PNPH_BOVIN
ID PNPH_BOVIN Reviewed; 289 AA.
AC P55859; Q3ZBH6; Q58DQ2;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Purine nucleoside phosphorylase;
DE Short=PNP;
DE EC=2.4.2.1 {ECO:0000250|UniProtKB:P00491};
DE AltName: Full=Inosine phosphorylase;
DE AltName: Full=Inosine-guanosine phosphorylase;
GN Name=PNP; Synonyms=NP;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP PROTEIN SEQUENCE.
RC TISSUE=Spleen;
RX PubMed=7607309; DOI=10.1016/0014-5793(95)00540-p;
RA Bzowska A., Luic M., Schroeder W., Shugar D., Saenger W., Koellner G.;
RT "Calf spleen purine nucleoside phosphorylase: purification, sequence and
RT crystal structure of its complex with an N(7)-acycloguanosine inhibitor.";
RL FEBS Lett. 367:214-218(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0007744|PDB:1VFN}
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 4-284 IN COMPLEX WITH
RP HYPOXANTHINE.
RC TISSUE=Spleen;
RX PubMed=9020983; DOI=10.1006/jmbi.1996.0730;
RA Koellner G., Luic M., Shugar D., Saenger W., Bzowska A.;
RT "Crystal structure of calf spleen purine nucleoside phosphorylase in a
RT complex with hypoxanthine at 2.15-A resolution.";
RL J. Mol. Biol. 265:202-216(1997).
RN [5] {ECO:0007744|PDB:1A9O, ECO:0007744|PDB:1A9P, ECO:0007744|PDB:1A9Q, ECO:0007744|PDB:1A9R, ECO:0007744|PDB:1A9S, ECO:0007744|PDB:1A9T, ECO:0007744|PDB:1PBN}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-282 IN COMPLEXES WITH THE
RP SUBSTRATE ANALOGS 9-DEAZAINOSINE; INOSINE; HYPOXANTHINE AND PHOSPHATE.
RC TISSUE=Spleen;
RX PubMed=9585525; DOI=10.1021/bi9723919;
RA Mao C., Cook W.J., Zhou M., Federov A.A., Almo S.C., Ealick S.E.;
RT "Calf spleen purine nucleoside phosphorylase complexed with substrates and
RT substrate analogues.";
RL Biochemistry 37:7135-7146(1998).
RN [6] {ECO:0007744|PDB:3PNP, ECO:0007744|PDB:4PNP}
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH PHOSPHATE.
RC TISSUE=Spleen;
RA Pugmire M.J., Mao C., Ealick S.E.;
RT "The high resolution crystal structure of bovine spleen purine nucleoside
RT phosphorylase in complex forms with phosphate and 9-deazainosine.";
RL Submitted (MAR-1998) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the phosphorolytic breakdown of the N-glycosidic
CC bond in the beta-(deoxy)ribonucleoside molecules, with the formation of
CC the corresponding free purine bases and pentose-1-phosphate (By
CC similarity). Preferentially acts on 6-oxopurine nucleosides including
CC inosine and guanosine (By similarity). {ECO:0000250|UniProtKB:P00491}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=inosine + phosphate = alpha-D-ribose 1-phosphate +
CC hypoxanthine; Xref=Rhea:RHEA:27646, ChEBI:CHEBI:17368,
CC ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1;
CC Evidence={ECO:0000250|UniProtKB:P00491};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine + phosphate = alpha-D-ribose 1-phosphate + guanine;
CC Xref=Rhea:RHEA:13233, ChEBI:CHEBI:16235, ChEBI:CHEBI:16750,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1;
CC Evidence={ECO:0000250|UniProtKB:P00491};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyguanosine + phosphate = 2-deoxy-alpha-D-ribose 1-
CC phosphate + guanine; Xref=Rhea:RHEA:27738, ChEBI:CHEBI:16235,
CC ChEBI:CHEBI:17172, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.1;
CC Evidence={ECO:0000250|UniProtKB:P23492};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyinosine + phosphate = 2-deoxy-alpha-D-ribose 1-
CC phosphate + hypoxanthine; Xref=Rhea:RHEA:27750, ChEBI:CHEBI:17368,
CC ChEBI:CHEBI:28997, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.1;
CC Evidence={ECO:0000250|UniProtKB:P23492};
CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC {ECO:0000250|UniProtKB:P00491}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P00491}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00491}.
CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family.
CC {ECO:0000305}.
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DR EMBL; BT021545; AAX46392.1; -; mRNA.
DR EMBL; BC103291; AAI03292.2; -; mRNA.
DR PIR; S66203; S66203.
DR PDB; 1A9O; X-ray; 2.00 A; A=1-289.
DR PDB; 1A9P; X-ray; 2.40 A; A=1-289.
