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Database: UniProt
Entry: A0A1I1D7G8_9FIRM
LinkDB: A0A1I1D7G8_9FIRM
Original site: A0A1I1D7G8_9FIRM 
ID   A0A1I1D7G8_9FIRM        Unreviewed;       258 AA.
AC   A0A1I1D7G8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Uridine phosphorylase {ECO:0000256|ARBA:ARBA00021980, ECO:0000256|RuleBase:RU361131};
DE            EC=2.4.2.3 {ECO:0000256|ARBA:ARBA00011888, ECO:0000256|RuleBase:RU361131};
GN   ORFNames=SAMN02910398_00232 {ECO:0000313|EMBL:SFB68750.1};
OS   Butyrivibrio sp. YAB3001.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=1520812 {ECO:0000313|EMBL:SFB68750.1, ECO:0000313|Proteomes:UP000198944};
RN   [1] {ECO:0000313|EMBL:SFB68750.1, ECO:0000313|Proteomes:UP000198944}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YAB3001 {ECO:0000313|EMBL:SFB68750.1,
RC   ECO:0000313|Proteomes:UP000198944};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the reversible phosphorylytic cleavage of uridine
CC       to uracil and ribose-1-phosphate. {ECO:0000256|RuleBase:RU361131}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate + uracil;
CC         Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704, ChEBI:CHEBI:17568,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.3;
CC         Evidence={ECO:0000256|ARBA:ARBA00001020,
CC         ECO:0000256|RuleBase:RU361131};
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via salvage pathway;
CC       uracil from uridine (phosphorylase route): step 1/1.
CC       {ECO:0000256|ARBA:ARBA00004825, ECO:0000256|RuleBase:RU361131}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC   -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family.
CC       {ECO:0000256|ARBA:ARBA00010456, ECO:0000256|RuleBase:RU361131}.
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DR   EMBL; FOKR01000002; SFB68750.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1D7G8; -.
DR   STRING; 1520812.SAMN02910398_00232; -.
DR   OrthoDB; 9772602at2; -.
DR   UniPathway; UPA00574; UER00633.
DR   Proteomes; UP000198944; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004850; F:uridine phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009164; P:nucleoside catabolic process; IEA:UniProt.
DR   GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR   GO; GO:0044206; P:UMP salvage; IEA:UniProtKB-UniPathway.
DR   CDD; cd17767; UP_EcUdp-like; 1.
DR   Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 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   NCBIfam; TIGR01718; Uridine-psphlse; 1.
DR   PANTHER; PTHR43691:SF11; FI09636P-RELATED; 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   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU361131};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198944};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU361131}.
FT   DOMAIN          23..228
FT                   /note="Nucleoside phosphorylase"
FT                   /evidence="ECO:0000259|Pfam:PF01048"
SQ   SEQUENCE   258 AA;  28009 MW;  AA2C29448B876DD2 CRC64;
     MVDYTEGAGY QYHTHVKKGD VGRYVILTGD PGRCETISHL FDNPEFIAYN REYNTYTGTI
     NGEKVSVMST GIGGASTAIA VEELVKCGAD TFIRMGTSGG MQDDVIGGDI VIANGAIRAE
     GTSKEYAPIE YPAVASFDVV NSLVQAAKKT NAKYHVGVVQ CKDSFFGQHE PETKPVGPEL
     LYKWDAWIKC GALCSEMESS TLFIVGDYLR VRTGAVLLVV ANQERAKKGL SNPQAHDMDI
     VYKTTIEAIK SLIDMDKA
//
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