ID   LIPL_STRSQ              Reviewed;         274 AA.
AC   D4QF25;
DT   12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=Uridine-5'-phosphate dioxygenase {ECO:0000305};
DE            EC=1.14.11.49 {ECO:0000269|PubMed:21216959, ECO:0000269|PubMed:23034228};
DE   AltName: Full=Fe(II)-dependent alpha-ketoglutarate:uridine-5'-monophosphate dioxygenase {ECO:0000303|PubMed:21216959};
DE            Short=Fe(II)-dependent alpha-KG:UMP dioxygenase {ECO:0000303|PubMed:21216959};
DE   AltName: Full=UMP:alpha-ketoglutarate dioxygenase {ECO:0000303|PubMed:23034228};
GN   Name=lipL {ECO:0000303|PubMed:20043306};
OS   Streptomyces sp.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=SANK 60405;
RX   PubMed=20043306; DOI=10.1002/cbic.200900665;
RA   Funabashi M., Baba S., Nonaka K., Hosobuchi M., Fujita Y., Shibata T.,
RA   Van Lanene S.G.;
RT   "The biosynthesis of liposidomycin-like A-90289 antibiotics featuring a new
RT   type of sulfotransferase.";
RL   ChemBioChem 11:184-190(2010).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY REGULATION, AND
RP   BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=SANK 60405;
RX   PubMed=21216959; DOI=10.1074/jbc.m110.203562;
RA   Yang Z., Chi X., Funabashi M., Baba S., Nonaka K., Pahari P., Unrine J.,
RA   Jacobsen J.M., Elliott G.I., Rohr J., Van Lanen S.G.;
RT   "Characterization of LipL as a non-heme, Fe(II)-dependent alpha-
RT   ketoglutarate:UMP dioxygenase that generates uridine-5'-aldehyde during A-
RT   90289 biosynthesis.";
RL   J. Biol. Chem. 286:7885-7892(2011).
RN   [3]
RP   CATALYTIC ACTIVITY.
RC   STRAIN=SANK 60405;
RX   PubMed=23034228; DOI=10.1016/b978-0-12-394291-3.00031-9;
RA   Yang Z., Unrine J., Nonaka K., Van Lanen S.G.;
RT   "Fe(II)-dependent, uridine-5'-monophosphate alpha-ketoglutarate
RT   dioxygenases in the synthesis of 5'-modified nucleosides.";
RL   Methods Enzymol. 516:153-168(2012).
CC   -!- FUNCTION: Catalyzes the dephosphorylation and oxidation of UMP to
CC       generate 5'-dehydrouridine, the first intermediate in the biosynthesis
CC       of the liposidomycin-like A-90289 antibiotic.
CC       {ECO:0000269|PubMed:21216959}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + O2 + UMP = CO2 + phosphate + succinate +
CC         uridine-5'-aldehyde; Xref=Rhea:RHEA:46500, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:30031,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57865, ChEBI:CHEBI:86258;
CC         EC=1.14.11.49; Evidence={ECO:0000269|PubMed:21216959,
CC         ECO:0000269|PubMed:23034228};
CC   -!- COFACTOR:
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000269|PubMed:21216959};
CC   -!- ACTIVITY REGULATION: Inhibited by several divalent cations, including
CC       Zn(2+). {ECO:0000269|PubMed:21216959}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=7.5 uM for 2-oxoglutarate {ECO:0000269|PubMed:21216959};
CC         KM=14 uM for UMP {ECO:0000269|PubMed:21216959};
CC         Note=kcat is 92 min(-1) with 2-oxoglutarate as substrate. kcat is 76
CC         min(-1) with UMP as substrate. {ECO:0000269|PubMed:21216959};
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DR   EMBL; AB530986; BAJ05888.1; -; Genomic_DNA.
DR   AlphaFoldDB; D4QF25; -.
DR   SMR; D4QF25; -.
DR   KEGG; ag:BAJ05888; -.
DR   BioCyc; MetaCyc:MON-17977; -.
DR   GO; GO:0051213; F:dioxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.60.130.10; -; 1.
DR   InterPro; IPR042098; TauD-like_sf.
DR   InterPro; IPR003819; TauD/TfdA-like.
DR   Pfam; PF02668; TauD; 1.
PE   1: Evidence at protein level;
KW   Antibiotic biosynthesis; Dioxygenase; Iron; Metal-binding; Oxidoreductase.
FT   CHAIN           1..274
FT                   /note="Uridine-5'-phosphate dioxygenase"
FT                   /id="PRO_0000450626"
FT   BINDING         103
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P37610"
FT   BINDING         105
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P37610"
FT   BINDING         246
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:P37610"
SQ   SEQUENCE   274 AA;  30832 MW;  B54FE08CCC8ACF16 CRC64;
     MQLMKSSYLE LTARGHVTDL LKPDDTLEML ETYGFAVTQS PVEAVSTAHA YREIAAIRED
     FGLGEPYVPL LYRDRDEPTV TAVTRKGGSD HPVFHTGEAQ GWHTDGLLED IGTIKTTLLY
     CVSPAHRGGR TFLLNAGRVF EELRMEDPEA ADVLLRDTIL GRRSTIPGVD REAVGPVFLE
     LGDGHYATRY GEGRVERWYP ADAAEQHALD RALRFFRARR DDPDVRIDLL LRAGQCLIFR
     NDVLAHGREN FTDDPQRPRL LLRSLHTNAP KKPS