Peroxisomal catalase - Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

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O13289 (CATA_CANAL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 72. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Peroxisomal catalase
EC=1.11.1.6

Gene names

Name:	CTA1
Synonyms:	CAT1
ORF Names:	CaO19.6229, CaO19.13609

Organism

Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)

Taxonomic identifier

237561 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › mitosporic Saccharomycetales › Candida

Protein attributes

Sequence length	487 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level

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.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Peroxisome
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from mutant phenotype. Source: CGD hyphal growth Inferred from mutant phenotype. Source: CGD interaction with host Inferred from physical interaction. Source: CGD pathogenesis Inferred from mutant phenotype Ref.1. Source: CGD
Cellular component	fungal-type cell wall Inferred from direct assay. Source: CGD peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	catalase activity Inferred from direct assay Ref.1. Source: CGD heme binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: CGD
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 487

486

Peroxisomal catalase

PRO_0000084918

Sites

Active site

By similarity

Active site

126

By similarity

Metal binding

336

Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict

114

I → F in BAA21767. Ref.2

Sequence conflict

114

I → F in EAK99824. Ref.3

Sequence conflict

114

I → F in EAK99912. Ref.3

Sequence conflict

224

N → T in BAA21767. Ref.2

Sequence conflict

224

N → T in EAK99824. Ref.3

Sequence conflict

224

N → T in EAK99912. Ref.3

Sequence conflict

284

R → K in BAA21767. Ref.2

Sequence conflict

284

R → K in EAK99824. Ref.3

Sequence conflict

284

R → K in EAK99912. Ref.3

Sequence conflict

288

M → L in BAA21767. Ref.2

Sequence conflict

288

M → L in EAK99824. Ref.3

Sequence conflict

288

M → L in EAK99912. Ref.3

Sequence conflict

301

E → K in BAA21767. Ref.2

Sequence conflict

301

E → K in EAK99824. Ref.3

Sequence conflict

301

E → K in EAK99912. Ref.3

Sequence conflict

342

Missing in BAA21767. Ref.2

Sequence conflict

342

Missing in EAK99824. Ref.3

Sequence conflict

342

Missing in EAK99912. Ref.3

Sequence conflict

367

S → M in BAA21767. Ref.2

Sequence conflict

367

S → M in EAK99824. Ref.3

Sequence conflict

367

S → M in EAK99912. Ref.3

Sequence conflict

398 – 399

SF → L in BAA21767. Ref.2

Sequence conflict

398 – 399

SF → L in EAK99824. Ref.3

Sequence conflict

398 – 399

SF → L in EAK99912. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

O13289 [UniParc].

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

FASTA

487

55,063

        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

« Hide

References

	« Hide 'large scale' referencesShow '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 / NBRC 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 / ATCC MYA-2876.
+	Additional computationally mapped references.

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.
RefSeq	XP_718734.1. XM_713641.1. XP_718818.1. XM_713725.1.
3D structure databases
ProteinModelPortal	O13289.
SMR	O13289. Positions 6-478.
ModBase	Search...
Protein-protein interaction databases
STRING	O13289.
Protein family/group databases
PeroxiBase	5253. CalKat01.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3639495. 3639575.
KEGG	cal:CaO19.13609. cal:CaO19.6229.
Family and domain databases
InterPro	IPR018028. Catalase. IPR020835. Catalase-like_dom. IPR024708. Catalase_AS. IPR024711. Catalase_clade1/3. IPR011614. Catalase_core. IPR002226. Catalase_haem_BS. IPR010582. Catalase_immune_responsive. [Graphical view]
Gene3D	G3DSA:2.40.180.10. Catalase_N. 1 hit.
KO	K03781.
PANTHER	PTHR11465. Catalase. 1 hit.
Pfam	PF00199. Catalase. 1 hit. PF06628. Catalase-rel. 1 hit. [Graphical view]
PIRSF	PIRSF038928. Catalase_clade1-3. 1 hit.
PRINTS	PR00067. CATALASE.
SMART	SM01060. Catalase. 1 hit. [Graphical view]
SUPFAM	SSF56634. Catalase_N. 1 hit.
PROSITE	PS00437. CATALASE_1. 1 hit. PS00438. CATALASE_2. 1 hit. PS51402. CATALASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CATA_CANAL

Accession

Primary (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 25, 2012
This is version 72 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Fungal Protein Annotation Program

Relevant documents

Candida albicans

Candida albicans: entries and gene names

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Family and domain databases

Entry information

Relevant documents