[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 10261 / CBS 2718 / IFO 1061; PubMed=9573075 [NCBI, ExPASy, EBI, Israel, Japan] Wysong D.R., Christin L., Sugar A.M., Robbins P.W., Diamond R.D.; "Cloning and sequencing of a Candida albicans catalase gene and effects of disruption of this gene."; Infect. Immun. 66:1953-1961(1998).
[2]	NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION. STRAIN=FC18; DOI=10.1111/j.1348-0421.2008.00006.x; PubMed=18352908 [NCBI, ExPASy, EBI, Israel, Japan] Nakagawa Y.; "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."; Microbiol. Immunol. 52:16-24(2008).

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.
CATALYTIC ACTIVITY: 2 H₂O₂ = O₂ + 2 H₂O.
COFACTOR: Heme group.
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Peroxisome (By similarity).
SIMILARITY: Belongs to the catalase 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

U40704; AAC39448.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB006327; BAA21767.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB006328; BAA21768.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P15202; 1A4E. [HSSP ENTRY / PDB]

ModBase

O13289.

Family and domain databases

InterPro

IPR002226; Catalase.
IPR011614; Catalase_N.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.180.10; Catalase_N; 1.

PANTHER

PTHR11465; Catalase; 1.

Pfam

PF00199; Catalase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00067; CATALASE.

ProDom

PD000510; Catalase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00437; CATALASE_1; 1.
PS00438; CATALASE_2; 1.

Other

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

Keywords

Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase; Peroxisome.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 487`	`486`	`Peroxisomal catalase.`	`PRO_0000084918`
`ACT_SITE`	`53 53`		`By similarity.`
`ACT_SITE`	`126 126`		`By similarity.`
`METAL`	`336 336`		`Iron (heme axial ligand) (By similarity).`
`CONFLICT`	`114 114`		`I -> F (in Ref. 2; BAA21767).`
`CONFLICT`	`224 224`		`N -> T (in Ref. 2; BAA21767).`
`CONFLICT`	`284 284`		`R -> K (in Ref. 2; BAA21767).`
`CONFLICT`	`288 288`		`M -> L (in Ref. 2; BAA21767).`
`CONFLICT`	`301 301`		`E -> K (in Ref. 2; BAA21767).`
`CONFLICT`	`342 342`		`Missing (in Ref. 2; BAA21767).`
`CONFLICT`	`367 367`		`S -> M (in Ref. 2; BAA21767).`
`CONFLICT`	`398 399`		`SF -> L (in Ref. 2; BAA21767).`

Sequence information

Length: 487 AA [This is the length of the unprocessed precursor]

Molecular weight: 55063 Da [This is the MW of the unprocessed precursor]

CRC64: 16C1A0EA163C658C [This is a checksum on the sequence]

        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

O13289 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