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Database: UniProt
Entry: A0A0N9NF42_9ACTN
LinkDB: A0A0N9NF42_9ACTN
Original site: A0A0N9NF42_9ACTN 
ID   A0A0N9NF42_9ACTN        Unreviewed;       270 AA.
AC   A0A0N9NF42;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
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=ACH46_06570 {ECO:0000313|EMBL:ALG84233.1};
OS   Gordonia phthalatica.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1136941 {ECO:0000313|EMBL:ALG84233.1, ECO:0000313|Proteomes:UP000063789};
RN   [1] {ECO:0000313|Proteomes:UP000063789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QH-11 {ECO:0000313|Proteomes:UP000063789};
RA   Jin D., Kong X., Bai Z.;
RT   "Complete genome sequence and metabolic analysis of phthalate degradation
RT   pathway in Gordonia sp. QH-11.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALG84233.1, ECO:0000313|Proteomes:UP000063789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QH-11 {ECO:0000313|EMBL:ALG84233.1,
RC   ECO:0000313|Proteomes:UP000063789};
RX   PubMed=29068282; DOI=10.1099/ijsem.0.002430;
RA   Jin D., Kong X., Jia M., Yu X., Wang X., Zhuang X., Deng Y., Bai Z.;
RT   "Gordonia phthalatica sp. nov., a di-n-butyl phthalate-degrading bacterium
RT   isolated from activated sludge.";
RL   Int. J. Syst. Evol. Microbiol. 67:5128-5133(2017).
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}.
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DR   EMBL; CP011853; ALG84233.1; -; Genomic_DNA.
DR   RefSeq; WP_062392211.1; NZ_CP011853.1.
DR   AlphaFoldDB; A0A0N9NF42; -.
DR   STRING; 1136941.ACH46_06570; -.
DR   KEGG; goq:ACH46_06570; -.
DR   PATRIC; fig|1136941.3.peg.1345; -.
DR   OrthoDB; 1523230at2; -.
DR   UniPathway; UPA00606; -.
DR   Proteomes; UP000063789; 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; 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:SF9; INOSINE PHOSPHORYLASE-RELATED; 1.
DR   PANTHER; PTHR11904; METHYLTHIOADENOSINE/PURINE NUCLEOSIDE PHOSPHORYLASE; 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          29..264
FT                   /note="Nucleoside phosphorylase"
FT                   /evidence="ECO:0000259|Pfam:PF01048"
FT   BINDING         35
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         67
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         87..89
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         119
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         188
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         207
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         230
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
SQ   SEQUENCE   270 AA;  27201 MW;  20935908FA6067C8 CRC64;
     MDPTADHAAA AAAAASVIAA QTDCDRHDVA VVLGSGWAPA AGAIGEPTAQ LPMAEIPGFG
     TPSAQGHAGT VQSILVGDTR ILVLLGRIHA YEGHPLARVV HPVRTAAAAG VGTVVLTNAA
     GGIRPGLQVG QPVLISDQIN LTGRSPLDGA HFVNMVDAYS PTLRDAARSV DPDLAEGVYA
     GLPGPQYETP AEIRMLGVLG ADLVGMSTVH ETIAARAAGL DVLGLSLVTN LAAGITGEPL
     DHAEVLAVGR DSAERMGALL RSVVTALAAR
//
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