DEOD_ECOLI
ID DEOD_ECOLI Reviewed; 239 AA.
AC P0ABP8; P09743; Q2M5T3;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Purine nucleoside phosphorylase DeoD-type {ECO:0000255|HAMAP-Rule:MF_01627};
DE Short=PNP {ECO:0000255|HAMAP-Rule:MF_01627};
DE EC=2.4.2.1 {ECO:0000255|HAMAP-Rule:MF_01627, ECO:0000269|PubMed:11786017, ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:235429, ECO:0000269|PubMed:30337572};
GN Name=deoD {ECO:0000255|HAMAP-Rule:MF_01627}; Synonyms=pup;
GN OrderedLocusNames=b4384, JW4347;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1714590; DOI=10.1073/pnas.88.16.7185;
RA Hershfield M.S., Chaffee S., Koro-Johnson L., Mary A., Smith A.A.,
RA Short S.A.;
RT "Use of site-directed mutagenesis to enhance the epitope-shielding effect
RT of covalent modification of proteins with polyethylene glycol.";
RL Proc. Natl. Acad. Sci. U.S.A. 88:7185-7189(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 2-21.
RX PubMed=8506346; DOI=10.1073/pnas.90.11.5011;
RA Henzel W.J., Billeci T.M., Stults J.T., Wong S.C., Grimley C., Watanabe C.;
RT "Identifying proteins from two-dimensional gels by molecular mass searching
RT of peptide fragments in protein sequence databases.";
RL Proc. Natl. Acad. Sci. U.S.A. 90:5011-5015(1993).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 225-239.
RC STRAIN=K12;
RX PubMed=3299264; DOI=10.1093/nar/15.13.5125;
RA Larsen J.E.L., Albrechtsen B., Valentin-Hansen P.;
RT "Analysis of the terminator region after the deoCABD operon of Escherichia
RT coli K-12 using a new class of single copy number operon-fusion vectors.";
RL Nucleic Acids Res. 15:5125-5140(1987).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=235429; DOI=10.1111/j.1432-1033.1975.tb03925.x;
RA Jensen K.F., Nygaard P.;
RT "Purine nucleoside phosphorylase from Escherichia coli and Salmonella
RT typhimurium. Purification and some properties.";
RL Eur. J. Biochem. 51:253-265(1975).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=9351810; DOI=10.1016/s0969-2126(97)00287-6;
RA Mao C., Cook W.J., Zhou M., Koszalka G.W., Krenitsky T.A., Ealick S.E.;
RT "The crystal structure of Escherichia coli purine nucleoside phosphorylase:
RT a comparison with the human enzyme reveals a conserved topology.";
RL Structure 5:1373-1383(1997).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), AND SUBUNIT.
RX PubMed=9653038; DOI=10.1006/jmbi.1998.1799;
RA Koellner G., Luic M., Shugar D., Saenger W., Bzowska A.;
RT "Crystal structure of the ternary complex of E. coli purine nucleoside
RT phosphorylase with formycin B, a structural analogue of the substrate
RT inosine, and phosphate (sulphate) at 2.1-A resolution.";
RL J. Mol. Biol. 280:153-166(1998).
RN [11] {ECO:0007744|PDB:1K9S}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-238 IN COMPLEX WITH
RP N(7)-METHYLFORMYCIN AND PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBUNIT.
RX PubMed=11786017; DOI=10.1006/jmbi.2001.5211;
RA Koellner G., Bzowska A., Wielgus-Kutrowska B., Luic M., Steiner T.,
RA Saenger W., Stepinski J.;
RT "Open and closed conformation of the E. coli purine nucleoside
RT phosphorylase active center and implications for the catalytic mechanism.";
RL J. Mol. Biol. 315:351-371(2002).
RN [12] {ECO:0007744|PDB:3ONV, ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH, ECO:0007744|PDB:3OPV}
RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 2-238 OF WILD TYPE AND MUTANT
RP ALA-25 IN COMPLEX WITH PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF ARG-25; ASP-205
RP AND ARG-218.
RX PubMed=21672603; DOI=10.1016/j.biochi.2011.05.030;
RA Mikleusevic G., Stefanic Z., Narczyk M., Wielgus-Kutrowska B., Bzowska A.,
RA Luic M.;
RT "Validation of the catalytic mechanism of Escherichia coli purine
RT nucleoside phosphorylase by structural and kinetic studies.";
RL Biochimie 93:1610-1622(2011).
