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Database: UniProt
Entry: A0A212TZF6_9MICO
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ID   A0A212TZF6_9MICO        Unreviewed;       282 AA.
AC   A0A212TZF6;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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|ARBA:ARBA00031036, ECO:0000256|PIRNR:PIRNR000477};
GN   ORFNames=SAMN05445756_1460 {ECO:0000313|EMBL:SNC71385.1};
OS   Kytococcus aerolatus.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Kytococcaceae;
OC   Kytococcus.
OX   NCBI_TaxID=592308 {ECO:0000313|EMBL:SNC71385.1, ECO:0000313|Proteomes:UP000198122};
RN   [1] {ECO:0000313|EMBL:SNC71385.1, ECO:0000313|Proteomes:UP000198122}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22179 {ECO:0000313|EMBL:SNC71385.1,
RC   ECO:0000313|Proteomes:UP000198122};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) 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}.
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DR   EMBL; FYEZ01000002; SNC71385.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A212TZF6; -.
DR   OrthoDB; 1523230at2; -.
DR   UniPathway; UPA00606; -.
DR   Proteomes; UP000198122; 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   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.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|PIRNR:PIRNR000477};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198122};
KW   Transferase {ECO:0000256|PIRNR:PIRNR000477}.
FT   DOMAIN          39..279
FT                   /note="Nucleoside phosphorylase"
FT                   /evidence="ECO:0000259|Pfam:PF01048"
FT   BINDING         45
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         77
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         102..104
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         134
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         203
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         222
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT   BINDING         245
FT                   /ligand="a purine D-ribonucleoside"
FT                   /ligand_id="ChEBI:CHEBI:142355"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
SQ   SEQUENCE   282 AA;  29285 MW;  0FCA71F4D84A7216 CRC64;
     MVTPQTQTDP STDPQAPFDL ARRAAEEIAA RTGVEQHDVA LVLGSGWGGA ADLLGEPVAS
     LDQSELPGFP PAAVAGHSSV LRSFAVAGPD GATRRVLAFG SRTHYYEGHG VRPVVHAPRT
     AAAAGCRTLV LTNGCGGLRP EWAPGTPVLI SDHINLTGTS PVEGANFVDL TDLYSPRLRE
     LAREVDPGLE EGVYVQFRGP HYETPAEVRM ARTLGGDLVG MSTTLEAIAA RQAGLEVLGL
     SLVTNAAAGI SPEPLSHAEV IEAGRAASAR CGELLAGIIP RL
//
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