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Database: UniProt
Entry: A0A1M3EHE8_9CELL
LinkDB: A0A1M3EHE8_9CELL
Original site: A0A1M3EHE8_9CELL 
ID   A0A1M3EHE8_9CELL        Unreviewed;       233 AA.
AC   A0A1M3EHE8;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=adenosylhomocysteine nucleosidase {ECO:0000256|ARBA:ARBA00011974};
DE            EC=3.2.2.9 {ECO:0000256|ARBA:ARBA00011974};
GN   ORFNames=BGO38_06705 {ECO:0000313|EMBL:OJV57915.1};
OS   Cellulomonas sp. 73-145.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC   Cellulomonas.
OX   NCBI_TaxID=1895739 {ECO:0000313|EMBL:OJV57915.1, ECO:0000313|Proteomes:UP000184491};
RN   [1] {ECO:0000313|EMBL:OJV57915.1, ECO:0000313|Proteomes:UP000184491}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=73-145 {ECO:0000313|EMBL:OJV57915.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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:OJV57915.1}.
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DR   EMBL; MKTI01000009; OJV57915.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3EHE8; -.
DR   STRING; 1895739.BGO38_06705; -.
DR   UniPathway; UPA00904; UER00871.
DR   Proteomes; UP000184491; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        47..67
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          6..226
FT                   /note="Nucleoside phosphorylase"
FT                   /evidence="ECO:0000259|Pfam:PF01048"
SQ   SEQUENCE   233 AA;  23758 MW;  07375EC0F0A931FA CRC64;
     MIAVDAVVVT AMAEEAEPFL ARADFVGAPT QVGRAVHRVV TLGGHGVLLV VCGIGLVNAA
     AAAAVAVTST APRTLISAGS AGGLGAEVRV RDVVVGTSYV YSGADARAFG YELGQVPGMP
     AVFDADPQLV EAMLAVRPES QRVLAGTMLS GDAFIDPSGV DRVRTAFPHA LSTDMESAAL
     AHVAHLYDVP FVSVRGISDL CGPADEFNQH VDDAADRSAA VVVGALQRIA ALV
//
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