RN [13] {ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ}
RP X-RAY CRYSTALLOGRAPHY (1.77 ANGSTROMS) OF 2-238 IN COMPLEX WITH PHOSPHATE
RP AND SUBSTRATE ANALOG FORMYCIN A, FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF
RP ASP-205 AND ARG-218.
RX PubMed=30337572; DOI=10.1038/s41598-018-33723-1;
RA Stefanic Z., Narczyk M., Mikleusevic G., Kazazic S., Bzowska A., Luic M.;
RT "Crystallographic snapshots of ligand binding to hexameric purine
RT nucleoside phosphorylase and kinetic studies give insight into the
RT mechanism of catalysis.";
RL Sci. Rep. 8:15427-15427(2018).
CC -!- FUNCTION: Catalyzes the reversible phosphorolytic breakdown of the N-
CC glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the
CC formation of the corresponding free purine bases and pentose-1-
CC phosphate (PubMed:235429, PubMed:11786017, PubMed:21672603,
CC PubMed:30337572). Acts on 6-amino and 6-oxopurines including
CC deoxyinosine, deoxyguanosine, deoxyadenosine, adenosine, guanosine, and
CC inosine (PubMed:235429, PubMed:11786017, PubMed:21672603,
CC PubMed:30337572). Does not act on xanthosine (Probable). May also
CC catalyze a phosphate-dependent transfer of the pentose moiety from one
CC purine base to another (PubMed:235429). {ECO:0000269|PubMed:11786017,
CC ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:235429,
CC ECO:0000269|PubMed:30337572, ECO:0000305|PubMed:235429}.
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:0000255|HAMAP-Rule:MF_01627};
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:0000255|HAMAP-Rule:MF_01627};
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:0000269|PubMed:21672603, ECO:0000269|PubMed:235429,
CC ECO:0000305|PubMed:11786017};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:27647;
CC Evidence={ECO:0000269|PubMed:235429};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:27648;
CC Evidence={ECO:0000269|PubMed:235429};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate;
CC Xref=Rhea:RHEA:27642, ChEBI:CHEBI:16335, ChEBI:CHEBI:16708,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1;
CC Evidence={ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:235429,
CC ECO:0000269|PubMed:30337572};
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:0000269|PubMed:21672603, ECO:0000269|PubMed:235429};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2'-deoxyadenosine + phosphate = 2-deoxy-alpha-D-ribose 1-
CC phosphate + adenine; Xref=Rhea:RHEA:27742, ChEBI:CHEBI:16708,
CC ChEBI:CHEBI:17256, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.1;
CC Evidence={ECO:0000269|PubMed:235429};
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:0000269|PubMed:235429};
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:0000269|PubMed:235429};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=230 uM for phosphate (at 25 degrees Celsius and pH 7)
CC {ECO:0000269|PubMed:30337572};
CC KM=520 uM for phosphate (at 25 degrees Celsius and pH 5.3)
CC {ECO:0000269|PubMed:30337572};
CC KM=120 uM for phosphate (at pH 7.1) {ECO:0000269|PubMed:235429};
CC KM=70 uM for inosine (at pH 7.1) {ECO:0000269|PubMed:235429};
CC KM=180 uM for deoxyinosine (at pH 7.1) {ECO:0000269|PubMed:235429};
CC KM=40 uM for ribose-1-phosphate (at pH 7.1)
CC {ECO:0000269|PubMed:235429};
CC KM=100 uM for deoxyribose-1-phosphate (at pH 7.1)
CC {ECO:0000269|PubMed:235429};
CC KM=40 uM for adenine (at pH 7.1) {ECO:0000269|PubMed:235429};
CC KM=28 uM for adenosine (at 25 degrees Celsius and pH 7)
CC {ECO:0000269|PubMed:30337572};
CC Vmax=20.8 umol/min/mg enzyme toward phosphate (at 25 degrees Celsius
CC and pH 7) {ECO:0000269|PubMed:30337572};
CC Vmax=3.5 umol/min/mg enzyme toward phosphate (at 25 degrees Celsius
CC and pH 5.3) {ECO:0000269|PubMed:30337572};
CC Vmax=51.1 umol/min/mg enzyme toward adenosine (at 25 degrees Celsius
CC and pH 7) {ECO:0000269|PubMed:30337572};
CC Vmax=66 umol/min/mg enzyme toward phosphate (at pH 7.1)
CC {ECO:0000269|PubMed:235429};
CC Vmax=230 umol/min/mg enzyme toward inosine (at pH 7.1)
CC {ECO:0000269|PubMed:235429};
CC Vmax=605 umol/min/mg enzyme toward deoxyinosine (at pH 7.1)
CC {ECO:0000269|PubMed:235429};
CC Vmax=342 umol/min/mg enzyme toward ribose-1-phosphate (at pH 7.1)
CC {ECO:0000269|PubMed:235429};
CC Vmax=565 umol/min/mg enzyme toward deoxyribose-1-phosphate (at pH
CC 7.1) {ECO:0000269|PubMed:235429};
CC Vmax=583 umol/min/mg enzyme toward adenine (with ribose-1-phosphate
CC as cosubstrate and at pH 7.1) {ECO:0000269|PubMed:235429};
CC Vmax=880 umol/min/mg enzyme toward adenine (with deoxyribose-1-
CC phosphate as cosubstrate and at pH 7.1) {ECO:0000269|PubMed:235429};
CC pH dependence:
CC Optimum pH is 7.1 for deoxyinosine as substrate (PubMed:235429).
