ID R5E8S4_9CLOT Unreviewed; 273 AA.
AC R5E8S4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=BN724_02172 {ECO:0000313|EMBL:CCX88883.1};
OS Clostridium sp. CAG:590.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262825 {ECO:0000313|EMBL:CCX88883.1, ECO:0000313|Proteomes:UP000017939};
RN [1] {ECO:0000313|EMBL:CCX88883.1, ECO:0000313|Proteomes:UP000017939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:590 {ECO:0000313|Proteomes:UP000017939};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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}.
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:CCX88883.1}.
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DR EMBL; CAXF010000180; CCX88883.1; -; Genomic_DNA.
DR AlphaFoldDB; R5E8S4; -.
DR STRING; 1262825.BN724_02172; -.
DR UniPathway; UPA00606; -.
DR Proteomes; UP000017939; 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 Reference proteome {ECO:0000313|Proteomes:UP000017939};
KW Transferase {ECO:0000256|PIRNR:PIRNR000477}.
FT DOMAIN 24..271
FT /note="Nucleoside phosphorylase"
FT /evidence="ECO:0000259|Pfam:PF01048"
FT BINDING 31
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT BINDING 62
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT BINDING 82..84
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT BINDING 114
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT BINDING 194
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT BINDING 213
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
FT BINDING 236
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000256|PIRSR:PIRSR000477-2"
SQ SEQUENCE 273 AA; 29668 MW; E53D982D1753C19E CRC64;
MGEKADRVER CLACVRKITD FQPKVALVLG SGLGDLAEQI EITATIAYSE ITDFPQSTVA
GHKGRFVFGY IGKTPLVIMQ GRVHYYEGYS MEDVVLPVRL MKEMGAEILF LTNAAGGLGD
GFSCGDLMLI TDHISCFVPN PLLGRNEDRF GVRFPDMSEI YNRSLQDCIR KSAKELNIPL
QEGVYLQLTG PSYESPAEIR MCKALGASAV GMSTAVEAIA ANHMGMQICG ISFISNLAAG
ISDKPLCHEE VKEAADQAAP MFQQLVKHVI ANL
//
