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 24-JAN-2024, entry version 140. 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; Pseudomonadota; 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 CC deoxyribose-1-phosphate as cosubstrate and at pH 7.1) CC {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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 jPOST; P0ABP8; -. DR PaxDb; 511145-b4384; -. DR EnsemblBacteria; AAC77337; AAC77337; b4384. DR GeneID; 75202933; -. 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 OrthoDB; 9782889at2; -. DR PhylomeDB; P0ABP8; -. DR BioCyc; EcoCyc:DEOD-MONOMER; -. DR BioCyc; MetaCyc:DEOD-MONOMER; -. 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:DNA damage response; 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; Nucleoside phosphorylase domain; 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 NCBIfam; TIGR00107; deoD; 1. DR PANTHER; PTHR43691:SF2; PURINE NUCLEOSIDE PHOSPHORYLASE DEOD-TYPE; 1. DR PANTHER; PTHR43691; URIDINE PHOSPHORYLASE; 1. DR Pfam; PF01048; PNP_UDP_1; 1. DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1. DR PROSITE; PS01232; PNP_UDP_1; 1. DR SWISS-2DPAGE; P0ABP8; -. 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 //