PNPH_MOOTA
ID PNPH_MOOTA Reviewed; 260 AA.
AC Q2RKL6;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Probable 6-oxopurine nucleoside phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963};
DE EC=2.4.2.1 {ECO:0000255|HAMAP-Rule:MF_01963};
DE AltName: Full=Purine nucleoside phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963};
DE Short=PNP {ECO:0000255|HAMAP-Rule:MF_01963};
GN OrderedLocusNames=Moth_0705;
OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Moorella group; Moorella.
OX NCBI_TaxID=264732;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 39073 / JCM 9320;
RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT thermoaceticum).";
RL Environ. Microbiol. 10:2550-2573(2008).
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:0000255|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:0000255|HAMAP-Rule:MF_01963};
CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC {ECO:0000255|HAMAP-Rule:MF_01963}.
CC -!- SUBUNIT: Homohexamer. Dimer of a homotrimer. {ECO:0000255|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:0000255|HAMAP-Rule:MF_01963}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01963}.
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DR EMBL; CP000232; ABC19023.1; -; Genomic_DNA.
DR RefSeq; WP_011392226.1; NC_007644.1.
DR RefSeq; YP_429566.1; NC_007644.1.
DR AlphaFoldDB; Q2RKL6; -.
DR SMR; Q2RKL6; -.
DR STRING; 264732.Moth_0705; -.
DR EnsemblBacteria; ABC19023; ABC19023; Moth_0705.
DR KEGG; mta:Moth_0705; -.
DR PATRIC; fig|264732.11.peg.754; -.
DR eggNOG; COG0005; Bacteria.
DR HOGENOM; CLU_054456_0_2_9; -.
DR OMA; ADPFCPE; -.
DR UniPathway; UPA00606; -.
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; -; 1.
DR HAMAP; MF_01963; MTAP; 1.
DR InterPro; IPR010044; MTAP.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR PANTHER; PTHR42679; PTHR42679; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
DR TIGRFAMs; TIGR01694; MTAP; 1.
PE 3: Inferred from homology;
KW Glycosyltransferase; Purine salvage; Transferase.
FT CHAIN 1..260
FT /note="Probable 6-oxopurine nucleoside phosphorylase"
FT /id="PRO_0000415082"
FT BINDING 9
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 49..50
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 182
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 183
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT BINDING 206..208
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT SITE 164
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
FT SITE 218
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01963"
SQ SEQUENCE 260 AA; 28319 MW; 336D6524DA87688F CRC64;
MRIAIIGGSG VYDPGILTNI HEERVETPYG AAVLKVGTYH GEEIGFMPRH GDKHTVPPHK
VNYRANIWAL KMLKVERVLA TAAVGSTNPE FRPGDFVIVN DFLDFTKTRT YTFFEGGETG
VVHTDFTTPY CPELGQVLVE TAARLGIKAH AGGVYACTEG PRFETPAEIR MIRQLGGDLV
GMTNVPEVVL AHEVGLCYGL IAMVTNMAAG ISSTPLSHEE VLEIMDQNGK NLRDLIMQAI
PGIPRQRNCR CSLAAGKIEV