CC Optimum pH is 7.5 for inosine as substrate (PubMed:235429). Optimum
CC pH is 8.2 for hypoxanthine as substrate (PubMed:235429).
CC {ECO:0000269|PubMed:235429};
CC -!- SUBUNIT: Homohexamer; trimer of homodimers. {ECO:0000255|HAMAP-
CC Rule:MF_01627, ECO:0000269|PubMed:11786017,
CC ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:235429,
CC ECO:0000269|PubMed:30337572, ECO:0000269|PubMed:9653038}.
CC -!- INTERACTION:
CC P0ABP8; P0ABP8: deoD; NbExp=7; IntAct=EBI-907568, EBI-907568;
CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family.
CC {ECO:0000255|HAMAP-Rule:MF_01627, ECO:0000305}.
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DR EMBL; M60917; AAA24401.1; -; Genomic_DNA.
DR EMBL; U14003; AAA97280.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77337.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78373.1; -; Genomic_DNA.
DR EMBL; X05629; CAA29114.1; -; Genomic_DNA.
DR PIR; A41143; A27854.
DR RefSeq; NP_418801.1; NC_000913.3.
DR RefSeq; WP_000224877.1; NZ_STEB01000033.1.
DR PDB; 1A69; X-ray; 2.10 A; A/B/C=2-239.
DR PDB; 1ECP; X-ray; 2.00 A; A/B/C/D/E/F=2-239.
DR PDB; 1K9S; X-ray; 2.00 A; A/B/C/D/E/F=2-238.
DR PDB; 1OTX; X-ray; 2.70 A; A/B/C=2-239.
DR PDB; 1OTY; X-ray; 2.50 A; A/B/C=2-239.
DR PDB; 1OU4; X-ray; 2.50 A; A/B/C=2-239.
DR PDB; 1OUM; X-ray; 2.40 A; A/B/C=2-239.
DR PDB; 1OV6; X-ray; 2.40 A; A/B/C=2-239.
DR PDB; 1OVG; X-ray; 2.20 A; A/B/C=2-239.
DR PDB; 3ONV; X-ray; 1.89 A; A/B/C=2-238.
DR PDB; 3OOE; X-ray; 2.00 A; A/B/C/D/E/F=2-238.
DR PDB; 3OOH; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R=2-238.
DR PDB; 3OPV; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I/J/K/L=2-238.
DR PDB; 3UT6; X-ray; 1.90 A; A/B/C=2-238.
DR PDB; 4TS3; X-ray; 2.30 A; A/B/C/D/E/F=2-238.
DR PDB; 4TS9; X-ray; 1.77 A; A/B/C=2-238.
DR PDB; 4TTA; X-ray; 2.00 A; A/B/C/D/E/F=2-238.
DR PDB; 4TTI; X-ray; 1.89 A; A/B/C/D/E/F=2-238.
DR PDB; 4TTJ; X-ray; 1.87 A; A/B/D=2-238.
DR PDB; 5I3C; X-ray; 2.32 A; A/B/C=2-238.
DR PDB; 5IU6; X-ray; 2.51 A; A/B/C=2-238.
DR PDB; 6XZ2; X-ray; 1.65 A; A/B/C=2-238.
DR PDBsum; 1A69; -.
DR PDBsum; 1ECP; -.
DR PDBsum; 1K9S; -.
DR PDBsum; 1OTX; -.
DR PDBsum; 1OTY; -.
DR PDBsum; 1OU4; -.
DR PDBsum; 1OUM; -.
DR PDBsum; 1OV6; -.
DR PDBsum; 1OVG; -.
DR PDBsum; 3ONV; -.
DR PDBsum; 3OOE; -.
DR PDBsum; 3OOH; -.
DR PDBsum; 3OPV; -.
DR PDBsum; 3UT6; -.
