ID Q2S0P3_SALRD Unreviewed; 262 AA.
AC Q2S0P3;
DT 24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT 24-JAN-2006, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Purine nucleoside phosphorylase {ECO:0000256|PIRNR:PIRNR000477};
DE EC=2.4.2.1 {ECO:0000256|PIRNR:PIRNR000477};
DE AltName: Full=Inosine-guanosine phosphorylase {ECO:0000256|PIRNR:PIRNR000477};
GN Name=deoD {ECO:0000313|EMBL:ABC44581.1};
GN OrderedLocusNames=SRU_2131 {ECO:0000313|EMBL:ABC44581.1};
OS Salinibacter ruber (strain DSM 13855 / M31).
OC Bacteria; Rhodothermota; Rhodothermia; Rhodothermales; Salinibacteraceae;
OC Salinibacter.
OX NCBI_TaxID=309807 {ECO:0000313|EMBL:ABC44581.1, ECO:0000313|Proteomes:UP000008674};
RN [1] {ECO:0000313|EMBL:ABC44581.1, ECO:0000313|Proteomes:UP000008674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13855 / CECT 5946 / M31
RC {ECO:0000313|Proteomes:UP000008674};
RX PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA Mongodin E.F., Nelson K.E., Daugherty S., Deboy R.T., Wister J., Khouri H.,
RA Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G., Sharma A.K.,
RA Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F., Charlebois R.L.,
RA Legault B., Rodriguez-Valera F.;
RT "The genome of Salinibacter ruber: convergence and gene exchange among
RT hyperhalophilic bacteria and archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
CC -!- FUNCTION: The purine nucleoside phosphorylases catalyze the
CC phosphorolytic breakdown of the N-glycosidic bond in the beta-
CC (deoxy)ribonucleoside molecules, with the formation of the
CC corresponding free purine bases and pentose-1-phosphate.
CC {ECO:0000256|PIRNR:PIRNR000477}.
CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC {ECO:0000256|ARBA:ARBA00005058, ECO:0000256|PIRNR:PIRNR000477}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006751, ECO:0000256|PIRNR:PIRNR000477}.
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DR EMBL; CP000159; ABC44581.1; -; Genomic_DNA.
DR RefSeq; YP_446238.1; NC_007677.1.
DR AlphaFoldDB; Q2S0P3; -.
DR STRING; 309807.SRU_2131; -.
DR EnsemblBacteria; ABC44581; ABC44581; SRU_2131.
DR KEGG; sru:SRU_2131; -.
DR PATRIC; fig|309807.25.peg.2219; -.
DR eggNOG; COG0005; Bacteria.
DR HOGENOM; CLU_054456_1_2_10; -.
DR OrthoDB; 1523230at2; -.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000008674; Chromosome.
DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR CDD; cd09009; PNP-EcPNPII_like; 1.
DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR InterPro; IPR011268; Purine_phosphorylase.
DR NCBIfam; TIGR01697; PNPH-PUNA-XAPA; 1.
DR PANTHER; PTHR11904; METHYLTHIOADENOSINE/PURINE NUCLEOSIDE PHOSPHORYLASE; 1.
DR PANTHER; PTHR11904:SF9; PURINE NUCLEOSIDE PHOSPHORYLASE-RELATED; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR PIRSF; PIRSF000477; PurNPase; 1.
DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|PIRNR:PIRNR000477,
KW ECO:0000313|EMBL:ABC44581.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008674};
KW Transferase {ECO:0000256|PIRNR:PIRNR000477, ECO:0000313|EMBL:ABC44581.1}.
FT DOMAIN 11..258
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
SQ SEQUENCE 262 AA; 27769 MW; DBFD886C5C3BE07A CRC64;
MRERVGWAPE MALILGSGLG RLAEAADETT VVPAAEIPGY PESTVEGHSG KLVFGALEDT
RVVFVQGRVH LYEGYPVQKI AMPVRLVHAL GADRMLVTNS AGGINRTFDP GTLMFITSHL
NMAFASPGVG AGAGPARQRS DEEQAPFYEP GWTSRAEQVA LDLGLDARRG TYAWTLGPSY
ETKAEVRALE QLGADAVGMS TVPEVIQAHQ LGMAVLGLST ITNPAAGLAP GGLDHDEVLE
VSERVRGDLM KLVRGIVRVA DA
//
