ID A0A1F8L649_9CHLR Unreviewed; 277 AA.
AC A0A1F8L649;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=Purine nucleoside phosphorylase {ECO:0000256|PIRNR:PIRNR000477};
DE EC=2.4.2.1 {ECO:0000256|PIRNR:PIRNR000477};
DE AltName: Full=Inosine-guanosine phosphorylase {ECO:0000256|PIRNR:PIRNR000477};
GN ORFNames=A2082_02555 {ECO:0000313|EMBL:OGN81922.1};
OS Chloroflexi bacterium GWC2_70_10.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797615 {ECO:0000313|EMBL:OGN81922.1, ECO:0000313|Proteomes:UP000180316};
RN [1] {ECO:0000313|EMBL:OGN81922.1, ECO:0000313|Proteomes:UP000180316}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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.
CC {ECO:0000256|PIRNR:PIRNR000477}.
CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC {ECO:0000256|ARBA:ARBA00005058, ECO:0000256|PIRNR:PIRNR000477}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family.
CC {ECO:0000256|ARBA:ARBA00006751, ECO:0000256|PIRNR:PIRNR000477}.
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:OGN81922.1}.
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DR EMBL; MGMI01000059; OGN81922.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8L649; -.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000180316; 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; IPR011270; Pur_Nuc_Pase_Ino/Guo-sp.
DR InterPro; IPR011268; Purine_phosphorylase.
DR NCBIfam; TIGR01700; PNPH; 1.
DR NCBIfam; TIGR01697; PNPH-PUNA-XAPA; 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 Transferase {ECO:0000256|PIRNR:PIRNR000477}.
FT DOMAIN 32..274
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
SQ SEQUENCE 277 AA; 29104 MW; 79A4675EBFB970EC CRC64;
MTDVAIPPTR SGAFGLAVEA IAARTKVRPI AAIILGSGLG ALADDVKEPT RIPYAEIPGW
KRSTAPGHAG ELVVGSLSGK PVAVMRGRLH YYEGYDMADV AYPVRVLAAW GIDTLIVTNA
CGGLNPAYSA GDIMVISDHI NLMAANPLRG VNDDALGPRF PDMVGVYTEE LRALAHEVDG
GLREGIYVAV AGPNFETPAE LRMLRGLGAD AVGMSTVPEI LVARHMGMRI LALSTVTDMA
TGIPGQIQHV THEEVLEVAG RTGKRLASLV KGVVARL
//
