ID A0A1E3S1C8_9MYCO Unreviewed; 264 AA.
AC A0A1E3S1C8;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=BHQ17_03280 {ECO:0000313|EMBL:ODQ95929.1};
OS Mycolicibacterium holsaticum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=152142 {ECO:0000313|EMBL:ODQ95929.1, ECO:0000313|Proteomes:UP000094243};
RN [1] {ECO:0000313|Proteomes:UP000094243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M7 {ECO:0000313|Proteomes:UP000094243};
RA Greninger A.L., Jerome K.R., Mcnair B., Wallis C., Fang F.;
RL Submitted (SEP-2016) 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:ODQ95929.1}.
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DR EMBL; MIGZ01000010; ODQ95929.1; -; Genomic_DNA.
DR RefSeq; WP_069403796.1; NZ_MIGZ01000010.1.
DR AlphaFoldDB; A0A1E3S1C8; -.
DR OrthoDB; 1523230at2; -.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000094243; 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 Reference proteome {ECO:0000313|Proteomes:UP000094243};
KW Transferase {ECO:0000256|PIRNR:PIRNR000477}.
FT DOMAIN 26..261
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT BINDING 32
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 185
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT BINDING 204
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT BINDING 227
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
SQ SEQUENCE 264 AA; 27202 MW; B8BF97CA2952F7BC CRC64;
MTTPDAVARE AAAAISDRTG VARHDVAVVL GSGWAPAAEQ FGDPVAAVPV AELPGFTPPT
AQGHGGQVLS TRVGGRRVLV FVGRIHAYEG HELRHVVHPV RAACAGGVRT VVLTNAAGGL
RDDLAVGQPV LISDHLNLTG RSPLVGAQFV DLVGAYSPRL RAVARDIDPT LAEGVYAGLV
GPHYETPAEI RMLRTLGADL VGMSTVHETI AARAAGAEVL AVSLVTNLAA GMTGQPLNHE
EVLATGRRSA TRMGDLLAGV ITQI
//
