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Pyrimidine/purine nucleoside phosphorylase (EC 2.4.2.1) (EC 2.4.2.2) (Adenosine phosphorylase) (Cytidine phosphorylase) (Guanosine phosphorylase) (EC 2.4.2.15) (Inosine phosphorylase) (Thymidine phosphorylase) (EC 2.4.2.4) (Uridine phosphorylase) (EC 2.4.2.3) (Xanthosine phosphorylase)

 F0JJN8_DESDE            Unreviewed;       104 AA.
F0JJN8;
03-MAY-2011, integrated into UniProtKB/TrEMBL.
03-MAY-2011, sequence version 1.
27-SEP-2017, entry version 35.
RecName: Full=Pyrimidine/purine nucleoside phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537};
EC=2.4.2.1 {ECO:0000256|HAMAP-Rule:MF_01537};
EC=2.4.2.2 {ECO:0000256|HAMAP-Rule:MF_01537};
AltName: Full=Adenosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537};
AltName: Full=Cytidine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537};
AltName: Full=Guanosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537};
EC=2.4.2.15 {ECO:0000256|HAMAP-Rule:MF_01537};
AltName: Full=Inosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537};
AltName: Full=Thymidine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537};
EC=2.4.2.4 {ECO:0000256|HAMAP-Rule:MF_01537};
AltName: Full=Uridine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537};
EC=2.4.2.3 {ECO:0000256|HAMAP-Rule:MF_01537};
AltName: Full=Xanthosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537};
Name=ppnP {ECO:0000256|HAMAP-Rule:MF_01537};
ORFNames=DND132_2934 {ECO:0000313|EMBL:EGB16137.1};
Desulfovibrio desulfuricans ND132.
Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
Desulfovibrionaceae; Desulfovibrio.
NCBI_TaxID=641491 {ECO:0000313|EMBL:EGB16137.1, ECO:0000313|Proteomes:UP000007845};
[1] {ECO:0000313|EMBL:EGB16137.1, ECO:0000313|Proteomes:UP000007845}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ND132 {ECO:0000313|EMBL:EGB16137.1};
PubMed=21357488; DOI=10.1128/JB.00170-11;
Brown S.D., Gilmour C.C., Kucken A.M., Wall J.D., Elias D.A.,
Brandt C.C., Podar M., Chertkov O., Held B., Bruce D.C., Detter J.C.,
Tapia R., Han C.S., Goodwin L.A., Cheng J.F., Pitluck S., Woyke T.,
Mikhailova N., Ivanova N.N., Han J., Lucas S., Lapidus A.L.,
Land M.L., Hauser L.J., Palumbo A.V.;
"Genome sequence of the mercury-methylating strain Desulfovibrio
desulfuricans ND132.";
J. Bacteriol. 193:2078-2079(2011).
-!- FUNCTION: Catalyzes the phosphorolysis of diverse nucleosides,
yielding D-ribose 1-phosphate and the respective free bases. Can
use uridine, adenosine, guanosine, cytidine, thymidine, inosine
and xanthosine as substrates. Also catalyzes the reverse
reactions. {ECO:0000256|HAMAP-Rule:MF_01537,
ECO:0000256|SAAS:SAAS00810279}.
-!- CATALYTIC ACTIVITY: Adenosine + phosphate = adenine + alpha-D-
ribose 1-phosphate. {ECO:0000256|HAMAP-Rule:MF_01537,
ECO:0000256|SAAS:SAAS00810289}.
-!- CATALYTIC ACTIVITY: Cytidine + phosphate = cytosine + alpha-D-
ribose 1-phosphate. {ECO:0000256|HAMAP-Rule:MF_01537,
ECO:0000256|SAAS:SAAS00810284}.
-!- CATALYTIC ACTIVITY: Guanosine + phosphate = guanine + alpha-D-
ribose 1-phosphate. {ECO:0000256|HAMAP-Rule:MF_01537,
ECO:0000256|SAAS:SAAS00810281}.
-!- CATALYTIC ACTIVITY: Inosine + phosphate = hypoxanthine + alpha-D-
ribose 1-phosphate. {ECO:0000256|HAMAP-Rule:MF_01537,
ECO:0000256|SAAS:SAAS00810291}.
-!- CATALYTIC ACTIVITY: Purine nucleoside + phosphate = purine +
alpha-D-ribose 1-phosphate. {ECO:0000256|HAMAP-Rule:MF_01537,
ECO:0000256|SAAS:SAAS00810288}.
-!- CATALYTIC ACTIVITY: Thymidine + phosphate = thymine + 2-deoxy-
alpha-D-ribose 1-phosphate. {ECO:0000256|HAMAP-Rule:MF_01537,
ECO:0000256|SAAS:SAAS00810285}.
-!- CATALYTIC ACTIVITY: Uridine + phosphate = uracil + alpha-D-ribose
1-phosphate. {ECO:0000256|HAMAP-Rule:MF_01537,
ECO:0000256|SAAS:SAAS00810286}.
-!- CATALYTIC ACTIVITY: Xanthosine + phosphate = xanthine + alpha-D-
ribose 1-phosphate. {ECO:0000256|HAMAP-Rule:MF_01537,
ECO:0000256|SAAS:SAAS00810283}.
-!- SIMILARITY: Belongs to the nucleoside phosphorylase PpnP family.
{ECO:0000256|HAMAP-Rule:MF_01537, ECO:0000256|SAAS:SAAS00810292}.
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EMBL; CP003220; EGB16137.1; -; Genomic_DNA.
RefSeq; WP_014323561.1; NC_016803.1.
STRING; 641491.DND132_2934; -.
EnsemblBacteria; EGB16137; EGB16137; DND132_2934.
KEGG; ddn:DND132_2934; -.
eggNOG; ENOG4105NBK; Bacteria.
eggNOG; COG3123; LUCA.
KO; K09913; -.
OrthoDB; POG091H03LQ; -.
BioCyc; DDES641491:GH21-2974-MONOMER; -.
Proteomes; UP000007845; Chromosome.
GO; GO:0047975; F:guanosine phosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:UniProtKB-UniRule.
GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:UniProtKB-UniRule.
GO; GO:0009032; F:thymidine phosphorylase activity; IEA:UniProtKB-EC.
GO; GO:0004850; F:uridine phosphorylase activity; IEA:UniProtKB-EC.
Gene3D; 2.60.120.10; -; 1.
HAMAP; MF_01537; UPF0345; 1.
InterPro; IPR009664; Ppnp.
InterPro; IPR014710; RmlC-like_jellyroll.
InterPro; IPR011051; RmlC_Cupin.
Pfam; PF06865; DUF1255; 1.
SUPFAM; SSF51182; SSF51182; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000007845};
Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01537,
ECO:0000256|SAAS:SAAS00810282};
Reference proteome {ECO:0000313|Proteomes:UP000007845};
Transferase {ECO:0000256|HAMAP-Rule:MF_01537,
ECO:0000256|SAAS:SAAS00810282}.
SEQUENCE 104 AA; 11357 MW; EAAA58795D9E6937 CRC64;
MTAFANATIK KQANIYFDGK VTSRTITLND GSVVTLGIML PGEYEFGTEK PEFMEITSGE
LSVQLPGIDD WVAVTSGQSF NVPGEAKFRL KVSTVTDYCC SYLD


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