PUNA_GEOSE
ID PUNA_GEOSE Reviewed; 274 AA.
AC P77834;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Purine nucleoside phosphorylase 1 {ECO:0000303|PubMed:8782414};
DE Short=PNP 1;
DE EC=2.4.2.1 {ECO:0000269|PubMed:8782414};
DE AltName: Full=Inosine phosphorylase;
DE AltName: Full=Inosine-guanosine phosphorylase;
DE AltName: Full=Purine nucleoside phosphorylase I;
DE Short=PNP I;
DE Short=Pu-NPase I {ECO:0000303|PubMed:8782414};
GN Name=punA; Synonyms=deoD;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=TH 6-2;
RX PubMed=9058965; DOI=10.1271/bbb.61.272;
RA Hamamoto T., Okuyama K., Noguchi T., Midorikawa Y.;
RT "Cloning and expression of purine nucleoside phosphorylase I gene from
RT Bacillus stearothermophilus TH 6-2.";
RL Biosci. Biotechnol. Biochem. 61:272-275(1997).
RN [2]
RP PROTEIN SEQUENCE OF 1-31, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, AND SUBUNIT.
RC STRAIN=TH 6-2;
RX PubMed=8782414; DOI=10.1271/bbb.60.1179;
RA Hamamoto T., Noguchi T., Midorikawa Y.;
RT "Purification and characterization of purine nucleoside phosphorylase and
RT pyrimidine nucleoside phosphorylase from Bacillus stearothermophilus TH 6-
RT 2.";
RL Biosci. Biotechnol. Biochem. 60:1179-1180(1996).
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. Cleaves
CC guanosine, inosine, 2'-deoxyguanosine and 2'-deoxyinosine.
CC {ECO:0000269|PubMed:8782414, ECO:0000269|PubMed:9058965}.
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:0000269|PubMed:8782414};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a purine 2'-deoxy-D-ribonucleoside + phosphate = 2-deoxy-
CC alpha-D-ribose 1-phosphate + a purine nucleobase;
CC Xref=Rhea:RHEA:36431, ChEBI:CHEBI:26386, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57259, ChEBI:CHEBI:142361; EC=2.4.2.1;
CC Evidence={ECO:0000269|PubMed:8782414};
CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:8782414}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family.
CC {ECO:0000305}.
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DR EMBL; D87959; BAA13509.1; -; Genomic_DNA.
DR PIR; JC5466; JT0873.
DR AlphaFoldDB; P77834; -.
DR SMR; P77834; -.
DR BRENDA; 2.4.2.1; 623.
DR UniPathway; UPA00606; -.
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; -; 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 InterPro; IPR018099; Purine_phosphorylase-2_CS.
DR PANTHER; PTHR11904; PTHR11904; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR PIRSF; PIRSF000477; PurNPase; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
DR TIGRFAMs; TIGR01700; PNPH; 1.
DR TIGRFAMs; TIGR01697; PNPH-PUNA-XAPA; 1.
DR PROSITE; PS01240; PNP_MTAP_2; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycosyltransferase; Phosphoprotein;
KW Transferase.
FT CHAIN 1..274
FT /note="Purine nucleoside phosphorylase 1"
FT /id="PRO_0000184539"
FT BINDING 29
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P9WP01"
FT BINDING 60
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P45563"
FT BINDING 80..82
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P45563"
FT BINDING 112
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P45563"
FT BINDING 192
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000250|UniProtKB:P45563"
FT BINDING 211
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P45563"
FT BINDING 234
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000250|UniProtKB:P45563"
FT MOD_RES 29
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 274 AA; 29637 MW; EC02BD23DA8A51C5 CRC64;
MNRTAIEQAA QFLKEKFPTS PQIGLILGSG LGVLADEIEQ AIKIPYSDIP NFPVSTVEGH
AGQLVYGQLE GATVVVMQGR FHYYEGYSFD KVTFPVRVMK ALGVEQLIVT NAAGGVNESF
EPGDLMIISD HINNMGGNPL IGPNDSALGV RFPDMSEAYS KRLRQLAKDV ANDIGLRVRE
GVYVANTGPA YETPAEIRMI RVMGGDAVGM STVPEVIVAR HAGMEVLGIS CISNMAAGIL
DQPLTHDEVI ETTEKVKADF LRFVKAIVRN MAKN
