ID A0A1H0F452_9ACTN Unreviewed; 283 AA.
AC A0A1H0F452;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
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=SAMN05216259_106144 {ECO:0000313|EMBL:SDN89361.1};
OS Actinacidiphila guanduensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=310781 {ECO:0000313|EMBL:SDN89361.1, ECO:0000313|Proteomes:UP000199341};
RN [1] {ECO:0000313|EMBL:SDN89361.1, ECO:0000313|Proteomes:UP000199341}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.2022 {ECO:0000313|EMBL:SDN89361.1,
RC ECO:0000313|Proteomes:UP000199341};
RA de Groot N.N.;
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; FNIE01000006; SDN89361.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0F452; -.
DR STRING; 310781.SAMN05216259_106144; -.
DR OrthoDB; 1523230at2; -.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000199341; 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:UP000199341};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01963}.
FT DOMAIN 11..255
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT BINDING 18
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 58..59
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 197
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 198
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 221..223
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT SITE 179
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT SITE 234
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
SQ SEQUENCE 283 AA; 30003 MW; B76286C3D13129F8 CRC64;
MANSSGEVQA EIGVIGGSGF YSFLDDVMEV TVDTPYGAPS DSLFLGEVAG RRVAFLPRHG
RKHHLPPHRI NYRANLWALA SLGARQILGP CAVGGLQTRY GPGTLLVPDQ LVDRTKSRAQ
TYFDGEPRLD GSVPNVVHVT FADPYCPVGR RVAVDTARAG GWDAVDGGTL VVVEGPRFST
RAESLWHAAQ GWSVVGMTGH PEAVLARELG LCYTSLTLVT DLDAGADTGE GVSHEEVLEV
FAANVGRMRN VLFDVVGALP ANSDRTCLCV SPLGGQEPGI DLP
//
