ID   CDO1_DANRE              Reviewed;         201 AA.
AC   Q6NWZ9;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Cysteine dioxygenase type 1;
DE            EC=1.13.11.20 {ECO:0000250|UniProtKB:Q16878};
DE   AltName: Full=Cysteine dioxygenase type I;
DE            Short=CDO;
DE            Short=CDO-I;
GN   Name=cdo1;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the oxidation of cysteine to cysteine sulfinic acid
CC       with addition of molecular dioxygen. {ECO:0000250|UniProtKB:Q16878}.
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         Evidence={ECO:0000250|UniProtKB:Q16878};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20442;
CC         Evidence={ECO:0000250|UniProtKB:Q16878};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000250|UniProtKB:P60334};
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000250|UniProtKB:P60334};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:P60334};
CC       Note=Binds 1 Fe cation per subunit. Ni(2+) and Zn(2+) can be used to a
CC       lesser extent. {ECO:0000250|UniProtKB:P60334};
CC   -!- PATHWAY: Organosulfur biosynthesis; taurine biosynthesis; hypotaurine
CC       from L-cysteine: step 1/2.
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q16878}.
CC   -!- PTM: The thioether cross-link between Cys-93 and Tyr-158 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; BC059531; AAH59531.1; -; mRNA.
DR   EMBL; BC067344; AAH67344.1; -; mRNA.
DR   RefSeq; NP_957035.2; NM_200741.1.
DR   AlphaFoldDB; Q6NWZ9; -.
DR   SMR; Q6NWZ9; -.
DR   STRING; 7955.ENSDARP00000137807; -.
DR   DNASU; 393714; -.
DR   GeneID; 393714; -.
DR   KEGG; dre:393714; -.
DR   AGR; ZFIN:ZDB-GENE-040426-1704; -.
DR   CTD; 1036; -.
DR   ZFIN; ZDB-GENE-040426-1704; cdo1.
DR   InParanoid; Q6NWZ9; -.
DR   OMA; MLLCWGE; -.
DR   OrthoDB; 314969at2759; -.
DR   PhylomeDB; Q6NWZ9; -.
DR   UniPathway; UPA00012; UER00537.
DR   PRO; PR:Q6NWZ9; -.
DR   Proteomes; UP000000437; Unplaced.
DR   Bgee; ENSDARG00000099389; Expressed in liver and 25 other cell types or tissues.
DR   GO; GO:0017172; F:cysteine dioxygenase activity; ISS:UniProtKB.
DR   GO; GO:0008198; F:ferrous iron binding; ISS:UniProtKB.
DR   GO; GO:0016151; F:nickel cation binding; ISS:UniProtKB.
DR   GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
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   2: Evidence at transcript level;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW   Thioether bond.
FT   CHAIN           1..201
FT                   /note="Cysteine dioxygenase type 1"
FT                   /id="PRO_0000206610"
FT   BINDING         86
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q16878"
FT   BINDING         88
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q16878"
FT   BINDING         141
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q16878"
FT   CROSSLNK        93..158
FT                   /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT                   /evidence="ECO:0000250|UniProtKB:Q16878"
SQ   SEQUENCE   201 AA;  23474 MW;  443CF9938F2752A7 CRC64;
     MEQTEVMKPE TLEDLIKTLH QIFQSDSINV EEVQNLMESY QSNPQDWMKF AKFDQYRYTR
     NLVDEGNGKF NLMILCWGEG HGSSIHDHTD SHCFLKLLQG QLKETLFDWP DRKLQSGMKP
     RGQSVLQENQ CAYINDSLGL HRVENVSHTE PAVSLHLYSP PFQSCRTFDQ RTGHHNTVKM
     TFWSKYGERT PYELSVSQEN N
//