CDO1_RAT
ID CDO1_RAT Reviewed; 200 AA.
AC P21816; Q6NS32;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Cysteine dioxygenase type 1;
DE EC=1.13.11.20 {ECO:0000269|PubMed:9824269};
DE AltName: Full=Cysteine dioxygenase type I;
DE Short=CDO;
DE Short=CDO-I;
GN Name=Cdo1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC TISSUE=Liver;
RX PubMed=2334417; DOI=10.1016/0006-291x(90)92345-z;
RA Hosokawa Y., Matsumoto A., Oka J., Itakura H., Yamaguchi K.;
RT "Isolation and characterization of a cDNA for rat liver cysteine
RT dioxygenase.";
RL Biochem. Biophys. Res. Commun. 168:473-478(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Liver;
RX PubMed=8973325; DOI=10.1016/s0378-1119(96)00496-9;
RA Tsuboyama N., Hosokawa Y., Totani M., Oka J., Matsumoto A., Koide T.,
RA Kodama H.;
RT "Structural organization and tissue-specific expression of the gene
RT encoding rat cysteine dioxygenase.";
RL Gene 181:161-165(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=9824269; DOI=10.1016/s0168-8278(98)80155-4;
RA Parsons R.B., Ramsden D.B., Waring R.H., Barber P.C., Williams A.C.;
RT "Hepatic localisation of rat cysteine dioxygenase.";
RL J. Hepatol. 29:595-602(1998).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH IRON, CROSS-LINK,
RP SUBUNIT, COFACTOR, PTM, AND IRON-BINDING SITES.
RX PubMed=16611640; DOI=10.1074/jbc.m601555200;
RA Simmons C.R., Liu Q., Huang Q., Hao Q., Begley T.P., Karplus P.A.,
RA Stipanuk M.H.;
RT "Crystal structure of mammalian cysteine dioxygenase. A novel mononuclear
RT iron center for cysteine thiol oxidation.";
RL J. Biol. Chem. 281:18723-18733(2006).
CC -!- FUNCTION: Catalyzes the oxidation of cysteine to cysteine sulfinic acid
CC with addition of molecular dioxygen. {ECO:0000269|PubMed:9824269}.
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:0000269|PubMed:9824269};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20442;
CC Evidence={ECO:0000269|PubMed:9824269};
CC -!- COFACTOR:
CC Name=Fe cation; Xref=ChEBI:CHEBI:24875;
CC Evidence={ECO:0000269|PubMed:16611640};
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 (PubMed:16611640). Ni(2+) and Zn(2+)
CC can be used to a lesser extent (By similarity).
CC {ECO:0000250|UniProtKB:P60334, ECO:0000269|PubMed:16611640};
CC -!- PATHWAY: Organosulfur biosynthesis; taurine biosynthesis; hypotaurine
CC from L-cysteine: step 1/2.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:16611640}.
CC -!- TISSUE SPECIFICITY: Highest levels in liver. Significant expression
CC also in kidney, lung and brain. {ECO:0000269|PubMed:8973325,
CC ECO:0000269|PubMed:9824269}.
CC -!- DEVELOPMENTAL STAGE: From neonate to weaning.
CC -!- INDUCTION: By increase of sulfur amino acid intake.
CC {ECO:0000269|PubMed:9824269}.
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:0000269|PubMed:16611640}.
CC -!- SIMILARITY: Belongs to the cysteine dioxygenase family. {ECO:0000305}.
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DR EMBL; M35266; AAA40904.1; -; mRNA.
DR EMBL; D83481; BAA11925.1; -; Genomic_DNA.
DR EMBL; BC070509; AAH70509.1; -; mRNA.
DR PIR; A34632; A34632.
DR RefSeq; NP_434696.1; NM_052809.1.
DR PDB; 2B5H; X-ray; 1.50 A; A=1-200.
DR PDB; 2GH2; X-ray; 1.50 A; A=1-200.
