ID F7YYG1_9THEM Unreviewed; 280 AA.
AC F7YYG1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
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=Theth_0901 {ECO:0000313|EMBL:AEH50985.1};
OS Pseudothermotoga thermarum DSM 5069.
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Pseudothermotoga.
OX NCBI_TaxID=688269 {ECO:0000313|EMBL:AEH50985.1, ECO:0000313|Proteomes:UP000006804};
RN [1] {ECO:0000313|EMBL:AEH50985.1, ECO:0000313|Proteomes:UP000006804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5069 {ECO:0000313|EMBL:AEH50985.1,
RC ECO:0000313|Proteomes:UP000006804};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Ivanova N., Zeytun A., Brettin T., Detter J.C.,
RA Tapia R., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M., Brambilla E.,
RA Klenk H.-P., Eisen J.A.;
RT "The complete genome of Thermotoga thermarum DSM 5069.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP002351; AEH50985.1; -; Genomic_DNA.
DR RefSeq; WP_013932205.1; NC_015707.1.
DR AlphaFoldDB; F7YYG1; -.
DR STRING; 688269.Theth_0901; -.
DR KEGG; tta:Theth_0901; -.
DR PATRIC; fig|688269.3.peg.923; -.
DR eggNOG; COG0005; Bacteria.
DR HOGENOM; CLU_054456_1_0_0; -.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000006804; Chromosome.
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 ECO:0000313|EMBL:AEH50985.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006804};
KW Transferase {ECO:0000256|PIRNR:PIRNR000477, ECO:0000313|EMBL:AEH50985.1}.
FT DOMAIN 30..276
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
SQ SEQUENCE 280 AA; 30626 MW; 755F6D7AEF93A6F6 CRC64;
MLPLGDIQEY VDRVKKAVEY LKEKINVQPK IAIILGSGLG GIAKALENPV VIKYSEIPGF
PVSTAPGHKG ELLFGKLSGK DVMLMNGRFH YYEGYSMRDV TFPIRVMQLL GVKYLFITNA
AGGLNPTFDV GKPMIIVDHI NFMGDNPLIG PNVDEWGPRF PDMSEPYNKE LIKLAEKVAQ
EEGIEVYKGV YVAVAGPNFE TRAELKMLRN FGADAVGMST VPEVIVACHA GIKVLGISAI
TDRAVPEDLK PLTAEEVLKI AEKTGEKIAR IIMGVVKLLD
//
