(data stored in ACNUC1104 zone)

SWISSPROT: D3UZ69_XENBS

ID   D3UZ69_XENBS            Unreviewed;       251 AA.
AC   D3UZ69;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 56.
DE   RecName: Full=Uridine phosphorylase {ECO:0000256|RuleBase:RU361131};
DE            EC=2.4.2.3 {ECO:0000256|RuleBase:RU361131};
GN   Name=udp {ECO:0000313|EMBL:CBJ79651.1};
GN   OrderedLocusNames=XBJ1_0502 {ECO:0000313|EMBL:CBJ79651.1};
OS   Xenorhabdus bovienii (strain SS-2004).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406818 {ECO:0000313|EMBL:CBJ79651.1, ECO:0000313|Proteomes:UP000002045};
RN   [1] {ECO:0000313|EMBL:CBJ79651.1, ECO:0000313|Proteomes:UP000002045}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SS-2004 {ECO:0000313|EMBL:CBJ79651.1,
RC   ECO:0000313|Proteomes:UP000002045};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
CC   -!- FUNCTION: Catalyzes the reversible phosphorylytic cleavage of
CC       uridine and deoxyuridine to uracil and ribose- or deoxyribose-1-
CC       phosphate. The produced molecules are then utilized as carbon and
CC       energy sources or in the rescue of pyrimidine bases for nucleotide
CC       synthesis. {ECO:0000256|RuleBase:RU361131}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate +
CC         uracil; Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704,
CC         ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720;
CC         EC=2.4.2.3; Evidence={ECO:0000256|RuleBase:RU361131};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage
CC       pathway; uracil from uridine (phosphorylase route): step 1/1.
CC       {ECO:0000256|RuleBase:RU361131}.
CC   -!- SUBUNIT: Homohexamer. {ECO:0000256|SAAS:SAAS01083847}.
CC   -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family.
CC       {ECO:0000256|RuleBase:RU361131, ECO:0000256|SAAS:SAAS00886275}.
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DR   EMBL; FN667741; CBJ79651.1; -; Genomic_DNA.
DR   RefSeq; WP_012987107.1; NC_013892.1.
DR   STRING; 406818.XBJ1_0502; -.
DR   EnsemblBacteria; CBJ79651; CBJ79651; XBJ1_0502.
DR   GeneID; 8830125; -.
DR   KEGG; xbo:XBJ1_0502; -.
DR   PATRIC; fig|406818.4.peg.462; -.
DR   eggNOG; ENOG4108I5U; Bacteria.
DR   eggNOG; COG2820; LUCA.
DR   HOGENOM; HOG000274897; -.
DR   KO; K00757; -.
DR   OMA; MSDVFHL; -.
DR   BioCyc; XBOV406818:XBJ1_RS02165-MONOMER; -.
DR   UniPathway; UPA00574; UER00633.
DR   Proteomes; UP000002045; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR   GO; GO:0004850; F:uridine phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro.
DR   GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR   GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.50.1580; -; 1.
DR   InterPro; IPR018016; Nucleoside_phosphorylase_CS.
DR   InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR   InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR   InterPro; IPR010058; Uridine_phosphorylase.
DR   PANTHER; PTHR43691:SF7; PTHR43691:SF7; 1.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   SUPFAM; SSF53167; SSF53167; 1.
DR   TIGRFAMs; TIGR01718; Uridine-psphlse; 1.
DR   PROSITE; PS01232; PNP_UDP_1; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3UZ69.
DR   SWISS-2DPAGE; D3UZ69.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002045};
KW   Glycosyltransferase {ECO:0000256|RuleBase:RU361131,
KW   ECO:0000256|SAAS:SAAS00886268, ECO:0000313|EMBL:CBJ79651.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002045};
KW   Transferase {ECO:0000256|RuleBase:RU361131,
KW   ECO:0000256|SAAS:SAAS00886295, ECO:0000313|EMBL:CBJ79651.1}.
FT   DOMAIN       19    225       PNP_UDP_1. {ECO:0000259|Pfam:PF01048}.
SQ   SEQUENCE   251 AA;  26854 MW;  620A7DC54C74A050 CRC64;
     MSDVFHLGIT KSDLQGATLA IVPGDPNRVE KIAKLMDNPV HLASHREFTT WRAEIDGKPV
     VVCSTGIGGP STSIAVEELA QLGVSTFLRI GTTGAIQPHI NVGDVLVTTA AVRLDGASLH
     FAPMEFPAVA DFECTNALYA AAKASGSATH VGITASSDTF YPGQERYDTY SGRVVRRFQG
     SMQEWQQMGV MNYEMESATL LTMCASQGLR AGMVAGVIVN RTQQEIPDVE LLKKTESNAL
     GIVVDAARRL L
//

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