DR PDB; 3ELN; X-ray; 1.42 A; A=1-200.
DR PDB; 4IEO; X-ray; 1.55 A; A=1-200.
DR PDB; 4IEP; X-ray; 1.45 A; A=1-200.
DR PDB; 4IEQ; X-ray; 1.40 A; A=1-200.
DR PDB; 4IER; X-ray; 1.45 A; A=1-200.
DR PDB; 4IES; X-ray; 1.40 A; A=1-200.
DR PDB; 4IET; X-ray; 1.40 A; A=1-200.
DR PDB; 4IEU; X-ray; 1.25 A; A=1-200.
DR PDB; 4IEV; X-ray; 1.60 A; A=1-200.
DR PDB; 4IEW; X-ray; 1.45 A; A=1-200.
DR PDB; 4IEX; X-ray; 2.15 A; A=1-200.
DR PDB; 4IEY; X-ray; 1.63 A; A=1-200.
DR PDB; 4IEZ; X-ray; 1.39 A; A=1-200.
DR PDB; 4JTN; X-ray; 1.59 A; A=1-200.
DR PDB; 4JTO; X-ray; 2.00 A; A=1-200.
DR PDB; 4KWJ; X-ray; 1.75 A; A=1-200.
DR PDB; 4KWK; X-ray; 1.95 A; A=1-200.
DR PDB; 4KWL; X-ray; 1.63 A; A=1-200.
DR PDB; 4PIX; X-ray; 1.35 A; A=1-200.
DR PDB; 4PIY; X-ray; 1.60 A; A=1-200.
DR PDB; 4PIZ; X-ray; 1.40 A; A=1-200.
DR PDB; 4PJY; X-ray; 1.50 A; A=1-200.
DR PDB; 4UBG; X-ray; 1.90 A; A=1-200.
DR PDB; 4UBH; X-ray; 1.81 A; A=1-200.
DR PDB; 4XET; X-ray; 1.30 A; A=1-200.
DR PDB; 4XEZ; X-ray; 1.25 A; A=1-200.
DR PDB; 4XF0; X-ray; 1.40 A; A=1-200.
DR PDB; 4XF1; X-ray; 1.55 A; A=1-200.
DR PDB; 4XF3; X-ray; 1.55 A; A=1-200.
DR PDB; 4XF4; X-ray; 1.35 A; A=1-200.
DR PDB; 4XF9; X-ray; 1.30 A; A=1-200.
DR PDB; 4XFA; X-ray; 1.65 A; A=1-200.
DR PDB; 4XFB; X-ray; 1.35 A; A=1-200.
DR PDB; 4XFC; X-ray; 1.35 A; A=1-200.
DR PDB; 4XFF; X-ray; 1.25 A; A=1-200.
DR PDB; 4XFG; X-ray; 1.40 A; A=1-200.
DR PDB; 4XFH; X-ray; 1.35 A; A=1-200.
DR PDB; 4XFI; X-ray; 1.40 A; A=1-200.
DR PDB; 4YNI; X-ray; 2.40 A; A=1-200.
DR PDB; 4YSF; X-ray; 1.94 A; A=1-200.
DR PDB; 4YYO; X-ray; 1.77 A; A=1-200.
DR PDB; 4Z82; X-ray; 1.70 A; A=1-200.
DR PDB; 5EFU; X-ray; 2.80 A; A=1-200.
DR PDB; 5EZW; X-ray; 1.65 A; A=1-200.
DR PDB; 5FDB; X-ray; 1.75 A; A=1-200.
DR PDB; 5I0R; X-ray; 1.35 A; A=1-200.
DR PDB; 5I0S; X-ray; 1.30 A; A=1-200.
DR PDB; 5I0T; X-ray; 1.37 A; A=1-200.
DR PDB; 5I0U; X-ray; 1.25 A; A=1-200.
DR PDB; 6U1M; X-ray; 1.61 A; A=1-200.
DR PDB; 6U4L; X-ray; 1.91 A; A=1-200.
