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Protein

Cysteine dioxygenase

Gene

CDO1

Organism
Ajellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432) (Darling's disease fungus) (Histoplasma capsulatum)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

L-cysteine + O2 = 3-sulfinoalanine.

Cofactori

Fe cationBy similarityNote: Binds 1 Fe cation per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi100 – 1001Iron; catalyticBy similarity
Metal bindingi102 – 1021Iron; catalyticBy similarity
Metal bindingi160 – 1601Iron; catalyticBy similarity

GO - Molecular functioni

  1. cysteine dioxygenase activity Source: UniProtKB-EC
  2. iron ion binding Source: InterPro

GO - Biological processi

  1. L-cysteine metabolic process Source: InterPro
  2. taurine biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Dioxygenase, Oxidoreductase

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00012; UER00537.

Names & Taxonomyi

Protein namesi
Recommended name:
Cysteine dioxygenase (EC:1.13.11.20)
Short name:
CDO
Gene namesi
Name:CDO1
ORF Names:HCBG_06968
OrganismiAjellomyces capsulatus (strain G186AR / H82 / ATCC MYA-2454 / RMSCC 2432) (Darling's disease fungus) (Histoplasma capsulatum)
Taxonomic identifieri447093 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeOnygenalesAjellomycetaceaeHistoplasma
ProteomesiUP000001631: Unassembled WGS sequence

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 213213Cysteine dioxygenasePRO_0000206614Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki107 ↔ 1773'-(S-cysteinyl)-tyrosine (Cys-Tyr)By similarity

Post-translational modificationi

The thioether cross-link between Cys-107 and Tyr-177 plays a structural role through stabilizing the Fe2+ ion, and prevents the production of highly damaging free hydroxyl radicals by holding the oxygen radical via hydroxyl hydrogen.By similarity

Keywords - PTMi

Thioether bond

Structurei

3D structure databases

ProteinModelPortaliQ5RLY7.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the cysteine dioxygenase family.Curated

Phylogenomic databases

InParanoidiQ5RLY7.
OrthoDBiEOG7Q5HQR.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR010300. Cys_dOase_I.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF05995. CDO_I. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.

Sequencei

Sequence statusi: Complete.

Q5RLY7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPYLENSESS PDPTPLDAFH CLVQDINKVL GPSSGLDSDD VDPMDIQKLM
60 70 80 90 100
EDYTSNESEW ERYAFGDAGR AYTRNLVDEG NGKCNLLILV WSPGKGSAIH
110 120 130 140 150
DHANAHCVMK VLKGSLRETL YGWPESDKVQ KGEPSPLTVT RDKVYKEGQV
160 170 180 190 200
TYMSDKLGLH KISNPDPTNF AISLHLYTPP NAAHYGFSLF DEKTGKSRHV
210
KQSVLFSRKG HKL
Length:213
Mass (Da):23,768
Last modified:June 16, 2009 - v2
Checksum:i62C0639517F657FB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti146 – 1461K → E in AAV66535 (Ref. 1) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY804144 mRNA. Translation: AAV66535.1.
GG663372 Genomic DNA. Translation: EEH05017.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY804144 mRNA. Translation: AAV66535.1.
GG663372 Genomic DNA. Translation: EEH05017.1.

3D structure databases

ProteinModelPortaliQ5RLY7.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

InParanoidiQ5RLY7.
OrthoDBiEOG7Q5HQR.

Enzyme and pathway databases

UniPathwayiUPA00012; UER00537.

Family and domain databases

Gene3Di2.60.120.10. 1 hit.
InterProiIPR010300. Cys_dOase_I.
IPR014710. RmlC-like_jellyroll.
IPR011051. RmlC_Cupin.
[Graphical view]
PfamiPF05995. CDO_I. 1 hit.
[Graphical view]
SUPFAMiSSF51182. SSF51182. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation and characterization of the cysteine dioxygenase gene (CDO1) from the dimorphic pathogenic fungus Histoplasma capsulatum."
    Hasler S., Shearer G. Jr.
    Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: G186AR / H82 / ATCC MYA-2454 / RMSCC 2432.

Entry informationi

Entry nameiCDO_AJECG
AccessioniPrimary (citable) accession number: Q5RLY7
Secondary accession number(s): C0NUD7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 27, 2005
Last sequence update: June 16, 2009
Last modified: February 4, 2015
This is version 53 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.