[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. PubMed=3691514 [NCBI, ExPASy, EBI, Israel, Japan] Okada H., Ueda M., Sugaya T., Atomi H., Mozaffar S., Hishida T., Teranishi Y., Okazaki K., Takechi T., Kamiryo T., Tanaka A.; "Catalase gene of the yeast Candida tropicalis. Sequence analysis and comparison with peroxisomal and cytosolic catalases from other sources."; Eur. J. Biochem. 170:105-110(1987).
[2]	NUCLEOTIDE SEQUENCE [MRNA]. STRAIN=ATCC 20336 / pK233 / NCYC 997; DOI=10.1016/0378-1119(87)90202-2; PubMed=3446581 [NCBI, ExPASy, EBI, Israel, Japan] Murray W.W., Rachubinski R.A.; "The nucleotide sequence of complementary DNA and the deduced amino acid sequence of peroxisomal catalase of the yeast Candida tropicalis pK233."; Gene 61:401-413(1987).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=ATCC 20336 / pK233 / NCYC 997; DOI=10.1093/nar/17.9.3600; PubMed=2726500 [NCBI, ExPASy, EBI, Israel, Japan] Murray W.W., Rachubinski R.A.; "Nucleotide sequence of peroxisomal catalase from the yeast Candida tropicalis pK233: identification of an upstream BamHI site polymorphism."; Nucleic Acids Res. 17:3600-3600(1989).
[4]	NUCLEOTIDE SEQUENCE [MRNA] OF 377-385. STRAIN=ATCC 20336 / pK233 / NCYC 997; DOI=10.1016/0167-4781(87)90044-3; PubMed=3580373 [NCBI, ExPASy, EBI, Israel, Japan] Rachubinski R.A., Fujiki Y., Lazarow P.B.; "Isolation of cDNA clones coding for peroxisomal proteins of Candida tropicalis: identification and sequence of a clone for catalase."; Biochim. Biophys. Acta 909:35-43(1987).
[5]	NUCLEOTIDE SEQUENCE OF 394-451, AND PARTIAL PROTEIN SEQUENCE. DOI=10.1016/0014-5793(87)80870-0; PubMed=2440725 [NCBI, ExPASy, EBI, Israel, Japan] Ueda M., Okada H., Hishida T., Teranishi Y., Tanaka A.; "Isolation of several cDNAs encoding yeast peroxisomal enzymes."; FEBS Lett. 220:31-35(1987).

Comments

FUNCTION: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
CATALYTIC ACTIVITY: 2 H₂O₂ = O₂ + 2 H₂O.
COFACTOR: Heme group.
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Peroxisome.
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

M18832; AAA34327.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X05886; CAA29310.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X05604; CAA29093.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X06660; CAA29859.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X13978; CAA32159.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

A29629; CSCKPT.

3D structure databases

HSSP

P15202; 1A4E. [HSSP ENTRY / PDB]

ModBase

P07820.

Protein family/group databases

PeroxiBase

5256; CtKat01.

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

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 485`	`484`	`Peroxisomal catalase.`	`PRO_0000084920`
`ACT_SITE`	`53 53`		`By similarity.`
`ACT_SITE`	`126 126`		`By similarity.`
`METAL`	`336 336`		`Iron (heme axial ligand) (By similarity).`
`CONFLICT`	`166 166`		`T -> S (in Ref. 2; AAA34327).`
`CONFLICT`	`377 377`		`L -> V (in Ref. 4; CAA29093).`
`CONFLICT`	`390 390`		`I -> V (in Ref. 2; AAA34327).`

Sequence information

Length: 485 AA [This is the length of the unprocessed precursor]

Molecular weight: 54938 Da [This is the MW of the unprocessed precursor]

CRC64: 612629F910FF4E8D [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 DVCAAKFLDT VGKKTRIFTR FSTVGGELGS ADTARDPRGF ATKFYTEEGN 

       130        140        150        160        170        180 
LDLVYNNTPV FFIRDPSKFP HFIHTQKRNP ETHLKDANMF WDYLTTNEES VHQVMVLFSD 

       190        200        210        220        230        240 
RGTPASYREM NGYSGHTYKW SNNKGEWFYV QVHFISDQGI KTLTNEEAGS LAGSNPDYAQ 

       250        260        270        280        290        300 
EDLFKNIAAG NYPSWTCYIQ TMTEAQAKEA EFSVFDLTKV WPHGKYPMRR FGKFTLNENP 

       310        320        330        340        350        360 
KNYFAEVEQA AFSPAHTVPH MEPSADPVLQ SRLFSYADTH RHRLGTNYTQ IPVNCPVTGA 

       370        380        390        400        410        420 
VFNPHMRDGA MNVNGNLGNH PNYLASDKPI EFKQFSLQED QEVWHGAATP FHWKATPADF 

       430        440        450        460        470        480 
KQATELWKVL KKYPNQQEHL AHNVAVHASA ADAPIQDRVI AYFTKVHPDL GDLIKKEILE 


LSPRK

P07820 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