DR PDB; 1A9Q; X-ray; 2.00 A; A=1-282.
DR PDB; 1A9R; X-ray; 2.00 A; A=1-282.
DR PDB; 1A9S; X-ray; 2.00 A; A=1-289.
DR PDB; 1A9T; X-ray; 2.00 A; A=1-284.
DR PDB; 1B8N; X-ray; 2.00 A; A=1-284.
DR PDB; 1B8O; X-ray; 1.50 A; A=1-284.
DR PDB; 1FXU; X-ray; 2.20 A; A=1-289.
DR PDB; 1LV8; X-ray; 2.30 A; A/B/C/D/E/F=1-289.
DR PDB; 1LVU; X-ray; 2.05 A; A/B/C/D/E/F=1-289.
DR PDB; 1PBN; X-ray; 2.00 A; A=1-289.
DR PDB; 1V48; X-ray; 2.20 A; A=1-289.
DR PDB; 1VFN; X-ray; 2.15 A; A=4-284.
DR PDB; 2AI1; X-ray; 2.00 A; A=1-289.
DR PDB; 2AI2; X-ray; 1.70 A; A=1-289.
DR PDB; 2AI3; X-ray; 1.70 A; A=1-289.
DR PDB; 2QPL; X-ray; 2.10 A; A=3-284.
DR PDB; 3FUC; X-ray; 1.45 A; A/B/C=1-284.
DR PDB; 3PNP; X-ray; 1.60 A; A=1-289.
DR PDB; 4PNP; X-ray; 1.80 A; A=1-289.
DR PDBsum; 1A9O; -.
DR PDBsum; 1A9P; -.
DR PDBsum; 1A9Q; -.
DR PDBsum; 1A9R; -.
DR PDBsum; 1A9S; -.
DR PDBsum; 1A9T; -.
DR PDBsum; 1B8N; -.
DR PDBsum; 1B8O; -.
DR PDBsum; 1FXU; -.
DR PDBsum; 1LV8; -.
DR PDBsum; 1LVU; -.
DR PDBsum; 1PBN; -.
DR PDBsum; 1V48; -.
DR PDBsum; 1VFN; -.
DR PDBsum; 2AI1; -.
DR PDBsum; 2AI2; -.
DR PDBsum; 2AI3; -.
DR PDBsum; 2QPL; -.
DR PDBsum; 3FUC; -.
DR PDBsum; 3PNP; -.
DR PDBsum; 4PNP; -.
DR AlphaFoldDB; P55859; -.
DR SMR; P55859; -.
DR STRING; 9913.ENSBTAP00000016346; -.
DR BindingDB; P55859; -.
DR ChEMBL; CHEMBL2935; -.
DR DrugCentral; P55859; -.
DR PaxDb; P55859; -.
DR PeptideAtlas; P55859; -.
DR PRIDE; P55859; -.
DR eggNOG; KOG3984; Eukaryota.
DR HOGENOM; CLU_054456_1_2_1; -.
DR InParanoid; P55859; -.
DR TreeFam; TF300049; -.
DR BRENDA; 2.4.2.1; 908.
DR SABIO-RK; P55859; -.
DR UniPathway; UPA00606; -.
DR EvolutionaryTrace; P55859; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0047975; F:guanosine phosphorylase activity; IEA:RHEA.
DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IDA:UniProtKB.
DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW.
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 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing;
KW Glycosyltransferase; Phosphoprotein; Purine salvage; Reference proteome;
KW Transferase.
