ID A0A1H4UBP8_9ACTN Unreviewed; 280 AA.
AC A0A1H4UBP8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Purine nucleoside phosphorylase {ECO:0000256|HAMAP-Rule:MF_01963};
DE Short=PNP {ECO:0000256|HAMAP-Rule:MF_01963};
DE EC=2.4.2.1 {ECO:0000256|HAMAP-Rule:MF_01963};
GN ORFNames=SAMN05216482_4136 {ECO:0000313|EMBL:SEC66085.1};
OS Streptomyces sp. PAN_FS17.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1855351 {ECO:0000313|EMBL:SEC66085.1, ECO:0000313|Proteomes:UP000199275};
RN [1] {ECO:0000313|Proteomes:UP000199275}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAN_FS17 {ECO:0000313|Proteomes:UP000199275};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Purine nucleoside phosphorylase involved in purine salvage.
CC {ECO:0000256|HAMAP-Rule:MF_01963}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a purine D-ribonucleoside + phosphate = a purine nucleobase +
CC alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:19805, ChEBI:CHEBI:26386,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720, ChEBI:CHEBI:142355; EC=2.4.2.1;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01963};
CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC {ECO:0000256|HAMAP-Rule:MF_01963}.
CC -!- SUBUNIT: Homohexamer. Dimer of a homotrimer. {ECO:0000256|HAMAP-
CC Rule:MF_01963}.
CC -!- MISCELLANEOUS: Although this enzyme belongs to the family of MTA
CC phosphorylases based on sequence homology, it lacks several conserved
CC amino acids in the substrate binding pocket that confer specificity
CC towards MTA. {ECO:0000256|HAMAP-Rule:MF_01963}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01963}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01963}.
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DR EMBL; FNTN01000001; SEC66085.1; -; Genomic_DNA.
DR RefSeq; WP_030958523.1; NZ_FNTN01000001.1.
DR AlphaFoldDB; A0A1H4UBP8; -.
DR STRING; 1855351.SAMN05216482_4136; -.
DR OrthoDB; 1523230at2; -.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000199275; Unassembled WGS sequence.
DR GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IEA:InterPro.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-UniRule.
DR CDD; cd09010; MTAP_SsMTAPII_like_MTIP; 1.
DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1.
DR HAMAP; MF_01963; MTAP; 1.
DR InterPro; IPR010044; MTAP.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR NCBIfam; TIGR01694; MTAP; 1.
DR PANTHER; PTHR42679; S-METHYL-5'-THIOADENOSINE PHOSPHORYLASE; 1.
DR PANTHER; PTHR42679:SF2; S-METHYL-5'-THIOADENOSINE PHOSPHORYLASE; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01963};
KW Purine salvage {ECO:0000256|HAMAP-Rule:MF_01963};
KW Reference proteome {ECO:0000313|Proteomes:UP000199275};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01963}.
FT DOMAIN 9..252
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT BINDING 15
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 55..56
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 194
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 195
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 218..220
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT SITE 176
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT SITE 231
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
SQ SEQUENCE 280 AA; 29908 MW; 53110B169B5F389B CRC64;
MANKANVELG VIGGSGFYSF LDDVTEIQVE TPYGPPSDSL FLGEIAGRRV AFLPRHGRGH
HLPPHRINYR ANLWALRSLG VRQVLGPCAV GGLRPEYGPG TLLVPDQLVD RTKSRVGTYF
DGLPLPDGTV PNVVHVSLAD PYCPTGRAAA LKAAHGRDWE PVDGGTLVVV EGPRFSTRAE
SLWHQAQGWS VVGMTGHPEA ALARELELCY TSLTLVTDLD AGAETGEGVS HDEVLRVFAA
NVDRLRGVLF DAVAGLPANE DRDCLCTKAL GGMDPGFVLP
//
