ID F2JRX5_CELLD Unreviewed; 244 AA.
AC F2JRX5;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=adenosylhomocysteine nucleosidase {ECO:0000256|ARBA:ARBA00011974};
DE EC=3.2.2.9 {ECO:0000256|ARBA:ARBA00011974};
GN OrderedLocusNames=Clole_1057 {ECO:0000313|EMBL:ADZ82789.1};
OS Cellulosilyticum lentocellum (strain ATCC 49066 / DSM 5427 / NCIMB 11756 /
OS RHM5) (Clostridium lentocellum).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Cellulosilyticaceae;
OC Cellulosilyticum.
OX NCBI_TaxID=642492 {ECO:0000313|EMBL:ADZ82789.1, ECO:0000313|Proteomes:UP000008467};
RN [1] {ECO:0000313|EMBL:ADZ82789.1, ECO:0000313|Proteomes:UP000008467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49066 / DSM 5427 / NCIMB 11756 / RHM5
RC {ECO:0000313|Proteomes:UP000008467};
RX PubMed=21398547; DOI=10.1128/JB.00239-11;
RG US DOE Joint Genome Institute;
RA Miller D.A., Suen G., Bruce D., Copeland A., Cheng J.F., Detter C.,
RA Goodwin L.A., Han C.S., Hauser L.J., Land M.L., Lapidus A., Lucas S.,
RA Meincke L., Pitluck S., Tapia R., Teshima H., Woyke T., Fox B.G.,
RA Angert E.R., Currie C.R.;
RT "Complete genome sequence of the cellulose-degrading bacterium
RT Cellulosilyticum lentocellum.";
RL J. Bacteriol. 193:2357-2358(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; CP002582; ADZ82789.1; -; Genomic_DNA.
DR AlphaFoldDB; F2JRX5; -.
DR STRING; 642492.Clole_1057; -.
DR KEGG; cle:Clole_1057; -.
DR eggNOG; COG0775; Bacteria.
DR HOGENOM; CLU_031248_2_0_9; -.
DR UniPathway; UPA00904; UER00871.
DR Proteomes; UP000008467; 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:ADZ82789.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ADZ82789.1};
KW Methionine biosynthesis {ECO:0000256|ARBA:ARBA00023167};
KW Reference proteome {ECO:0000313|Proteomes:UP000008467}.
FT DOMAIN 16..241
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
SQ SEQUENCE 244 AA; 26540 MW; 1D4CE6BDCD913BC4 CRC64;
MLSEKADLVE GDTRLIGIIG AMDEEIISLK RKMEVKEQKE IAGMTFYVGT VGEKEIVLVR
CGIGKVNAAV CTQVLVDIFH AEYIINTGVA GGLYPELNIG DIVISSDTVE HDMDASAVGN
PRGEIPRMKK TYFEADQKLI EVAQKAAEKL KGAGKVYVGR VASGDQFVCS MKVKEDIYST
FTAYCAEMEG AAIAHTCFLN QVPFVIIRAI SDKADQSADV NFEEFVDVAA KNASRMIEGI
LKTL
//
