NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBCELLULAR LOCATION.
STRAIN=S2;
DOI=10.1128/JB.183.21.6372-6383.2001; PubMed=11591682 [NCBI, ExPASy, EBI, Israel, Japan]
Horiguchi H., Yurimoto H., Goh T.K., Nakagawa T., Kato N., Sakai Y.;
"Peroxisomal catalase in the methylotrophic yeast Candida boidinii: transport efficiency and metabolic significance.";
J. Bacteriol. 183:6372-6383(2001).

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.
SUBCELLULAR LOCATION: Peroxisome. Note=Bimodally distributed between the cytosol and peroxisomes in methanol-grown cells but is localized exclusively in peroxisomes in oleate- and D-alanine-grown cells.
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

AB064338; BAB69893.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

3D structure databases

HSSP

P15202; 1A4E. [HSSP ENTRY / PDB]

ModBase

Q96VB8.

Protein family/group databases

PeroxiBase

5262; CboiKat01.

Enzyme and pathway databases

BioCyc

MetaCyc:MON-13166; -.

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

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 504`	`504`	`Peroxisomal catalase.`	`PRO_0000084919`
`MOTIF`	`502 504`	`3`	`Microbody targeting signal.`
`ACT_SITE`	`63 63`		`By similarity.`
`ACT_SITE`	`136 136`		`By similarity.`
`METAL`	`345 345`		`Iron (heme axial ligand) (By similarity).`

Sequence information

Length: 504 AA [This is the length of the unprocessed precursor]

Molecular weight: 57095 Da [This is the MW of the unprocessed precursor]

CRC64: CCF63C4FA752DC3B [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSNPPTYTTS QGCPVSDAFS TQRISGTKIS IKTPVGPLLL QDFKFLDSLA HFDRERIPER 

        70         80         90        100        110        120 
VVHAKGAGAY GVFEVTEDIS DICSAKFLDT VGKKTKIFTR FSTVGGEKGS SDSARDPRGF 

       130        140        150        160        170        180 
ATKFYTEEGN LDLVYNNTPI FFIRDPTKFP HFIHTQKRNP ATNCKDANMF WDYLTNNPES 

       190        200        210        220        230        240 
LHQIMYLFSN RGTPTSYRKM NGYSGHSYKW YNAKGEWVSS VHFISNQGVH NMTDEEAGDL 

       250        260        270        280        290        300 
SGKDPDFQTM DLYKAIEQGD YPSWECYVQT MTLEEAKKQP FSVYDLTKVW PHKDFPLRHF 

       310        320        330        340        350        360 
GKFTLNENAQ NYFAEVEQAA FSPSHTVPGM EPSNDPVLQS RLFSYPDTHR HRLGVNYSQI 

       370        380        390        400        410        420 
PVNCPMRAVF APQIRDGSMM VNGNLGGTPN YAGAYNCPVQ YQAPIKASSK TPEEQYEGET 

       430        440        450        460        470        480 
LSYDWTEVNE YDFYQPGRFW EVLGKTKGEQ EALVHNVANH VSGADEFIQD RVFAYFSKAN 

       490        500 
PVIGDLIRKE VLKKSPRGAS KNKF

Q96VB8 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	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