ID DEOD_BACAH Reviewed; 235 AA. AC A0RBS0; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 27-MAR-2024, entry version 99. 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}; GN Name=deoD {ECO:0000255|HAMAP-Rule:MF_01627}; GN OrderedLocusNames=BALH_1318; OS Bacillus thuringiensis (strain Al Hakam). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=412694; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Al Hakam; RX PubMed=17337577; DOI=10.1128/jb.00241-07; RA Challacombe J.F., Altherr M.R., Xie G., Bhotika S.S., Brown N., Bruce D., RA Campbell C.S., Campbell M.L., Chen J., Chertkov O., Cleland C., RA Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T., Goodwin L.A., RA Green L.D., Han C.S., Hill K.K., Hitchcock P., Jackson P.J., Keim P., RA Kewalramani A.R., Longmire J., Lucas S., Malfatti S., Martinez D., RA McMurry K., Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C., RA Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P., RA Robinson D.L., Saunders E., Tapia R., Tesmer J.G., Thayer N., RA Thompson L.S., Tice H., Ticknor L.O., Wills P.L., Gilna P., Brettin T.S.; RT "The complete genome sequence of Bacillus thuringiensis Al Hakam."; RL J. Bacteriol. 189:3680-3681(2007). 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. {ECO:0000255|HAMAP-Rule:MF_01627}. 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 -!- SUBUNIT: Homohexamer; trimer of homodimers. {ECO:0000255|HAMAP- CC Rule:MF_01627}. CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. CC {ECO:0000255|HAMAP-Rule:MF_01627}. 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; CP000485; ABK84663.1; -; Genomic_DNA. DR RefSeq; WP_000110707.1; NC_008600.1. DR AlphaFoldDB; A0RBS0; -. DR SMR; A0RBS0; -. DR GeneID; 84224236; -. DR KEGG; btl:BALH_1318; -. DR HOGENOM; CLU_068457_2_0_9; -. DR Proteomes; UP000000761; Chromosome. DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009164; P:nucleoside catabolic process; IEA:UniProt. DR GO; GO:0042278; P:purine nucleoside metabolic process; IEA:UniProtKB-UniRule. 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:SF11; FI09636P-RELATED; 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. PE 3: Inferred from homology; KW Glycosyltransferase; Transferase. FT CHAIN 1..235 FT /note="Purine nucleoside phosphorylase DeoD-type" FT /id="PRO_1000069619" FT ACT_SITE 204 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01627" FT BINDING 4 FT /ligand="a purine D-ribonucleoside" FT /ligand_id="ChEBI:CHEBI:142355" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P50389" FT BINDING 20 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:0000250|UniProtKB:P50389" FT BINDING 24 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:0000250|UniProtKB:P50389" FT BINDING 43 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P50389" FT BINDING 87..90 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:0000250|UniProtKB:P50389" FT BINDING 179..181 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:0000250|UniProtKB:P50389" FT BINDING 203..204 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:0000250|UniProtKB:P50389" FT SITE 217 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01627" SQ SEQUENCE 235 AA; 25675 MW; 41A138A380CA3C31 CRC64; MSVHIEAKQG EIAESILLPG DPLRAKYIAE TFLEDVTCYN NVRGMLGFTG TYKGKRVSVQ GTGMGVPSIS IYVNELIQSY GVKNLIRVGT CGAIQKDVKV RDVIIAMTAC TDSNMNRLTF PGFDFAPAAN FDLLKKAYDA GTEKGLHVRV GNVLTADVFY RESMDMVKKL GDYGVLAVEM ETTALYTLAA KYGVNALSVL TVSDHIFTGE ETTSEERQTT FNEMIEIALD AAIQQ //