
RA   Casjens S.R., Mongodin E.F., Qiu W.-G., Dunn J.J., Luft B.J.,
RA   Fraser-Liggett C.M., Schutzer S.E.;
RT   "Whole-genome sequences of two Borrelia afzelii and two Borrelia garinii
RT   Lyme disease agent isolates.";
RL   J. Bacteriol. 193:6995-6996(2011).
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:0000256|ARBA:ARBA00004945}.
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DR   EMBL; CP002933; AEL69808.1; -; Genomic_DNA.
DR   RefSeq; WP_004789691.1; NC_008277.1.
DR   AlphaFoldDB; Q0SMS0; -.
DR   STRING; 29518.BLA32_01325; -.
DR   KEGG; baf:BAPKO_0619; -.
DR   KEGG; bafz:BafPKo_0604; -.
DR   PATRIC; fig|390236.22.peg.581; -.
DR   eggNOG; COG0775; Bacteria.
DR   HOGENOM; CLU_031248_2_2_12; -.
DR   OrthoDB; 9792278at2; -.
DR   UniPathway; UPA00904; UER00871.
DR   Proteomes; UP000005216; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0008782; F:adenosylhomocysteine nucleosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008930; F:methylthioadenosine nucleosidase activity; IEA:InterPro.
DR   GO; GO:0009164; P:nucleoside catabolic process; IEA:InterPro.
DR   CDD; cd09008; MTAN; 1.
DR   Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR   InterPro; IPR010049; MTA_SAH_Nsdase.
DR   InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR   InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR   NCBIfam; TIGR01704; MTA_SAH-Nsdase; 1.
DR   NCBIfam; NF004079; PRK05584.1; 1.
DR   PANTHER; PTHR46832; 5'-METHYLTHIOADENOSINE/S-ADENOSYLHOMOCYSTEINE NUCLEOSIDASE; 1.
DR   PANTHER; PTHR46832:SF1; 5'-METHYLTHIOADENOSINE_S-ADENOSYLHOMOCYSTEINE NUCLEOSIDASE; 1.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005216}.
FT   DOMAIN          28..262
FT                   /note="Nucleoside phosphorylase"
FT                   /evidence="ECO:0000259|Pfam:PF01048"
SQ   SEQUENCE   264 AA;  28967 MW;  93CD5DE3D599D8E8 CRC64;
     MNNFLIKLLL FLLVFSNSYV AFSKNSNVLI ITAMDSEVEQ INKLMSNKEE IVLKEYGLNK
     KILKGKLSNR NVITIVCGVG KVNAGVWTSY ILSKYNISHV INSGVAGGVV SDKYKDIKVG
     DVVVSSEVAY HDVDLTKFGH KVGQLMGLPQ KFSANKNLVD KATKAVKSKV ASSNSYSGLI
     LSGDQFIDPA YINKIIGNFK DVIAVEMEGA AVGHVSHMFN VPFIVIRSIS DIVNKEGNEL
     EYSKFLKLAA FNSAKVVQEI LRIL
//