URC1_LACKL
ID URC1_LACKL Reviewed; 444 AA.
AC Q6YFE5;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 44.
DE RecName: Full=Putative GTP cyclohydrolase URC1;
DE AltName: Full=Uracil catabolism protein 1;
DE EC=3.5.4.-;
GN Name=URC1;
OS Lachancea kluyveri (Yeast) (Saccharomyces kluyveri).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Lachancea.
OX NCBI_TaxID=4934;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RX PubMed=18550080; DOI=10.1016/j.jmb.2008.05.029;
RA Andersen G., Bjoernberg O., Polakova S., Pynyaha Y., Rasmussen A.,
RA Moeller K., Hofer A., Moritz T., Sandrini M.P., Merico A.M., Compagno C.,
RA Aekerlund H.E., Gojkovic Z., Piskur J.;
RT "A second pathway to degrade pyrimidine nucleic acid precursors in
RT eukaryotes.";
RL J. Mol. Biol. 380:656-666(2008).
CC -!- FUNCTION: Involved in uracil catabolism. {ECO:0000269|PubMed:18550080}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase II family. {ECO:0000305}.
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DR EMBL; AY154654; AAO06876.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6YFE5; -.
DR SMR; Q6YFE5; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003935; F:GTP cyclohydrolase II activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR CDD; cd00641; GTP_cyclohydro2; 1.
DR Gene3D; 3.40.50.10990; -; 1.
DR InterPro; IPR022163; GTP_CH_N.
DR InterPro; IPR032677; GTP_cyclohydro_II.
DR InterPro; IPR000926; RibA.
DR InterPro; IPR036144; RibA-like_sf.
DR Pfam; PF12471; GTP_CH_N; 1.
DR Pfam; PF00925; GTP_cyclohydro2; 1.
DR SUPFAM; SSF142695; SSF142695; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Hydrolase; Metal-binding; Nucleotide-binding;
KW Nucleus; Zinc.
FT CHAIN 1..444
FT /note="Putative GTP cyclohydrolase URC1"
FT /id="PRO_0000367270"
FT ACT_SITE 353
FT /note="Proton acceptor"
FT /evidence="ECO:0000255"
FT ACT_SITE 355
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 268..272
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 315..317
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 377
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 382
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 444 AA; 49332 MW; 2E8236E4621F1392 CRC64;
MSPIAVTSQT PATEVPSVKE IPQVITKSSP VENLILTTYP EDSSPIPLQW GAPSTDSRGP
IIATRYKEGL AKHNAIGAHS GSYCVYHALA VGTKQLDPEH VADYTNSQPA FAVPEQKTWY
NDEDIVAMDP FGHLTPYLFD EVSTKENVEI RPTIAVTKAT MQLFEMKDAV EKGRLEVDGE
VVINKNGDLN VSKVAVEPVW YLPGVAKRFG VTEEELRKAL FEDTNGMYPE LVTRPDIKVF
LPPIGGLTVY IFGNPDFVSD PSKKLALRVH DECNGSDVFG SDICTCRPYL MFGIEEAVKE
AQNGGSGVVV YFRKEGRALG EVTKYLVYNA RKRGGDTADE YFHRTECIAG VRDMRFQQLM
PDVLKWLGIS KIDRMLSMSN MKHDAIVDQG IPIIERIPIP DELVPPDSRV EIDAKINSGY
FTNGKVMDKN ELKSVQGRTW NDVK
