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Reviewed, UniProtKB/Swiss-Prot O13289 (CATA_CANAL)

Last modified January 19, 2010. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Peroxisomal catalase
    EC=1.11.1.6
Gene names
Name: CTA1
Synonyms: CAT1
ORF Names: CaO19.6229, CaO19.13609
OrganismCandida albicans (Yeast)
Taxonomic identifier5476 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

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Protein attributes

Sequence length487 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Required for hyphal growth. Ref.2

Catalytic activity

2 H2O2 = O2 + 2 H2O.

Cofactor

Heme group.

Subunit structure

Homotetramer By similarity.

Subcellular location

Peroxisome By similarity.

Sequence similarities

Belongs to the catalase family.

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Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentPeroxisome
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
Gene Ontology (GO)
   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperoxisome

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncatalase activity

Inferred from electronic annotation. Source: EC

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 487486Peroxisomal catalase
PRO_0000084918

Sites

Active site531 By similarity
Active site1261 By similarity
Metal binding3361Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict1141I → F in BAA21767. Ref.2
Sequence conflict1141I → F in EAK99824. Ref.3
Sequence conflict1141I → F in EAK99912. Ref.3
Sequence conflict2241N → T in BAA21767. Ref.2
Sequence conflict2241N → T in EAK99824. Ref.3
Sequence conflict2241N → T in EAK99912. Ref.3
Sequence conflict2841R → K in BAA21767. Ref.2
Sequence conflict2841R → K in EAK99824. Ref.3
Sequence conflict2841R → K in EAK99912. Ref.3
Sequence conflict2881M → L in BAA21767. Ref.2
Sequence conflict2881M → L in EAK99824. Ref.3
Sequence conflict2881M → L in EAK99912. Ref.3
Sequence conflict3011E → K in BAA21767. Ref.2
Sequence conflict3011E → K in EAK99824. Ref.3
Sequence conflict3011E → K in EAK99912. Ref.3
Sequence conflict3421Missing in BAA21767. Ref.2
Sequence conflict3421Missing in EAK99824. Ref.3
Sequence conflict3421Missing in EAK99912. Ref.3
Sequence conflict3671S → M in BAA21767. Ref.2
Sequence conflict3671S → M in EAK99824. Ref.3
Sequence conflict3671S → M in EAK99912. Ref.3
Sequence conflict398 – 3992SF → L in BAA21767. Ref.2
Sequence conflict398 – 3992SF → L in EAK99824. Ref.3
Sequence conflict398 – 3992SF → L in EAK99912. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
O13289-1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 16C1A0EA163C658C

FASTA48755,063
        10         20         30         40         50         60 
MAPTFTNSNG QPIPEPFATQ RVGQHGPLLL QDFNLIDSLA HFDRERIPER VVHAKGSGAY 

        70         80         90        100        110        120 
GVFEVTDDIT DICAAKFLDT VGKKTRIFTR FSTVGGELGS ADTARDPRGF ATKIYTEEGN 

       130        140        150        160        170        180 
LDLVYNNTPV FFIRDPSKFP HFIHTQKRNP ETHLKDANMF WDYLTSNEES IHQVMVLFSD 

       190        200        210        220        230        240 
RGTPASYREM NGYSGHTYKW SNKKGEWFYV QVHFISDQGI KTLNNEEAGA LAGSNPDYAQ 

       250        260        270        280        290        300 
EDLFKNIAAG NYPSWTAYIQ TMTEAEAKEA EFSVFDLTKV WPHRKYPMRR FGKFTLNENP 

       310        320        330        340        350        360 
ENYFAEVEQA AFSPAHTVPY MEPSADPVLQ SRLFSYADTH RPHRLGTNYT QIPVNCPVTG 

       370        380        390        400        410        420 
AVFNPHSRDG AMTVNGNLGS HPNYLASDKP VEFKQFSSFQ EDQEVWNGAA TPFHWKATPA 

       430        440        450        460        470        480 
DFKQAQELWK VLKRYPNQQE HLAHNIAVHA AGADAAIQDR VFAYFGKVSQ DLADAIKKEV 


LELSPRK

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References

« Hide 'large scale' references
[1]"Cloning and sequencing of a Candida albicans catalase gene and effects of disruption of this gene."
Wysong D.R., Christin L., Sugar A.M., Robbins P.W., Diamond R.D.
Infect. Immun. 66:1953-1961(1998) [PubMed: 9573075] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 10261 / CBS 2718 / IFO 1061.
[2]"Catalase gene disruptant of the human pathogenic yeast Candida albicans is defective in hyphal growth, and a catalase-specific inhibitor can suppress hyphal growth of wild-type cells."
Nakagawa Y.
Microbiol. Immunol. 52:16-24(2008) [PubMed: 18352908] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION.
Strain: FC18.
[3]"The diploid genome sequence of Candida albicans."
Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B., Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W., Scherer S.
Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004) [PubMed: 15123810] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: SC5314.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U40704 Genomic DNA. Translation: AAC39448.1.
AB006327 mRNA. Translation: BAA21767.1.
AB006328 Genomic DNA. Translation: BAA21768.1.
AACQ01000038 Genomic DNA. Translation: EAK99824.1.
AACQ01000037 Genomic DNA. Translation: EAK99912.1.
RefSeqXP_718734.1.
XP_718818.1.

3D structure databases

SMRO13289. Positions 6-478.
ModBaseSearch...

Genome annotation databases

GeneID3639495.
3639575.
KEGGcal:CaO19.13609.
cal:CaO19.6229.

Phylogenomic databases

OrthoDBEOG9QNPCB.

Enzyme and pathway databases

BRENDA1.11.1.6. 1124.

Family and domain databases

InterProIPR002226. Catalase.
IPR020835. Catalase-like_haem-dep.
IPR010582. Catalase-rel_immune_responsive.
IPR011614. Catalase_N.
IPR018028. Catalase_rel_subgroup.
[Graphical view]
Gene3DG3DSA:2.40.180.10. Catalase_N. 1 hit.
PANTHERPTHR11465. Catalase. 1 hit.
PfamPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PRINTSPR00067. CATALASE.
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameCATA_CANAL
AccessionPrimary (citable) accession number: O13289
Secondary accession number(s): O42616, Q5AAT2, Q9URJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: January 19, 2010
This is version 56 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

Candida albicans

Candida albicans: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents