CDO1_BOVIN
ID CDO1_BOVIN Reviewed; 200 AA.
AC Q3SZU4;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 88.
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 Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) 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}.
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DR EMBL; BT025474; ABF57430.1; -; mRNA.
DR EMBL; BC102709; AAI02710.1; -; mRNA.
DR RefSeq; NP_001029637.1; NM_001034465.2.
DR AlphaFoldDB; Q3SZU4; -.
DR SMR; Q3SZU4; -.
DR STRING; 9913.ENSBTAP00000023186; -.
DR PaxDb; Q3SZU4; -.
DR PRIDE; Q3SZU4; -.
DR GeneID; 514462; -.
DR KEGG; bta:514462; -.
DR CTD; 1036; -.
DR eggNOG; KOG4064; Eukaryota.
DR InParanoid; Q3SZU4; -.
DR OrthoDB; 1516232at2759; -.
DR UniPathway; UPA00012; UER00537.
DR Proteomes; UP000009136; Unplaced.
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:0016702; F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB.
DR GO; GO:0019448; P:L-cysteine catabolic process; IBA:GO_Central.
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_0000246081"
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; 23013 MW; 65796B06507CF936 CRC64;
MERTEVLKPR TLADLIRVLH QLFAGEEINV EEVQAVMEAY ESNPAEWAVY AKFDQYRYTR
NLVDQGNGKF NLMILCWGEG HGSSIHDHTD SHCFLKMLQG NLKETLFAWP DKKSNEMIKK
SERILRENQC AYINDSIGLH RVENISHTEP AVSLHLYSPP FDTCHAFDQR TGHKNKVIMT
FHSKFGIKTP FTTSGSLENN
