ID A0A2C6MCT7_9FIRM Unreviewed; 243 AA.
AC A0A2C6MCT7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Probable 6-oxopurine nucleoside phosphorylase {ECO:0000256|HAMAP-Rule:MF_01963};
DE EC=2.4.2.1 {ECO:0000256|HAMAP-Rule:MF_01963};
DE AltName: Full=Purine nucleoside phosphorylase {ECO:0000256|HAMAP-Rule:MF_01963};
DE Short=PNP {ECO:0000256|HAMAP-Rule:MF_01963};
GN ORFNames=P378_18555 {ECO:0000313|EMBL:PHJ37056.1};
OS Desulforamulus profundi.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=1383067 {ECO:0000313|EMBL:PHJ37056.1, ECO:0000313|Proteomes:UP000222564};
RN [1] {ECO:0000313|EMBL:PHJ37056.1, ECO:0000313|Proteomes:UP000222564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bs107 {ECO:0000313|EMBL:PHJ37056.1,
RC ECO:0000313|Proteomes:UP000222564};
RA Aullo T., Berlendis S., Lascourreges J.-F., Dessort D., Saint-Laurent S.,
RA Schraauwers B., Mas J., Magot M., Ranchou-Peyruse A.;
RT "Biodegradation of hydrocarbons in the deep terrestrial subsurface :
RT characterization of a microbial consortium composed of two Desulfotomaculum
RT species originating from a deep geological formation.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Purine nucleoside phosphorylase which is highly specific for
CC 6-oxopurine nucleosides. Cleaves guanosine or inosine to respective
CC bases and sugar-1-phosphate molecules. 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 has been shown that
CC conserved amino acid substitutions in the substrate binding pocket
CC convert the substrate specificity of this enzyme from 6-aminopurines to
CC 6-oxopurines. {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}.
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:PHJ37056.1}.
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DR EMBL; AWQQ01000118; PHJ37056.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2C6MCT7; -.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000222564; 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 ECO:0000313|EMBL:PHJ37056.1};
KW Purine salvage {ECO:0000256|HAMAP-Rule:MF_01963};
KW Reference proteome {ECO:0000313|Proteomes:UP000222564};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01963, ECO:0000313|EMBL:PHJ37056.1}.
FT DOMAIN 4..238
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT BINDING 11
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 51..52
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 185
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT BINDING 208..210
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT SITE 166
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
FT SITE 220
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01963"
SQ SEQUENCE 243 AA; 26467 MW; BFC131B36B321108 CRC64;
MTVRIAIIGG TGVYDPNILT NIRDEKVNTP YGEVGLKIGD YQGKSVAFLN RHGAGHSVPP
HLVNYRANIA ALKELGVKSI FATAAVGSLN MNMAPGHFVF ADQFLDFTKV RKHTFYEGGD
QGVVHIDMTD PYCPELRQVL AGAAAELGLT YHRYGTYVTT EGPRFETPAE IKMYKLLGGD
LVGMTSVPEV VLAREKEMCY TNISMVTNYA AGISPTKLTH QEVLDVMAAN AENLRKLAMK
PSA
//
