CDO1_CAEEL
ID CDO1_CAEEL Reviewed; 190 AA.
AC Q20893;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Cysteine dioxygenase 1;
DE Short=CDO;
DE EC=1.13.11.20;
GN Name=cdo-1; ORFNames=F56F10.3;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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-85 and Tyr-149 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; FO081336; CCD70867.1; -; Genomic_DNA.
DR PIR; T16488; T16488.
DR RefSeq; NP_508168.1; NM_075767.3.
DR AlphaFoldDB; Q20893; -.
DR SMR; Q20893; -.
DR BioGRID; 45387; 5.
DR STRING; 6239.F56F10.3; -.
DR EPD; Q20893; -.
DR PaxDb; Q20893; -.
DR PeptideAtlas; Q20893; -.
DR EnsemblMetazoa; F56F10.3.1; F56F10.3.1; WBGene00018986.
DR GeneID; 180434; -.
DR KEGG; cel:CELE_F56F10.3; -.
DR UCSC; F56F10.3; c. elegans.
DR CTD; 180434; -.
DR WormBase; F56F10.3; CE28465; WBGene00018986; cdo-1.
DR eggNOG; KOG4064; Eukaryota.
DR GeneTree; ENSGT00390000018226; -.
DR HOGENOM; CLU_079443_4_1_1; -.
DR InParanoid; Q20893; -.
DR OMA; WPDRKSH; -.
DR OrthoDB; 1516232at2759; -.
DR PhylomeDB; Q20893; -.
DR Reactome; R-CEL-1614558; Degradation of cysteine and homocysteine.
DR UniPathway; UPA00012; UER00537.
DR PRO; PR:Q20893; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00018986; Expressed in larva and 4 other tissues.
DR GO; GO:0017172; F:cysteine dioxygenase activity; IBA:GO_Central.
DR GO; GO:0008198; F:ferrous iron binding; IBA:GO_Central.
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: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 3: Inferred from homology;
KW Dioxygenase; Iron; Metal-binding; Oxidoreductase; Reference proteome;
KW Thioether bond.
FT CHAIN 1..190
FT /note="Cysteine dioxygenase 1"
FT /id="PRO_0000206612"
FT BINDING 78
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q16878"
FT BINDING 80
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q16878"
FT BINDING 132
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250|UniProtKB:Q16878"
FT CROSSLNK 85..149
FT /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT /evidence="ECO:0000250|UniProtKB:Q16878"
SQ SEQUENCE 190 AA; 21879 MW; 273A194DBFFA0C55 CRC64;
MISFVQLVVQ IREIFQQKLI DVDEVMKLMA SYKSNANEWR RFAIFDMNKY TRNLVDVGNG
KYNLMILCWG PGMASSVHDH TDAHCFVKIL DGELTETKYA WPRKRHVPLD ISENKTYGMN
GVSYMNDELG LHRMENLSHS NGAVSLHLYI PPYSTCNAFD ERTGKKTQCT VTFYSKYGKK
VDYRGSKNGN