DR PDBsum; 4TS3; -.
DR PDBsum; 4TS9; -.
DR PDBsum; 4TTA; -.
DR PDBsum; 4TTI; -.
DR PDBsum; 4TTJ; -.
DR PDBsum; 5I3C; -.
DR PDBsum; 5IU6; -.
DR PDBsum; 6XZ2; -.
DR AlphaFoldDB; P0ABP8; -.
DR SMR; P0ABP8; -.
DR BioGRID; 4263006; 10.
DR DIP; DIP-36195N; -.
DR IntAct; P0ABP8; 2.
DR MINT; P0ABP8; -.
DR STRING; 511145.b4384; -.
DR DrugBank; DB02947; 2-Fluoro-2'-Deoxyadenosine.
DR DrugBank; DB04441; 2-Fluoroadenosine.
DR DrugBank; DB03986; 6-methyl-formycin A.
DR DrugBank; DB02113; 6-Methylpurine.
DR DrugBank; DB03735; 9-(2-Deoxy-Beta-D-Ribofuranosyl)-6-Methylpurine.
DR DrugBank; DB02934; 9-(6-deoxy-alpha-L-talofuranosyl)-6-methylpurine.
DR DrugBank; DB03952; 9-(6-deoxy-beta-D-allofuranosyl)-6-methylpurine.
DR DrugBank; DB03528; 9-Beta-D-Xylofuranosyl-Adenine.
DR DrugBank; DB04198; Formycin B.
DR DrugBank; DB04335; Inosine.
DR DrugBank; DB02896; Methylthioinosine.
DR DrugBank; DB02066; N7-Methyl-Formycin A.
DR DrugBank; DB03172; Tubercidin.
DR iPTMnet; P0ABP8; -.
DR SWISS-2DPAGE; P0ABP8; -.
DR jPOST; P0ABP8; -.
DR PaxDb; P0ABP8; -.
DR PRIDE; P0ABP8; -.
DR EnsemblBacteria; AAC77337; AAC77337; b4384.
DR EnsemblBacteria; BAE78373; BAE78373; BAE78373.
DR GeneID; 66671728; -.
DR GeneID; 945654; -.
DR KEGG; ecj:JW4347; -.
DR KEGG; eco:b4384; -.
DR PATRIC; fig|1411691.4.peg.2301; -.
DR EchoBASE; EB0218; -.
DR eggNOG; COG0813; Bacteria.
DR HOGENOM; CLU_068457_2_0_6; -.
DR InParanoid; P0ABP8; -.
DR OMA; PQCLLCG; -.
DR PhylomeDB; P0ABP8; -.
DR BioCyc; EcoCyc:DEOD-MON; -.
DR BioCyc; MetaCyc:DEOD-MON; -.
DR BRENDA; 2.4.2.1; 2026.
DR EvolutionaryTrace; P0ABP8; -.
DR PRO; PR:P0ABP8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0047975; F:guanosine phosphorylase activity; IEA:RHEA.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IDA:UniProtKB.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0006152; P:purine nucleoside catabolic process; IMP:EcoCyc.
DR GO; GO:0019686; P:purine nucleoside interconversion; IDA:EcoCyc.
DR CDD; cd09006; PNP_EcPNPI-like; 1.
DR Gene3D; 3.40.50.1580; -; 1.
DR HAMAP; MF_01627; Pur_nucleosid_phosp; 1.
DR InterPro; IPR004402; DeoD-type.
DR InterPro; IPR018016; Nucleoside_phosphorylase_CS.
DR InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR PANTHER; PTHR43691:SF2; PTHR43691:SF2; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
DR TIGRFAMs; TIGR00107; deoD; 1.
