[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. TISSUE=Hypocotyl; DOI=10.1007/BF00043878; PubMed=8049373 [NCBI, ExPASy, EBI, Israel, Japan] Suzuki M., Ario T., Hattori T., Nakamura K., Asahi T.; "Isolation and characterization of two tightly linked catalase genes from castor bean that are differentially regulated."; Plant Mol. Biol. 25:507-516(1994).
[2]	NUCLEOTIDE SEQUENCE [MRNA] OF 404-492. STRAIN=cv. Hale; PubMed=1712298 [NCBI, ExPASy, EBI, Israel, Japan] Gonzalez E.; "The C-terminal domain of plant catalases. Implications for a glyoxysomal targeting sequence."; Eur. J. Biochem. 199:211-215(1991).

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 (Potential). Glyoxysome (Potential).
TISSUE SPECIFICITY: Abundant in endosperms and cotyledons. Only in small amount in root.
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

D21161; BAA04697.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X59694; CAA42215.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S46297; S46297.

3D structure databases

HSSP

P46206; 1M7S. [HSSP ENTRY / PDB]

ModBase

Q01297.

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

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

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 492`	`492`	`Catalase isozyme 1.`	`PRO_0000084956`
`ACT_SITE`	`65 65`		`By similarity.`
`ACT_SITE`	`138 138`		`By similarity.`
`METAL`	`348 348`		`Iron (heme axial ligand) (By similarity).`
`CONFLICT`	`439 439`		`A -> P (in Ref. 2; CAA42215).`
`CONFLICT`	`446 446`		`F -> S (in Ref. 2; CAA42215).`
`CONFLICT`	`454 454`		`L -> F (in Ref. 2).`
`CONFLICT`	`456 456`		`D -> E (in Ref. 2).`
`CONFLICT`	`461 461`		`H -> Q (in Ref. 2; CAA42215).`

Sequence information

Length: 492 AA [This is the length of the unprocessed precursor]

Molecular weight: 56464 Da [This is the MW of the unprocessed precursor]

CRC64: B5E28A425088BF63 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MDPYRNRPSS GFNTPFWTTN SGAPVWNNNS SLTVGSRGPI LLEDYHLIEK LANFDRERIP 

        70         80         90        100        110        120 
ERVVHARGAS AKGFFEVTHD VSHLTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR 

       130        140        150        160        170        180 
GFAVKFYTRE GNFDLVGNNF PVFFIRDGMK FPDVVHAFKP NPKSHLQENW RIFDFLSHVP 

       190        200        210        220        230        240 
ESLHMLTFLL DDLGIPQDYR HMEGSGVNTY TLINKAGKVH YVKFHWKPTC GVKCLLENEA 

       250        260        270        280        290        300 
IKVGGSNHSH ATQDLYDSIS AGNYPEWKLY IQIMDPAHED KFDFDPLDVT KTWPEDILPL 

       310        320        330        340        350        360 
QPVGRLVLNK NIDNFFAENE QLAFCPGIVV PGVSYSEDKL LQTRIFSYSD TQRHRLGPNY 

       370        380        390        400        410        420 
LQLPVNAPKC AHHNNHHEGF MNFMHRDEEV NYFPSRCDPA RNAESFPVPS AICSGKREKC 

       430        440        450        460        470        480 
VIEKENNFKQ PGERYRSWAP DRQERFLNRL VGGLSDPRIT HELRTIWISY WIQCDKSLGQ 

       490 
KLATRLNVKP SI

Q01297 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