CDO_CAEBR
ID CDO_CAEBR Reviewed; 190 AA.
AC Q60TI7; A8XXT1;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Cysteine dioxygenase;
DE Short=CDO;
DE EC=1.13.11.20;
GN Name=cdo-1; ORFNames=CBG20456;
OS Caenorhabditis briggsae.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF16;
RX PubMed=14624247; DOI=10.1371/journal.pbio.0000045;
RA Stein L.D., Bao Z., Blasiar D., Blumenthal T., Brent M.R., Chen N.,
RA Chinwalla A., Clarke L., Clee C., Coghlan A., Coulson A., D'Eustachio P.,
RA Fitch D.H.A., Fulton L.A., Fulton R.E., Griffiths-Jones S., Harris T.W.,
RA Hillier L.W., Kamath R., Kuwabara P.E., Mardis E.R., Marra M.A.,
RA Miner T.L., Minx P., Mullikin J.C., Plumb R.W., Rogers J., Schein J.E.,
RA Sohrmann M., Spieth J., Stajich J.E., Wei C., Willey D., Wilson R.K.,
RA Durbin R.M., Waterston R.H.;
RT "The genome sequence of Caenorhabditis briggsae: a platform for comparative
RT genomics.";
RL PLoS Biol. 1:166-192(2003).
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; HE601085; CAP37450.3; -; Genomic_DNA.
DR RefSeq; XP_002632069.1; XM_002632023.1.
DR AlphaFoldDB; Q60TI7; -.
DR SMR; Q60TI7; -.
DR STRING; 6238.CBG20456; -.
DR PRIDE; Q60TI7; -.
DR EnsemblMetazoa; CBG20456.1; CBG20456.1; WBGene00039434.
DR GeneID; 8574068; -.
DR KEGG; cbr:CBG_20456; -.
DR CTD; 8574068; -.
DR WormBase; CBG20456; CBP11524; WBGene00039434; Cbr-cdo-1.
DR eggNOG; KOG4064; Eukaryota.
DR HOGENOM; CLU_079443_4_1_1; -.
DR InParanoid; Q60TI7; -.
DR OMA; WPDRKSH; -.
DR OrthoDB; 1516232at2759; -.
DR UniPathway; UPA00012; UER00537.
DR Proteomes; UP000008549; Chromosome II.
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"
FT /id="PRO_0000206611"
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; 21962 MW; 85AC945875B513F7 CRC64;
MVSFVQLVVQ IREIFEHKMV DVDEVMKLMG SYKSDINEWR RFAIFDMNKY TRNLVDIGNG
KYNLMILCWG PGMASSVHDH TDAHCFVKIL DGELTETKYD WPKKKHTPLE TIENKTYGLN
GVSYMNDELG LHRMENQSHS NGAVSLHLYI PPYSTCNAFD ERTGKKTKCT VTFYSKYGEK
IDYHGSKEGK