ID   CDO1_PONAB              Reviewed;         200 AA.
AC   Q5RBQ7;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   03-AUG-2022, entry version 90.
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   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Liver;
RG   The German cDNA consortium;
RL   Submitted (NOV-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-157 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; CR858581; CAH90803.1; -; mRNA.
DR   RefSeq; NP_001127336.1; NM_001133864.1.
DR   AlphaFoldDB; Q5RBQ7; -.
DR   SMR; Q5RBQ7; -.
DR   STRING; 9601.ENSPPYP00000017558; -.
DR   Ensembl; ENSPPYT00000018267; ENSPPYP00000017558; ENSPPYG00000015698.
DR   GeneID; 100174398; -.
DR   KEGG; pon:100174398; -.
DR   CTD; 1036; -.
DR   eggNOG; KOG4064; Eukaryota.
DR   GeneTree; ENSGT00390000018226; -.
DR   HOGENOM; CLU_079443_1_0_1; -.
DR   InParanoid; Q5RBQ7; -.
DR   OMA; WPDRKSH; -.
DR   OrthoDB; 1516232at2759; -.
DR   TreeFam; TF105636; -.
DR   UniPathway; UPA00012; UER00537.
DR   Proteomes; UP000001595; Chromosome 5.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
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:0042412; P:taurine biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 2.60.120.10; -; 1.
DR   InterPro; IPR010300; CDO_1.
DR   InterPro; IPR014710; RmlC-like_jellyroll.
DR   InterPro; IPR011051; RmlC_Cupin_sf.
DR   PANTHER; PTHR12918; PTHR12918; 1.
DR   Pfam; PF05995; CDO_I; 1.
DR   SUPFAM; SSF51182; SSF51182; 1.
PE   2: Evidence at transcript level;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW   Thioether bond.
FT   CHAIN           1..200
FT                   /note="Cysteine dioxygenase type 1"
FT                   /id="PRO_0000206608"
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         140
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q16878"
FT   CROSSLNK        93..157
FT                   /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT                   /evidence="ECO:0000250|UniProtKB:Q16878"
SQ   SEQUENCE   200 AA;  22972 MW;  E4EF87221D05C14D CRC64;
     MEQTEVLKPR TLADLIRILH QLFAGDEVNV EEVQAIMEAY ESDPTEWAMY AKFDQYRYTR
     NLVDQGNGKF NLMILCWGEG HGSSIHDHTN SHCFLKMLQG NLKETLFAWP DKKSNEMVKK
     SERVLRENQC AYINDSIGLH RVENISHTEP AVSLHLYSPP FDTCHAFDQR TGHKNKVTMT
     FHSKFGIRTP NATSGSLENN