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DEOD_LIMRJ
ID   DEOD_LIMRJ              Reviewed;         236 AA.
AC   B2G592;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 70.
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}; OrderedLocusNames=LAR_0108;
OS   Limosilactobacillus reuteri (strain JCM 1112) (Lactobacillus reuteri).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=557433;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 1112;
RX   PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA   Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA   Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA   Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA   Hattori M.;
RT   "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT   fermentum reveal a genomic island for reuterin and cobalamin production.";
RL   DNA Res. 15:151-161(2008).
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}.
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DR   EMBL; AP007281; BAG24624.1; -; Genomic_DNA.
DR   RefSeq; WP_003665392.1; NC_010609.1.
DR   AlphaFoldDB; B2G592; -.
DR   SMR; B2G592; -.
DR   GeneID; 66470196; -.
DR   KEGG; lrf:LAR_0108; -.
DR   HOGENOM; CLU_068457_2_0_9; -.
DR   OMA; PQCLLCG; -.
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; -; 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   3: Inferred from homology;
KW   Glycosyltransferase; Transferase.
FT   CHAIN           1..236
FT                   /note="Purine nucleoside phosphorylase DeoD-type"
FT                   /id="PRO_1000186209"
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   236 AA;  25751 MW;  3CBA0DBDB8F45770 CRC64;
     MSTHINAKMG DYADTVLLPG DPLRAKYIAE NFLENVKQVN SVRNAFGYTG EYKGHRISVQ
     GSGMGIPSMS IYINELVREF GVKTIIRVGS CGGIAPDVHV RDVLLAQGSS TDSAVTVNTF
     GPGFHYAPLA DFKLLDTAYH VAGKLGIETK VGDIFAADRF YNDELDMEKL RDYGILGTEM
     ESAGLYLLAA KLHFRALSVL TVSDLIFGDE KATAEERERT FNDMINISLE TAIAGK
 
 
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