ID   CDO_SCHJA               Reviewed;         212 AA.
AC   Q9U8F1;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   22-FEB-2023, entry version 76.
DE   RecName: Full=Cysteine dioxygenase;
DE            Short=CDO;
DE            EC=1.13.11.20;
GN   Name=CDO;
OS   Schistosoma japonicum (Blood fluke).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes; Trematoda;
OC   Digenea; Strigeidida; Schistosomatoidea; Schistosomatidae; Schistosoma.
OX   NCBI_TaxID=6182;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Philippines;
RA   Fan J., Brindley P.J.;
RT   "Cloning and expression in Escherichia coli of a cysteine dioxygenase from
RT   Schistosoma japonicum.";
RL   Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
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-102 and Tyr-178 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; AF091540; AAD52701.1; -; mRNA.
DR   AlphaFoldDB; Q9U8F1; -.
DR   SMR; Q9U8F1; -.
DR   UniPathway; UPA00012; UER00537.
DR   GO; GO:0017172; F:cysteine dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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; Thioether bond.
FT   CHAIN           1..212
FT                   /note="Cysteine dioxygenase"
FT                   /id="PRO_0000206613"
FT   BINDING         95
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q16878"
FT   BINDING         97
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q16878"
FT   BINDING         161
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q16878"
FT   CROSSLNK        102..178
FT                   /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT                   /evidence="ECO:0000250|UniProtKB:Q16878"
SQ   SEQUENCE   212 AA;  25035 MW;  39BE01713721F46C CRC64;
     MSMYTHQSNN ELIPLKTVST LNDLIKTIRI IFNQKEINVN EIHKILNDFQ CDFTEWQKYI
     YFNKTHYTRN LIDEGNGRYN LFLLCWSEDQ GTRIHDHSGA HCFVKLIKGC IKETIFEWPK
     YFTVEKSNYS INQIDLPLTV KSVSEMRPGD VTYMHDKIGI HRLHNPSTTE TAITLHLYFP
     PYTNSMIFEE STSRMKKMDV TFHSKFGKQI PQ
//