DEOD_SALTY
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 03-AUG-2022, entry version 104.
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}; OrderedLocusNames=STM4570;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; 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 deoxyribose-1-
CC phosphate as cosubstrate and at pH 7.1) {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; Q8ZJV7; -.
DR EnsemblBacteria; AAL23385; AAL23385; 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-MON; -.
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; -; 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 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
