ID A0A2Y9L639_ENHLU Unreviewed; 200 AA.
AC A0A2Y9L639;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Cysteine dioxygenase {ECO:0000256|RuleBase:RU366010};
DE EC=1.13.11.20 {ECO:0000256|RuleBase:RU366010};
GN Name=LOC111158895 {ECO:0000313|RefSeq:XP_022376904.1,
GN ECO:0000313|RefSeq:XP_022376905.1};
OS Enhydra lutris kenyoni (northern sea otter).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Musteloidea; Mustelidae;
OC Lutrinae; Enhydra.
OX NCBI_TaxID=391180 {ECO:0000313|Proteomes:UP000248482, ECO:0000313|RefSeq:XP_022376905.1};
RN [1] {ECO:0000313|RefSeq:XP_022376904.1, ECO:0000313|RefSeq:XP_022376905.1}
RP IDENTIFICATION.
RC TISSUE=Blood {ECO:0000313|RefSeq:XP_022376904.1,
RC ECO:0000313|RefSeq:XP_022376905.1};
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the oxidation of cysteine to cysteine sulfinic acid
CC with addition of molecular dioxygen. {ECO:0000256|ARBA:ARBA00033725}.
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|ARBA:ARBA00024284};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20442;
CC Evidence={ECO:0000256|ARBA:ARBA00024284};
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 -!- COFACTOR:
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000256|ARBA:ARBA00001967};
CC -!- PATHWAY: Organosulfur biosynthesis; taurine biosynthesis; hypotaurine
CC from L-cysteine: step 1/2. {ECO:0000256|ARBA:ARBA00004759,
CC ECO:0000256|RuleBase:RU366010}.
CC -!- SIMILARITY: Belongs to the cysteine dioxygenase family.
CC {ECO:0000256|ARBA:ARBA00006622, ECO:0000256|RuleBase:RU366010}.
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DR RefSeq; XP_022376904.1; XM_022521196.1.
DR RefSeq; XP_022376905.1; XM_022521197.1.
DR KEGG; elk:111158895; -.
DR UniPathway; UPA00012; UER00537.
DR Proteomes; UP000248482; Unplaced.
DR GO; GO:0017172; F:cysteine dioxygenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0042412; P:taurine biosynthetic process; 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:UP000248482};
KW Thioether bond {ECO:0000256|ARBA:ARBA00022784,
KW ECO:0000256|PIRSR:PIRSR610300-50}.
FT BINDING 86
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT BINDING 88
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT BINDING 140
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-51"
FT CROSSLNK 93..157
FT /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT /evidence="ECO:0000256|PIRSR:PIRSR610300-50"
SQ SEQUENCE 200 AA; 22989 MW; 58667E13E1E55609 CRC64;
MEQTEVLKPR SLEDLIRLLH QLFAGEEVNV EEVQAVMEAY ESDPAEWAAY AKFDQYRYTR
NLVDEGNGKF NLMILCWGEG HGSSIHDHTD SHCFLKMLQG NLKETLFAWP DKKSNEMIKK
SERILRENQC AYINDSIGLH RVENISHTEP AVSLHLYSPP FDTCHAFDQR TGHKNKVTMT
FHSKFGIRTP FTASGSLENN
//
