ID   CDO_CAEBR               Reviewed;         190 AA.
AC   Q60TI7; A8XXT1;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   24-JAN-2024, entry version 97.
DE   RecName: Full=Cysteine dioxygenase;
DE            Short=CDO;
DE            EC=1.13.11.20;
GN   Name=cdo-1; ORFNames=CBG20456;
OS   Caenorhabditis briggsae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6238;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF16;
RX   PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA   Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA   Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA   Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA   Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA   Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA   Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA   Durbin R.M., Waterston R.H.;
RT   "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT   genomics.";
RL   PLoS Biol. 1:166-192(2003).
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}.
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DR   EMBL; HE601085; CAP37450.3; -; Genomic_DNA.
DR   RefSeq; XP_002632069.1; XM_002632023.1.
DR   AlphaFoldDB; Q60TI7; -.
DR   SMR; Q60TI7; -.
DR   STRING; 6238.Q60TI7; -.
DR   EnsemblMetazoa; CBG20456.1; CBG20456.1; WBGene00039434.
DR   GeneID; 8574068; -.
DR   KEGG; cbr:CBG_20456; -.
DR   CTD; 8574068; -.
DR   WormBase; CBG20456; CBP11524; WBGene00039434; Cbr-cdo-1.
DR   eggNOG; KOG4064; Eukaryota.
DR   HOGENOM; CLU_079443_4_1_1; -.
DR   InParanoid; Q60TI7; -.
DR   OMA; MLLCWGE; -.
DR   OrthoDB; 314969at2759; -.
DR   UniPathway; UPA00012; UER00537.
DR   Proteomes; UP000008549; Chromosome II.
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"
FT                   /id="PRO_0000206611"
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;  21962 MW;  85AC945875B513F7 CRC64;
     MVSFVQLVVQ IREIFEHKMV DVDEVMKLMG SYKSDINEWR RFAIFDMNKY TRNLVDIGNG
     KYNLMILCWG PGMASSVHDH TDAHCFVKIL DGELTETKYD WPKKKHTPLE TIENKTYGLN
     GVSYMNDELG LHRMENQSHS NGAVSLHLYI PPYSTCNAFD ERTGKKTKCT VTFYSKYGEK
     IDYHGSKEGK
//