ID   A0A436ZP72_9PEZI        Unreviewed;       227 AA.
AC   A0A436ZP72;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Cysteine dioxygenase {ECO:0000256|ARBA:ARBA00013133, ECO:0000256|RuleBase:RU366010};
DE            EC=1.13.11.20 {ECO:0000256|ARBA:ARBA00013133, ECO:0000256|RuleBase:RU366010};
GN   ORFNames=DFL_008496 {ECO:0000313|EMBL:RVD80602.1};
OS   Arthrobotrys flagrans.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Orbiliomycetes;
OC   Orbiliales; Orbiliaceae; Arthrobotrys.
OX   NCBI_TaxID=97331 {ECO:0000313|EMBL:RVD80602.1, ECO:0000313|Proteomes:UP000283090};
RN   [1] {ECO:0000313|EMBL:RVD80602.1, ECO:0000313|Proteomes:UP000283090}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS H-5679 {ECO:0000313|EMBL:RVD80602.1,
RC   ECO:0000313|Proteomes:UP000283090};
RA   Youssar L., Wernet V., Hensel N., Hildebrandt H.-G., Fischer R.;
RT   "Intercellular communication is required for trap formation in the
RT   nematode-trapping fungus Duddingtonia flagrans.";
RL   Submitted (JAN-2019) 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         Evidence={ECO:0000256|RuleBase:RU366010};
CC   -!- COFACTOR:
CC       Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC         Evidence={ECO:0000256|RuleBase:RU366010};
CC       Note=Binds 1 Fe cation per subunit. {ECO:0000256|RuleBase:RU366010};
CC   -!- SIMILARITY: Belongs to the cysteine dioxygenase family.
CC       {ECO:0000256|ARBA:ARBA00006622, ECO:0000256|RuleBase:RU366010}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RVD80602.1}.
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DR   EMBL; SAEB01000012; RVD80602.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A436ZP72; -.
DR   STRING; 97331.A0A436ZP72; -.
DR   VEuPathDB; FungiDB:DFL_008496; -.
DR   Proteomes; UP000283090; Unassembled WGS sequence.
DR   GO; GO:0017172; F:cysteine dioxygenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
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 {ECO:0000256|ARBA:ARBA00022964, ECO:0000256|RuleBase:RU366010};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR610300-51};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR610300-51};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU366010};
KW   Reference proteome {ECO:0000313|Proteomes:UP000283090};
KW   Thioether bond {ECO:0000256|PIRSR:PIRSR610300-50}.
FT   BINDING         113
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT   BINDING         115
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT   BINDING         168
FT                   /ligand="Fe cation"
FT                   /ligand_id="ChEBI:CHEBI:24875"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT   CROSSLNK        120..185
FT                   /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR610300-50"
SQ   SEQUENCE   227 AA;  26026 MW;  A304B73AC121653B CRC64;
     MSPIAVQSPQ AVAEFQSHQH QDLSLVQRRS NFDILISSIR DTLGTNPELK FDDVDVDKLQ
     MLLRAYQSSR PEWERFSFID FSRNYTRNLV DNLHGNANLI LMTWTPNKAS LIHDHTSAHC
     VMRILQGHII ETRYEWPTPG VEEPLKVKQV RHYYAGDVAY MSDDLGIHKV ENGDPDSVAV
     SLHLYTPPYI EKRGCNTFNA KTGKSCHIKL SEYYSRKGEK ISKPSSH
//