DR PROSITE; PS01232; PNP_UDP_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing; Glycosyltransferase;
KW Reference proteome; Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8506346"
FT CHAIN 2..239
FT /note="Purine nucleoside phosphorylase DeoD-type"
FT /id="PRO_0000063130"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01627,
FT ECO:0000269|PubMed:30337572"
FT BINDING 5
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000305|PubMed:30337572,
FT ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9,
FT ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI,
FT ECO:0007744|PDB:4TTJ"
FT BINDING 21
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:11786017,
FT ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572,
FT ECO:0007744|PDB:1K9S, ECO:0007744|PDB:3ONV,
FT ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH,
FT ECO:0007744|PDB:3OPV, ECO:0007744|PDB:4TS3,
FT ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA,
FT ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ"
FT BINDING 25
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:11786017,
FT ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572,
FT ECO:0007744|PDB:1K9S, ECO:0007744|PDB:3ONV,
FT ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH,
FT ECO:0007744|PDB:3OPV, ECO:0007744|PDB:4TS3,
FT ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA,
FT ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ"
FT BINDING 44
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000269|PubMed:11786017,
FT ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572,
FT ECO:0007744|PDB:1K9S, ECO:0007744|PDB:3ONV,
FT ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH,
FT ECO:0007744|PDB:3OPV, ECO:0007744|PDB:4TS3,
FT ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA,
FT ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ"
FT BINDING 88..91
FT /ligand="phosphate"
FT /ligand_id="ChEBI:CHEBI:43474"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000269|PubMed:11786017,
FT ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572,
FT ECO:0007744|PDB:1K9S, ECO:0007744|PDB:3ONV,
FT ECO:0007744|PDB:3OOE, ECO:0007744|PDB:3OOH,
FT ECO:0007744|PDB:3OPV, ECO:0007744|PDB:4TS3,
FT ECO:0007744|PDB:4TS9, ECO:0007744|PDB:4TTA,
FT ECO:0007744|PDB:4TTI, ECO:0007744|PDB:4TTJ"
FT BINDING 180..182
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000305|PubMed:30337572,
FT ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9,
FT ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI,
FT ECO:0007744|PDB:4TTJ"
FT BINDING 204..205
FT /ligand="a purine D-ribonucleoside"
FT /ligand_id="ChEBI:CHEBI:142355"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000305|PubMed:30337572,
FT ECO:0007744|PDB:4TS3, ECO:0007744|PDB:4TS9,
FT ECO:0007744|PDB:4TTA, ECO:0007744|PDB:4TTI,
FT ECO:0007744|PDB:4TTJ"
FT SITE 218
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01627,
FT ECO:0000269|PubMed:21672603, ECO:0000269|PubMed:30337572"
FT MOD_RES 27
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000269|PubMed:18723842"
FT MUTAGEN 25
FT /note="R->A: Severe loss of catalytic activity. 20-fold
FT decrease in affinity for phosphate."
FT /evidence="ECO:0000269|PubMed:21672603"
FT MUTAGEN 205
FT /note="D->A,N: Severe loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:21672603,
FT ECO:0000269|PubMed:30337572"
FT MUTAGEN 218
FT /note="R->A: Severe loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:21672603,
FT ECO:0000269|PubMed:30337572"
FT STRAND 15..19
FT /evidence="ECO:0007829|PDB:6XZ2"
FT HELIX 24..33
FT /evidence="ECO:0007829|PDB:6XZ2"
FT STRAND 35..41
FT /evidence="ECO:0007829|PDB:6XZ2"
FT HELIX 43..45
FT /evidence="ECO:0007829|PDB:6XZ2"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:6XZ2"
FT STRAND 56..61
FT /evidence="ECO:0007829|PDB:6XZ2"
FT HELIX 67..80
FT /evidence="ECO:0007829|PDB:6XZ2"
FT STRAND 85..94
FT /evidence="ECO:0007829|PDB:6XZ2"
FT STRAND 96..99
FT /evidence="ECO:0007829|PDB:3OOH"
FT STRAND 104..113
FT /evidence="ECO:0007829|PDB:6XZ2"
FT HELIX 116..120
FT /evidence="ECO:0007829|PDB:6XZ2"
FT TURN 121..123
FT /evidence="ECO:0007829|PDB:6XZ2"
FT HELIX 132..144
FT /evidence="ECO:0007829|PDB:6XZ2"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:6XZ2"
FT HELIX 166..173
FT /evidence="ECO:0007829|PDB:6XZ2"
FT STRAND 178..182
FT /evidence="ECO:0007829|PDB:6XZ2"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:6XZ2"
FT STRAND 196..206
FT /evidence="ECO:0007829|PDB:6XZ2"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:4TS9"
FT HELIX 215..236
FT /evidence="ECO:0007829|PDB:6XZ2"
SQ SEQUENCE 239 AA; 25950 MW; 71D3DFAA5A176970 CRC64;
MATPHINAEM GDFADVVLMP GDPLRAKYIA ETFLEDAREV NNVRGMLGFT GTYKGRKISV
MGHGMGIPSC SIYTKELITD FGVKKIIRVG SCGAVLPHVK LRDVVIGMGA CTDSKVNRIR
FKDHDFAAIA DFDMVRNAVD AAKALGIDAR VGNLFSADLF YSPDGEMFDV MEKYGILGVE
MEAAGIYGVA AEFGAKALTI CTVSDHIRTH EQTTAAERQT TFNDMIKIAL ESVLLGDKE
