PUNA_CELSP
ID PUNA_CELSP Reviewed; 282 AA.
AC P81989;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2000, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Purine nucleoside phosphorylase;
DE Short=PNP;
DE Short=Pu-NPase;
DE EC=2.4.2.1;
DE AltName: Full=Inosine phosphorylase;
DE AltName: Full=Inosine-guanosine phosphorylase;
GN Name=punA;
OS Cellulomonas sp.
OC Bacteria; Actinobacteria; Micrococcales; Cellulomonadaceae; Cellulomonas;
OC unclassified Cellulomonas.
OX NCBI_TaxID=40001;
RN [1]
RP PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION,
RP CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=10600382; DOI=10.1006/jmbi.1999.3327;
RA Tebbe J., Bzowska A., Wielgus-Kutrowska B., Schroeder W., Kazimierczuk Z.,
RA Shugar D., Saenger W., Koellner G.;
RT "Crystal structure of the purine nucleoside phosphorylase (PNP) from
RT Cellulomonas sp. and its implication for the mechanism of trimeric PNPs.";
RL J. Mol. Biol. 294:1239-1255(1999).
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:10600382}.
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:10600382};
CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:10600382}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family.
CC {ECO:0000305}.
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DR PDB; 1C3X; X-ray; 2.40 A; A/B/C=9-282.
DR PDB; 1QE5; X-ray; 2.20 A; A/B/C=9-282.
DR PDBsum; 1C3X; -.
DR PDBsum; 1QE5; -.
DR AlphaFoldDB; P81989; -.
DR SMR; P81989; -.
DR DrugBank; DB02985; 8-iodo-guanine.
DR BRENDA; 2.4.2.1; 1235.
DR UniPathway; UPA00606; -.
DR EvolutionaryTrace; P81989; -.
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; IPR011269; PUNP.
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; TIGR01697; PNPH-PUNA-XAPA; 1.
DR TIGRFAMs; TIGR01698; PUNP; 1.
DR PROSITE; PS01240; PNP_MTAP_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Glycosyltransferase; Transferase.
FT CHAIN 1..282
FT /note="Purine nucleoside phosphorylase"
FT /id="PRO_0000184541"
FT ACT_SITE 204
FT /evidence="ECO:0000255"
FT BINDING 46
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P9WP01"
FT BINDING 78
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P45563"
FT BINDING 103..105
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P45563"
FT BINDING 204
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000250|UniProtKB:P45563"
FT BINDING 223
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000250|UniProtKB:P45563"
FT BINDING 246
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000250|UniProtKB:P45563"
FT HELIX 18..33
FT /evidence="ECO:0007829|PDB:1QE5"
FT STRAND 39..43
FT /evidence="ECO:0007829|PDB:1QE5"
FT TURN 49..54
FT /evidence="ECO:0007829|PDB:1QE5"
FT STRAND 57..63
FT /evidence="ECO:0007829|PDB:1QE5"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1QE5"
FT STRAND 81..88
FT /evidence="ECO:0007829|PDB:1QE5"
FT STRAND 94..99
FT /evidence="ECO:0007829|PDB:1QE5"
FT HELIX 106..108
FT /evidence="ECO:0007829|PDB:1QE5"
FT HELIX 112..115
FT /evidence="ECO:0007829|PDB:1QE5"
FT HELIX 117..124
FT /evidence="ECO:0007829|PDB:1QE5"
FT STRAND 129..138
FT /evidence="ECO:0007829|PDB:1QE5"
FT STRAND 148..156
FT /evidence="ECO:0007829|PDB:1QE5"
FT HELIX 177..186
FT /evidence="ECO:0007829|PDB:1QE5"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:1QE5"
FT HELIX 206..215
FT /evidence="ECO:0007829|PDB:1QE5"
FT STRAND 218..224
FT /evidence="ECO:0007829|PDB:1QE5"
FT HELIX 225..233
FT /evidence="ECO:0007829|PDB:1QE5"
FT STRAND 237..247
FT /evidence="ECO:0007829|PDB:1QE5"
FT TURN 249..251
FT /evidence="ECO:0007829|PDB:1QE5"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:1C3X"
FT HELIX 258..280
FT /evidence="ECO:0007829|PDB:1QE5"
SQ SEQUENCE 282 AA; 29021 MW; 65F468DACC43D360 CRC64;
TTTTPPSTPP LDDPATDPFL VARAAADHIA QATGVEGHDM ALVLGSGWGG AAELLGEVVA
EVPTHEIPGF SAPAVAGHLS VTRSIRVERA DGSVRHALVL GSRTHLYEGK GVRAVVHGVR
TAAATGAETL ILTNGCGGLN QEWGAGTPVL LSDHINLTAR SPLEGPTFVD LTDVYSPRLR
ELAHRVDPTL PEGVYAQFPG PHYETPAEVR MAGILGADLV GMSTTLEAIA ARHCGLEVLG
VSLVTNLAAG ISPTPLSHAE VIEAGQAAGP RISALLADIA KR
