[1]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=ATCC 26029 / G186A; Hasler S., Shearer G. Jr.; "Isolation and characterization of the cysteine dioxygenase gene (CDO1) from the dimorphic pathogenic fungus Histoplasma capsulatum."; Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.

Comments

CATALYTIC ACTIVITY: L-cysteine + O₂ = 3-sulfinoalanine.
COFACTOR: Binds 1 iron ion per subunit (By similarity).
PATHWAY: Organosulfur biosynthesis; taurine biosynthesis; hypotaurine from L-cysteine: step 1/2 .
PTM: The thioether cross-link between Cys-107 and Tyr-177 plays a structural role through stabilizing the ferrous ion, and prevents the production of highly damaging free hydroxyl radicals by holding the oxygen radical via hydroxyl hydrogen (By similarity).
SIMILARITY: Belongs to the cysteine dioxygenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AY804144; AAV66535.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

ModBase

Q5RLY7.

Ontologies

GO:0017172;	Molecular function: cysteine dioxygenase activity (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from InterPro).
GO:0046439;	Biological process: L-cysteine metabolic process (inferred from electronic annotation from InterPro).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR010300; Cys_dOase_I.
Graphical view of domain structure.

Pfam

PF05995; CDO_I; 1.
Pfam graphical view of domain structure.

ProtoNet

Q5RLY7.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Dioxygenase; Iron; Metal-binding; Oxidoreductase; Thioether bond.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 213`	`213`	`Cysteine dioxygenase.`	`PRO_0000206614`
`METAL`	`100 100`		`Iron; catalytic (By similarity).`
`METAL`	`102 102`		`Iron; catalytic (By similarity).`
`METAL`	`160 160`		`Iron; catalytic (By similarity).`
`CROSSLNK`	`107 177`		`3'-(S-cysteinyl)-tyrosine (Cys-Tyr) (By similarity).`

Sequence information

Length: 213 AA [This is the length of the unprocessed precursor]

Molecular weight: 23769 Da [This is the MW of the unprocessed precursor]

CRC64: 54C0639D3FD65FD3 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPYLENSESS PDPTPLDAFH CLVQDINKVL GPSSGLDSDD VDPMDIQKLM EDYTSNESEW 

        70         80         90        100        110        120 
ERYAFGDAGR AYTRNLVDEG NGKCNLLILV WSPGKGSAIH DHANAHCVMK VLKGSLRETL 

       130        140        150        160        170        180 
YGWPESDKVQ KGEPSPLTVT RDKVYEEGQV TYMSDKLGLH KISNPDPTNF AISLHLYTPP 

       190        200        210 
NAAHYGFSLF DEKTGKSRHV KQSVLFSRKG HKL

Q5RLY7 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools