ID   DEOD_SALTY              Reviewed;         239 AA.
AC   Q8ZJV7;
DT   10-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 112.
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:235429};
GN   Name=deoD {ECO:0000255|HAMAP-Rule:MF_01627};
GN   OrderedLocusNames=STM4570;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
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).
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). Acts on 6-amino and 6-oxopurines including
CC       deoxyinosine, deoxyguanosine, deoxyadenosine, adenosine, guanosine, and
CC       inosine (PubMed:235429). {ECO:0000269|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:235429};
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:235429};
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: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=100 uM for phosphate (at pH 7.1) {ECO:0000269|PubMed:235429};
CC         KM=90 uM for inosine (at pH 7.1) {ECO:0000269|PubMed:235429};
CC         KM=170 uM for deoxyinosine (at pH 7.1) {ECO:0000269|PubMed:235429};
CC         KM=100 uM for deoxyribose-1-phosphate (at pH 7.1)
CC         {ECO:0000269|PubMed:235429};
CC         KM=110 uM for adenine (at pH 7.1) {ECO:0000269|PubMed:235429};
CC         Vmax=115 umol/min/mg enzyme toward phosphate (at pH 7.1)
CC         {ECO:0000269|PubMed:235429};
CC         Vmax=352 umol/min/mg enzyme toward inosine (at pH 7.1)
CC         {ECO:0000269|PubMed:235429};
CC         Vmax=732 umol/min/mg enzyme toward deoxyinosine (at pH 7.1)
CC         {ECO:0000269|PubMed:235429};
CC         Vmax=1025 umol/min/mg enzyme toward deoxyribose-1-phosphate (at pH
CC         7.1) {ECO:0000269|PubMed:235429};
CC         Vmax=795 umol/min/mg enzyme toward adenine (with
CC         deoxyribose-1-phosphate as cosubstrate and at pH 7.1)
CC         {ECO:0000269|PubMed:235429};
CC   -!- SUBUNIT: Homohexamer; trimer of homodimers. {ECO:0000255|HAMAP-
CC       Rule:MF_01627, ECO:0000269|PubMed:235429}.
CC   -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01627}.
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DR   EMBL; AE006468; AAL23385.1; -; Genomic_DNA.
DR   RefSeq; NP_463426.1; NC_003197.2.
DR   RefSeq; WP_000224870.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZJV7; -.
DR   SMR; Q8ZJV7; -.
DR   STRING; 99287.STM4570; -.
DR   PaxDb; 99287-STM4570; -.
DR   GeneID; 1256096; -.
DR   KEGG; stm:STM4570; -.
DR   PATRIC; fig|99287.12.peg.4812; -.
DR   HOGENOM; CLU_068457_2_0_6; -.
DR   OMA; PQCLLCG; -.
DR   PhylomeDB; Q8ZJV7; -.
DR   BioCyc; SENT99287:STM4570-MONOMER; -.
DR   SABIO-RK; Q8ZJV7; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0047975; F:guanosine phosphorylase activity; IEA:RHEA.
DR   GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IBA:GO_Central.
DR   GO; GO:0006152; P:purine nucleoside catabolic process; IBA:GO_Central.
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.
PE   1: Evidence at protein level;
KW   Glycosyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..239
FT                   /note="Purine nucleoside phosphorylase DeoD-type"
FT                   /id="PRO_0000063158"
FT   ACT_SITE        205
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P0ABP8, ECO:0000255|HAMAP-
FT                   Rule:MF_01627"
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:0000250|UniProtKB:P50389, ECO:0000255|HAMAP-
FT                   Rule:MF_01627"
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:0000250|UniProtKB:P50389, ECO:0000255|HAMAP-
FT                   Rule:MF_01627"
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:0000250|UniProtKB:P50389, ECO:0000255|HAMAP-
FT                   Rule:MF_01627"
FT   BINDING         44
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000250|UniProtKB:P50389, ECO:0000255|HAMAP-
FT                   Rule:MF_01627"
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:0000250|UniProtKB:P50389, ECO:0000255|HAMAP-
FT                   Rule:MF_01627"
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:0000250|UniProtKB:P50389, ECO:0000255|HAMAP-
FT                   Rule:MF_01627"
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:0000250|UniProtKB:P50389, ECO:0000255|HAMAP-
FT                   Rule:MF_01627"
FT   SITE            218
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250|UniProtKB:P0ABP8, ECO:0000255|HAMAP-
FT                   Rule:MF_01627"
SQ   SEQUENCE   239 AA;  25978 MW;  90ED901A61814796 CRC64;
     MATPHINAEM GDFADVVLMP GDPLRAKHIA ETFLENVREV NNVRGMLGFT GTYKGRKISV
     MGHGMGIPSC SIYTKELITD FGVKKIIRVG SCGAVRMDVK LRDVVIGMGA CTDSKVNRIR
     FKDHDFAAIA DFDMVRNAVD AAKALGVDAR VGNLFSADLF YSPDGEMFDV MEKYGVLGVE
     MEAAGIYGVA AEFGAKALTI CTVSDHIRTH EQTTAAERQT TFNDMIKIAL ESVLLGDKE
//