DR PDB; 6U4S; X-ray; 2.49 A; A=1-200.
DR PDB; 6U4V; X-ray; 2.30 A; A=1-200.
DR PDBsum; 2B5H; -.
DR PDBsum; 2GH2; -.
DR PDBsum; 3ELN; -.
DR PDBsum; 4IEO; -.
DR PDBsum; 4IEP; -.
DR PDBsum; 4IEQ; -.
DR PDBsum; 4IER; -.
DR PDBsum; 4IES; -.
DR PDBsum; 4IET; -.
DR PDBsum; 4IEU; -.
DR PDBsum; 4IEV; -.
DR PDBsum; 4IEW; -.
DR PDBsum; 4IEX; -.
DR PDBsum; 4IEY; -.
DR PDBsum; 4IEZ; -.
DR PDBsum; 4JTN; -.
DR PDBsum; 4JTO; -.
DR PDBsum; 4KWJ; -.
DR PDBsum; 4KWK; -.
DR PDBsum; 4KWL; -.
DR PDBsum; 4PIX; -.
DR PDBsum; 4PIY; -.
DR PDBsum; 4PIZ; -.
DR PDBsum; 4PJY; -.
DR PDBsum; 4UBG; -.
DR PDBsum; 4UBH; -.
DR PDBsum; 4XET; -.
DR PDBsum; 4XEZ; -.
DR PDBsum; 4XF0; -.
DR PDBsum; 4XF1; -.
DR PDBsum; 4XF3; -.
DR PDBsum; 4XF4; -.
DR PDBsum; 4XF9; -.
DR PDBsum; 4XFA; -.
DR PDBsum; 4XFB; -.
DR PDBsum; 4XFC; -.
DR PDBsum; 4XFF; -.
DR PDBsum; 4XFG; -.
DR PDBsum; 4XFH; -.
DR PDBsum; 4XFI; -.
DR PDBsum; 4YNI; -.
DR PDBsum; 4YSF; -.
DR PDBsum; 4YYO; -.
DR PDBsum; 4Z82; -.
DR PDBsum; 5EFU; -.
DR PDBsum; 5EZW; -.
DR PDBsum; 5FDB; -.
DR PDBsum; 5I0R; -.
DR PDBsum; 5I0S; -.
DR PDBsum; 5I0T; -.
DR PDBsum; 5I0U; -.
DR PDBsum; 6U1M; -.
DR PDBsum; 6U4L; -.
DR PDBsum; 6U4S; -.
DR PDBsum; 6U4V; -.
DR AlphaFoldDB; P21816; -.
DR SMR; P21816; -.
DR IntAct; P21816; 13.
DR STRING; 10116.ENSRNOP00000000172; -.
DR jPOST; P21816; -.
DR PaxDb; P21816; -.
DR PRIDE; P21816; -.
DR DNASU; 81718; -.
DR Ensembl; ENSRNOT00000000172; ENSRNOP00000000172; ENSRNOG00000000158.
DR GeneID; 81718; -.
DR KEGG; rno:81718; -.
DR UCSC; RGD:69262; rat.
DR CTD; 1036; -.
DR RGD; 69262; Cdo1.
DR eggNOG; KOG4064; Eukaryota.
DR GeneTree; ENSGT00390000018226; -.
DR HOGENOM; CLU_079443_1_0_1; -.
DR InParanoid; P21816; -.
DR OMA; WPDRKSH; -.
DR OrthoDB; 1516232at2759; -.
DR PhylomeDB; P21816; -.
DR TreeFam; TF105636; -.
DR BioCyc; MetaCyc:MON-8844; -.
DR BRENDA; 1.13.11.20; 5301.
DR Reactome; R-RNO-1614558; Degradation of cysteine and homocysteine.
DR SABIO-RK; P21816; -.
DR UniPathway; UPA00012; UER00537.
DR EvolutionaryTrace; P21816; -.
DR PRO; PR:P21816; -.
DR Proteomes; UP000002494; Chromosome 18.
DR Bgee; ENSRNOG00000000158; Expressed in liver and 20 other tissues.
DR Genevisible; P21816; RN.
DR GO; GO:0005829; C:cytosol; ISO:RGD.
DR GO; GO:0017172; F:cysteine dioxygenase activity; IDA:UniProtKB.
DR GO; GO:0008198; F:ferrous iron binding; IDA:RGD.
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; ISO:RGD.
DR GO; GO:0006534; P:cysteine metabolic process; TAS:RGD.
DR GO; GO:0019448; P:L-cysteine catabolic process; IDA:RGD.
DR GO; GO:0046439; P:L-cysteine metabolic process; NAS:RGD.
DR GO; GO:0007595; P:lactation; IDA:RGD.
DR GO; GO:0043200; P:response to amino acid; IDA:RGD.
DR GO; GO:0051591; P:response to cAMP; IDA:RGD.
DR GO; GO:0045471; P:response to ethanol; IDA:RGD.
DR GO; GO:0033762; P:response to glucagon; IDA:RGD.
DR GO; GO:0051384; P:response to glucocorticoid; IDA:RGD.
DR GO; GO:0010243; P:response to organonitrogen compound; IDA:RGD.
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 1: Evidence at protein level;
KW 3D-structure; Dioxygenase; Direct protein sequencing; Iron; Metal-binding;
KW Oxidoreductase; Reference proteome; Thioether bond.
FT CHAIN 1..200
FT /note="Cysteine dioxygenase type 1"
FT /id="PRO_0000206609"
FT BINDING 86
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16611640"
FT BINDING 88
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16611640"
FT BINDING 140
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000269|PubMed:16611640"
FT CROSSLNK 93..157
FT /note="3'-(S-cysteinyl)-tyrosine (Cys-Tyr)"
FT /evidence="ECO:0000269|PubMed:16611640"
FT CONFLICT 89
FT /note="T -> S (in Ref. 3; AAH70509)"
FT /evidence="ECO:0000305"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:4XEZ"
FT STRAND 24..27
FT /evidence="ECO:0007829|PDB:4XEZ"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:4XEZ"
FT HELIX 44..47
FT /evidence="ECO:0007829|PDB:4XEZ"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:4XEZ"
FT STRAND 55..57
FT /evidence="ECO:0007829|PDB:4XEZ"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:4XEZ"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:4XFF"
FT STRAND 71..77
FT /evidence="ECO:0007829|PDB:4XEZ"
FT STRAND 92..100
FT /evidence="ECO:0007829|PDB:4XEZ"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:4XEZ"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:6U1M"
FT STRAND 121..125
FT /evidence="ECO:0007829|PDB:4XEZ"
FT STRAND 130..133
FT /evidence="ECO:0007829|PDB:4XEZ"
FT TURN 135..137
FT /evidence="ECO:0007829|PDB:4XEZ"
FT STRAND 139..143
FT /evidence="ECO:0007829|PDB:4XEZ"
FT STRAND 151..159
FT /evidence="ECO:0007829|PDB:4XEZ"
FT STRAND 162..167
FT /evidence="ECO:0007829|PDB:4XEZ"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:4XEZ"
FT STRAND 174..178
FT /evidence="ECO:0007829|PDB:4XEZ"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:4XEZ"
SQ SEQUENCE 200 AA; 23026 MW; 118F1A3326B340F9 CRC64;
MERTELLKPR TLADLIRILH ELFAGDEVNV EEVQAVLEAY ESNPAEWALY AKFDQYRYTR
NLVDQGNGKF NLMILCWGEG HGSSIHDHTD SHCFLKLLQG NLKETLFDWP DKKSNEMIKK
SERTLRENQC AYINDSIGLH RVENVSHTEP AVSLHLYSPP FDTCHAFDQR TGHKNKVTMT
FHSKFGIRTP FTTSGSLENN
