ID   CDO_ARTBE               Reviewed;         219 AA.
AC   D1MF76;
DT   04-MAR-2015, integrated into UniProtKB/Swiss-Prot.
DT   19-JAN-2010, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Cysteine dioxygenase {ECO:0000303|PubMed:21039937};
DE            Short=CDO {ECO:0000303|PubMed:21039937};
DE            EC=1.13.11.20 {ECO:0000269|PubMed:21039937};
GN   Name=CDO1 {ECO:0000250|UniProtKB:D4AN26};
OS   Arthroderma benhamiae (Trichophyton mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=63400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC
RP   ACTIVITY, AND FUNCTION.
RC   STRAIN=TM-10;
RX   PubMed=21039937; DOI=10.1111/j.1439-0507.2010.01948.x;
RA   Kasperova A., Kunert J., Horynova M., Weigl E., Sebela M., Lenobel R.,
RA   Raska M.;
RT   "Isolation of recombinant cysteine dioxygenase protein from Trichophyton
RT   mentagrophytes.";
RL   Mycoses 54:E456-E462(2011).
CC   -!- FUNCTION: Cysteine dioxygenase involved in sulfite formation from
CC       cysteine. Required for keratin degradation and plays an important role
CC       in filamentous growth and virulence. {ECO:0000269|PubMed:21039937}.
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:0000269|PubMed:21039937};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000250|UniProtKB:Q16878};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000250|UniProtKB:Q16878};
CC   -!- PTM: The thioether cross-link between Cys-113 and Tyr-183 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; GU139238; ACZ26339.1; -; mRNA.
DR   AlphaFoldDB; D1MF76; -.
DR   SMR; D1MF76; -.
DR   GO; GO:0017172; F:cysteine dioxygenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
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   1: Evidence at protein level;
KW   Dioxygenase; Iron; Metal-binding; Oxidoreductase; Thioether bond;
KW   Virulence.
FT   CHAIN           1..219
FT                   /note="Cysteine dioxygenase"
FT                   /id="PRO_0000432124"
FT   BINDING         106
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q16878"
FT   BINDING         108
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q16878"
FT   BINDING         166
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250|UniProtKB:Q16878"
FT   CROSSLNK        113..183
FT                   /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT                   /evidence="ECO:0000250|UniProtKB:Q16878"
SQ   SEQUENCE   219 AA;  24535 MW;  934E92BFB8F5196C CRC64;
     MPFIENQTTT AEPIVPVDVK GKDAFHKLVD DLSAVLGPSS GLDSDDVDPM DIQKLMEGYV
     SNHEEWQRYA LADESRAYTR NLVDEGNGKS NLLVLVWNPG KSSPIHDHAN AHCVMKILHG
     SLKEHRYDWP EQDKINNGEA CPLTVTKETI LRENEVAYMS DKLGLHKISN PDPNDFAISL
     HLYTPPNAAH FGCSLFDEKT GKSHHIKQCT FFSNRGLKL