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Database: UniProt
Entry: U2Q162_9BACL
LinkDB: U2Q162_9BACL
Original site: U2Q162_9BACL 
ID   U2Q162_9BACL            Unreviewed;       227 AA.
AC   U2Q162;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=adenosylhomocysteine nucleosidase {ECO:0000256|ARBA:ARBA00011974};
DE            EC=3.2.2.9 {ECO:0000256|ARBA:ARBA00011974};
GN   ORFNames=HMPREF1983_01338 {ECO:0000313|EMBL:ERK56465.1};
OS   Gemella bergeri ATCC 700627.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Gemellaceae; Gemella.
OX   NCBI_TaxID=1321820 {ECO:0000313|EMBL:ERK56465.1, ECO:0000313|Proteomes:UP000016637};
RN   [1] {ECO:0000313|EMBL:ERK56465.1, ECO:0000313|Proteomes:UP000016637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700627 {ECO:0000313|EMBL:ERK56465.1,
RC   ECO:0000313|Proteomes:UP000016637};
RA   Weinstock G., Sodergren E., Wylie T., Fulton L., Fulton R., Fronick C.,
RA   O'Laughlin M., Godfrey J., Miner T., Herter B., Appelbaum E., Cordes M.,
RA   Lek S., Wollam A., Pepin K.H., Palsikar V.B., Mitreva M., Wilson R.K.;
RL   Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ERK56465.1}.
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DR   EMBL; AWVP01000089; ERK56465.1; -; Genomic_DNA.
DR   RefSeq; WP_021752878.1; NZ_KI271826.1.
DR   AlphaFoldDB; U2Q162; -.
DR   PATRIC; fig|1321820.3.peg.1296; -.
DR   eggNOG; COG0775; Bacteria.
DR   HOGENOM; CLU_031248_2_2_9; -.
DR   UniPathway; UPA00904; UER00871.
DR   Proteomes; UP000016637; Unassembled WGS sequence.
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   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   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}.
FT   DOMAIN          2..225
FT                   /note="Nucleoside phosphorylase"
FT                   /evidence="ECO:0000259|Pfam:PF01048"
SQ   SEQUENCE   227 AA;  25342 MW;  D1545A64E7BA9939 CRC64;
     MIALIGAMPE EVAIIRKKIK NLKENKIAHV NFYEGQYENK DIVLMLSLPG KVNAAIATTL
     LLDNYDIDYV INIGTCGALQ GDMEIGDMIV ATEVRHFDVD ATEFGYEIGQ VPQMPAKYES
     DKYLQQLAGE IVLPNHKIHF GLVGTSDSFI SNKKIKENIL KNFPTMQVVE MEAAAIAQTC
     YQFNTKFIVC RSVSDKAEEG NRVTFDEFLK IAALNSSILT TELIKKL
//
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