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Database: UniProt
Entry: A0A0W0WV72_9GAMM
LinkDB: A0A0W0WV72_9GAMM
Original site: A0A0W0WV72_9GAMM 
ID   A0A0W0WV72_9GAMM        Unreviewed;       276 AA.
AC   A0A0W0WV72;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=xapA {ECO:0000313|EMBL:KTD36213.1};
GN   ORFNames=Lnau_1197 {ECO:0000313|EMBL:KTD36213.1};
OS   Legionella nautarum.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=45070 {ECO:0000313|EMBL:KTD36213.1, ECO:0000313|Proteomes:UP000054725};
RN   [1] {ECO:0000313|EMBL:KTD36213.1, ECO:0000313|Proteomes:UP000054725}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49506 {ECO:0000313|EMBL:KTD36213.1,
RC   ECO:0000313|Proteomes:UP000054725};
RA   Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA   Pupko T., Shuman H.A., Segal G.;
RT   "Genomic analysis of 38 Legionella species identifies large and diverse
RT   effector repertoires.";
RL   Submitted (NOV-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.
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}.
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:KTD36213.1}.
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DR   EMBL; LNYO01000013; KTD36213.1; -; Genomic_DNA.
DR   RefSeq; WP_058504229.1; NZ_LNYO01000013.1.
DR   AlphaFoldDB; A0A0W0WV72; -.
DR   STRING; 45070.Lnau_1197; -.
DR   PATRIC; fig|45070.6.peg.1262; -.
DR   OrthoDB; 1523230at2; -.
DR   UniPathway; UPA00606; -.
DR   Proteomes; UP000054725; 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; IPR011270; Pur_Nuc_Pase_Ino/Guo-sp.
DR   InterPro; IPR011268; Purine_phosphorylase.
DR   NCBIfam; TIGR01700; PNPH; 1.
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:KTD36213.1};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000477, ECO:0000313|EMBL:KTD36213.1}.
FT   DOMAIN          27..273
FT                   /note="Nucleoside phosphorylase"
FT                   /evidence="ECO:0000259|Pfam:PF01048"
FT   BINDING         33
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         64
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         84..86
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         116
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         196
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         215
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         238
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
SQ   SEQUENCE   276 AA;  29726 MW;  C9A54246AC531D95 CRC64;
     MSNITKTAAH LAAEKIKQLL PNFKPTLGIV LGSGLGSFAE QLEDSISINY DELPGFPKPT
     VLGHSGKLVL GHLYGKGVIC LQGRAHSYEG ANFETVKTYV RCLRLLGCEY FFATNASGSL
     REDVGPGELM LISDHINLQP GNPLAGPNDD EFGPRFVPLD NAYDRQIREK LLEISDKEKT
     TLHQGVYVSV LGPNFETAAE IRAFRILGAD AVGMSTVPEV LVANHCGMKV AVIAIITNYA
     TGLATTSHSH EAVLQMAASA ADKLSKIVNK FIADYI
//
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