ID A0A0L8LK58_9ACTN Unreviewed; 273 AA.
AC A0A0L8LK58;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Purine nucleoside phosphorylase {ECO:0000256|ARBA:ARBA00013834, ECO:0000256|PIRNR:PIRNR000477};
DE EC=2.4.2.1 {ECO:0000256|ARBA:ARBA00011886, ECO:0000256|PIRNR:PIRNR000477};
DE AltName: Full=Inosine-guanosine phosphorylase {ECO:0000256|PIRNR:PIRNR000477};
GN ORFNames=ADK74_32580 {ECO:0000313|EMBL:KOG38490.1};
OS Streptomyces decoyicus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=249567 {ECO:0000313|EMBL:KOG38490.1, ECO:0000313|Proteomes:UP000037606};
RN [1] {ECO:0000313|Proteomes:UP000037606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 2666 {ECO:0000313|Proteomes:UP000037606};
RG Consortium for Microbial Forensics and Genomics (microFORGE);
RA Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U.,
RA Blagden T., Winegar R.A.;
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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. Cleaves
CC guanosine, inosine, 2'-deoxyguanosine and 2'-deoxyinosine.
CC {ECO:0000256|ARBA:ARBA00002678}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a purine 2'-deoxy-D-ribonucleoside + phosphate = 2-deoxy-
CC alpha-D-ribose 1-phosphate + a purine nucleobase;
CC Xref=Rhea:RHEA:36431, ChEBI:CHEBI:26386, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57259, ChEBI:CHEBI:142361; EC=2.4.2.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001173};
CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC {ECO:0000256|ARBA:ARBA00005058, ECO:0000256|PIRNR:PIRNR000477}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|ARBA:ARBA00011233}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006751, ECO:0000256|PIRNR:PIRNR000477}.
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:KOG38490.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LGUU01000275; KOG38490.1; -; Genomic_DNA.
DR RefSeq; WP_053210301.1; NZ_LGUU01000275.1.
DR AlphaFoldDB; A0A0L8LK58; -.
DR SMR; A0A0L8LK58; -.
DR PATRIC; fig|249567.6.peg.7170; -.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000037606; Unassembled WGS sequence.
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; IPR011269; PUNP.
DR InterPro; IPR011268; Purine_phosphorylase.
DR InterPro; IPR018099; Purine_phosphorylase-2_CS.
DR NCBIfam; TIGR01697; PNPH-PUNA-XAPA; 1.
DR NCBIfam; TIGR01698; PUNP; 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.
DR PROSITE; PS01240; PNP_MTAP_2; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|PIRNR:PIRNR000477};
KW Transferase {ECO:0000256|PIRNR:PIRNR000477}.
FT DOMAIN 35..270
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT BINDING 41
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT BINDING 73
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT BINDING 93..95
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT BINDING 125
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT BINDING 194
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT BINDING 213
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT BINDING 236
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
SQ SEQUENCE 273 AA; 28345 MW; 4AA36C3918E002CF CRC64;
MNASVTPDIA RDPQGAAADA AARLRELTGA ETHDVALVMG SGWAPAAEAL GAPEHEFPVT
ELPGFPPPAV AGHGGTIRSY RVGEKRALVF LGRTHYYEGR GVAAVAHGVR TAVAAGCKTI
VLTNGCGGLR EGMRPGQPVL ISDHLNLTAT SPIAGANFVD LTDLYSPRLR ALCKEVDPSL
EEGVYAQFPG PHYETPAEIK MIRTLGADLV GMSTVLEAIA AREAGAEVLG LSLVTNLAAG
MTGEPLNHEE VLQAGRDSAT RMGSLLAQVL GKL
//