FT CHAIN 1..289
FT /note="Purine nucleoside phosphorylase"
FT /id="PRO_0000184535"
FT BINDING 33
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000269|PubMed:9585525,
FT ECO:0007744|PDB:1A9O, ECO:0007744|PDB:1A9P,
FT ECO:0007744|PDB:1A9S, ECO:0007744|PDB:1A9T,
FT ECO:0007744|PDB:3PNP, ECO:0007744|PDB:4PNP"
FT BINDING 64
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000269|PubMed:9585525,
FT ECO:0007744|PDB:1A9P, ECO:0007744|PDB:1A9T,
FT ECO:0007744|PDB:3PNP, ECO:0007744|PDB:4PNP"
FT BINDING 84..86
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000269|PubMed:9585525,
FT ECO:0007744|PDB:1A9O, ECO:0007744|PDB:1A9P,
FT ECO:0007744|PDB:1A9Q, ECO:0007744|PDB:1A9R,
FT ECO:0007744|PDB:1A9S, ECO:0007744|PDB:1A9T,
FT ECO:0007744|PDB:3PNP, ECO:0007744|PDB:4PNP"
FT BINDING 88
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000269|PubMed:9585525,
FT ECO:0007744|PDB:1A9P, ECO:0007744|PDB:1A9S,
FT ECO:0007744|PDB:1A9T"
FT BINDING 116
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000269|PubMed:9585525,
FT ECO:0007744|PDB:1A9O, ECO:0007744|PDB:1A9P,
FT ECO:0007744|PDB:1A9Q, ECO:0007744|PDB:1A9R,
FT ECO:0007744|PDB:1A9S, ECO:0007744|PDB:1A9T,
FT ECO:0007744|PDB:3PNP, ECO:0007744|PDB:4PNP"
FT BINDING 201
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000269|PubMed:9585525,
FT ECO:0000305|PubMed:9020983, ECO:0007744|PDB:1A9P,
FT ECO:0007744|PDB:1A9Q, ECO:0007744|PDB:1A9R,
FT ECO:0007744|PDB:1VFN"
FT BINDING 219
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000269|PubMed:9585525,
FT ECO:0007744|PDB:1A9P, ECO:0007744|PDB:1A9S,
FT ECO:0007744|PDB:1A9T"
FT BINDING 220
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /evidence="ECO:0000269|PubMed:9585525,
FT ECO:0007744|PDB:1A9O, ECO:0007744|PDB:1A9P,
FT ECO:0007744|PDB:1A9Q, ECO:0007744|PDB:1A9R,
FT ECO:0007744|PDB:1A9S, ECO:0007744|PDB:1A9T,
FT ECO:0007744|PDB:3PNP, ECO:0007744|PDB:4PNP"
FT BINDING 243
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000269|PubMed:9585525,
FT ECO:0000305|PubMed:9020983, ECO:0007744|PDB:1A9P,
FT ECO:0007744|PDB:1A9Q, ECO:0007744|PDB:1A9R,
FT ECO:0007744|PDB:1VFN"
FT BINDING 257
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /evidence="ECO:0000269|PubMed:9585525,
FT ECO:0007744|PDB:1A9P, ECO:0007744|PDB:1A9S,
FT ECO:0007744|PDB:1A9T"
FT SITE 243
FT /note="Important for substrate specificity"
FT /evidence="ECO:0000250|UniProtKB:P00491"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:P00491"
FT MOD_RES 251
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00491"
FT CONFLICT 2
FT /note="A -> Q (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="P -> S (in Ref. 2; AAX46392)"
FT /evidence="ECO:0000305"
FT HELIX 7..20
FT /evidence="ECO:0007829|PDB:3FUC"
FT STRAND 26..31
FT /evidence="ECO:0007829|PDB:3FUC"
FT HELIX 36..41
FT /evidence="ECO:0007829|PDB:3FUC"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:3FUC"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:3FUC"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1A9O"
FT STRAND 67..73
FT /evidence="ECO:0007829|PDB:3FUC"
FT STRAND 76..83
FT /evidence="ECO:0007829|PDB:3FUC"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:3FUC"
FT HELIX 93..96
FT /evidence="ECO:0007829|PDB:3FUC"
FT HELIX 98..106
FT /evidence="ECO:0007829|PDB:3FUC"
FT STRAND 110..119
FT /evidence="ECO:0007829|PDB:3FUC"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:3FUC"
FT HELIX 138..141
FT /evidence="ECO:0007829|PDB:3FUC"
FT TURN 153..155
FT /evidence="ECO:0007829|PDB:3FUC"
FT HELIX 168..181
FT /evidence="ECO:0007829|PDB:3FUC"
FT STRAND 188..194
FT /evidence="ECO:0007829|PDB:3FUC"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:3FUC"
FT STRAND 215..221
FT /evidence="ECO:0007829|PDB:3FUC"
FT HELIX 222..230
FT /evidence="ECO:0007829|PDB:3FUC"
FT STRAND 234..244
FT /evidence="ECO:0007829|PDB:3FUC"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:1A9O"
FT HELIX 257..278
FT /evidence="ECO:0007829|PDB:3FUC"
FT HELIX 279..281
FT /evidence="ECO:0007829|PDB:3FUC"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:1A9O"
SQ SEQUENCE 289 AA; 32037 MW; 7ECF84CCA494DEED CRC64;
MANGYTYEDY QDTAKWLLSH TEQRPQVAVI CGSGLGGLVN KLTQAQTFDY SEIPNFPEST
VPGHAGRLVF GILNGRACVM MQGRFHMYEG YPFWKVTFPV RVFRLLGVET LVVTNAAGGL
NPNFEVGDIM LIRDHINLPG FSGENPLRGP NEERFGVRFP AMSDAYDRDM RQKAHSTWKQ
MGEQRELQEG TYVMLGGPNF ETVAECRLLR NLGADAVGMS TVPEVIVARH CGLRVFGFSL
ITNKVIMDYE SQGKANHEEV LEAGKQAAQK LEQFVSLLMA SIPVSGHTG
