ID CDO1_CAEEL Reviewed; 190 AA. AC Q20893; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2001, sequence version 2. DT 27-MAR-2024, entry version 133. DE RecName: Full=Cysteine dioxygenase 1; DE Short=CDO; DE EC=1.13.11.20; GN Name=cdo-1; ORFNames=F56F10.3; OS Caenorhabditis elegans. OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; OC Caenorhabditis. OX NCBI_TaxID=6239; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Bristol N2; RX PubMed=9851916; DOI=10.1126/science.282.5396.2012; RG The C. elegans sequencing consortium; RT "Genome sequence of the nematode C. elegans: a platform for investigating RT biology."; RL Science 282:2012-2018(1998). CC -!- CATALYTIC ACTIVITY: CC Reaction=L-cysteine + O2 = 3-sulfino-L-alanine + H(+); CC Xref=Rhea:RHEA:20441, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, CC ChEBI:CHEBI:35235, ChEBI:CHEBI:61085; EC=1.13.11.20; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250}; CC Note=Binds 1 Fe cation per subunit. {ECO:0000250}; CC -!- PATHWAY: Organosulfur biosynthesis; taurine biosynthesis; hypotaurine CC from L-cysteine: step 1/2. CC -!- PTM: The thioether cross-link between Cys-85 and Tyr-149 plays a CC structural role through stabilizing the Fe(2+) ion, and prevents the CC production of highly damaging free hydroxyl radicals by holding the CC oxygen radical via hydroxyl hydrogen. {ECO:0000250|UniProtKB:Q16878}. CC -!- SIMILARITY: Belongs to the cysteine dioxygenase family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; FO081336; CCD70867.1; -; Genomic_DNA. DR PIR; T16488; T16488. DR RefSeq; NP_508168.1; NM_075767.3. DR AlphaFoldDB; Q20893; -. DR SMR; Q20893; -. DR BioGRID; 45387; 5. DR STRING; 6239.F56F10.3.2; -. DR EPD; Q20893; -. DR PaxDb; 6239-F56F10-3; -. DR PeptideAtlas; Q20893; -. DR EnsemblMetazoa; F56F10.3.1; F56F10.3.1; WBGene00018986. DR GeneID; 180434; -. DR KEGG; cel:CELE_F56F10.3; -. DR UCSC; F56F10.3; c. elegans. DR AGR; WB:WBGene00018986; -. DR WormBase; F56F10.3; CE28465; WBGene00018986; cdo-1. DR eggNOG; KOG4064; Eukaryota. DR GeneTree; ENSGT00390000018226; -. DR HOGENOM; CLU_079443_4_1_1; -. DR InParanoid; Q20893; -. DR OMA; NQVAYMA; -. DR OrthoDB; 314969at2759; -. DR PhylomeDB; Q20893; -. DR Reactome; R-CEL-1614558; Degradation of cysteine and homocysteine. DR UniPathway; UPA00012; UER00537. DR PRO; PR:Q20893; -. DR Proteomes; UP000001940; Chromosome X. DR Bgee; WBGene00018986; Expressed in larva and 4 other cell types or tissues. DR GO; GO:0017172; F:cysteine dioxygenase activity; IBA:GO_Central. DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central. DR GO; GO:0019448; P:L-cysteine catabolic process; IBA:GO_Central. DR GO; GO:0042412; P:taurine biosynthetic process; IEA:UniProtKB-UniPathway. DR CDD; cd10548; cupin_CDO; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 1. DR InterPro; IPR010300; CDO_1. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin_sf. DR PANTHER; PTHR12918; CYSTEINE DIOXYGENASE; 1. DR PANTHER; PTHR12918:SF1; CYSTEINE DIOXYGENASE TYPE 1; 1. DR Pfam; PF05995; CDO_I; 1. DR SUPFAM; SSF51182; RmlC-like cupins; 1. PE 3: Inferred from homology; KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome; KW Thioether bond. FT CHAIN 1..190 FT /note="Cysteine dioxygenase 1" FT /id="PRO_0000206612" FT BINDING 78 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:Q16878" FT BINDING 80 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:Q16878" FT BINDING 132 FT /ligand="Fe cation" FT /ligand_id="ChEBI:CHEBI:24875" FT /ligand_note="catalytic" FT /evidence="ECO:0000250|UniProtKB:Q16878" FT CROSSLNK 85..149 FT /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)" FT /evidence="ECO:0000250|UniProtKB:Q16878" SQ SEQUENCE 190 AA; 21879 MW; 273A194DBFFA0C55 CRC64; MISFVQLVVQ IREIFQQKLI DVDEVMKLMA SYKSNANEWR RFAIFDMNKY TRNLVDVGNG KYNLMILCWG PGMASSVHDH TDAHCFVKIL DGELTETKYA WPRKRHVPLD ISENKTYGMN GVSYMNDELG LHRMENLSHS NGAVSLHLYI PPYSTCNAFD ERTGKKTQCT VTFYSKYGKK VDYRGSKNGN //