ID F8A103_CELGA Unreviewed; 255 AA.
AC F8A103;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=adenosylhomocysteine nucleosidase {ECO:0000256|ARBA:ARBA00011974};
DE EC=3.2.2.9 {ECO:0000256|ARBA:ARBA00011974};
GN OrderedLocusNames=Celgi_2261 {ECO:0000313|EMBL:AEI12761.1};
OS Cellulomonas gilvus (strain ATCC 13127 / NRRL B-14078) (Cellvibrio gilvus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Cellulomonas.
OX NCBI_TaxID=593907 {ECO:0000313|EMBL:AEI12761.1, ECO:0000313|Proteomes:UP000000485};
RN [1] {ECO:0000313|Proteomes:UP000000485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13127 / NRRL B-14078 {ECO:0000313|Proteomes:UP000000485};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Munk A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Mead D., Brumm P.,
RA Woyke T.;
RT "Complete sequence of Cellvibrio gilvus ATCC 13127.";
RL Submitted (APR-2011) 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}.
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DR EMBL; CP002665; AEI12761.1; -; Genomic_DNA.
DR RefSeq; WP_013884279.1; NC_015671.1.
DR AlphaFoldDB; F8A103; -.
DR STRING; 593907.Celgi_2261; -.
DR KEGG; cga:Celgi_2261; -.
DR eggNOG; COG0775; Bacteria.
DR HOGENOM; CLU_031248_2_2_11; -.
DR UniPathway; UPA00904; UER00871.
DR Proteomes; UP000000485; 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 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 Glycosidase {ECO:0000313|EMBL:AEI12761.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AEI12761.1};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Reference proteome {ECO:0000313|Proteomes:UP000000485}.
FT DOMAIN 17..248
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
SQ SEQUENCE 255 AA; 25301 MW; 986BB6B7528EC831 CRC64;
MTDASTTAAD GSGRVDAVVV VAMDVEAEPF VALAESAGAA RDVAGATWRR LRLAGRDVLL
VRSGVGLVNA ASSAALALAV HPPTVLVSAG SAGGLGVGVR VGDVVVGTEH VYTGADARAF
GYALGQVPGM PATYAGDPTL HADALAAAAA LGPWAGAPHD VRVLPGAIVA GDVFVDAERV
GPVREAFPAA LATDMETTAL AQTAFRAGVP FLSVRGISDL CSPMEAGEFA THVDDAADRS
AAVVAALLAS ARLLA
//
