[1]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. STRAIN=Hereford; TISSUE=Rumen reticulum; NIH - Mammalian Gene Collection (MGC) project; Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
[2]	PROTEIN SEQUENCE OF 2-507. TISSUE=Liver; DOI=10.1016/0003-9861(82)90044-3; PubMed=7082009 [NCBI, ExPASy, EBI, Israel, Japan] Schroeder W.A., Shelton J.R., Shelton J.B., Robberson B., Apell G., Fang R.S., Bonaventura J.; "The complete amino acid sequence of bovine liver catalase and the partial sequence of bovine erythrocyte catalase."; Arch. Biochem. Biophys. 214:397-421(1982).
[3]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). TISSUE=Liver; DOI=10.1016/0022-2836(81)90254-0; PubMed=7328661 [NCBI, ExPASy, EBI, Israel, Japan] Murthy M.R.N., Reid T.J. III, Sicignano A., Tanaka N., Rossmann M.G.; "Structure of beef liver catalase."; J. Mol. Biol. 152:465-499(1981).
[4]	X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). TISSUE=Liver; Fita I., Silva A.M., Murthy M.R.N., Rossmann M.G.; "The refined structure of beef liver catalase at 2.5-A resolution."; Acta Crystallogr. B 42:497-515(1986).
[5]	X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). TISSUE=Liver; DOI=10.1107/S0907444999007052; PubMed=10417406 [NCBI, ExPASy, EBI, Israel, Japan] Ko T.P., Day J., Malkin A.J., McPherson A.; "Structure of orthorhombic crystals of beef liver catalase."; Acta Crystallogr. D 55:1383-1394(1999).
[6]	SIMILARITY TO P.VITALE CATALASE. DOI=10.1016/0022-2836(86)90480-8; PubMed=3712444 [NCBI, ExPASy, EBI, Israel, Japan] Melik-Adamyan W.R., Barynin V.V., Vagin A.A., Borisov V.V., Vainshtein B.K., Fita I., Murthy M.R.N., Rossmann M.G.; "Comparison of beef liver and Penicillium vitale catalases."; J. Mol. Biol. 188:63-72(1986).

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.
COFACTOR: NADP.
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Peroxisome.
SIMILARITY: Belongs to the catalase family.
WEB RESOURCE: Name=Worthington enzyme manual; URL="http://www.worthington-biochem.com/CTL/";.

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

BC103066; AAI03067.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

A00500; CSBO.

NP_001030463.1; -.

3D structure databases

PDB

1TGU; X-ray; 2.80 A; A/B/C/D=1-507.	[ExPASy / RCSB / EBI]
1TH2; X-ray; 2.80 A; A/B/C/D=1-507.	[ExPASy / RCSB / EBI]
1TH3; X-ray; 2.80 A; A/B/C/D=1-507.	[ExPASy / RCSB / EBI]
1TH4; X-ray; 2.98 A; A/B/C/D=1-507.	[ExPASy / RCSB / EBI]
4BLC; X-ray; 2.30 A; A/B/C/D=1-507.	[ExPASy / RCSB / EBI]
8CAT; X-ray; 2.50 A; A/B=1-507.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1TGU; -.
1TH2; -.
1TH3; -.
1TH4; -.
4BLC; -.
8CAT; -.

ModBase

P00432.

Protein family/group databases

PeroxiBase

5281; BtKat01.

Ontologies

GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0042744;	Biological process: hydrogen peroxide catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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.
PS51402; CATALASE_3; 1.
PROSITE graphical view of domain structure (profiles).

Other

Genome annotation databases

Ensembl

ENSBTAG00000020980; Bos taurus. [Contig view]

GeneID

531682; -.

KEGG

bta:531682; -.

Phylogenomic databases

HOVERGEN

P00432; -.

Other

LinkHub

P00432; -.

UniRef

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

Keywords

3D-structure; Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding; NADP; Oxidoreductase; Peroxidase; Peroxisome; Phosphoprotein.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 527`	`526`	`Catalase.`	`PRO_0000084898`
`ACT_SITE`	`75 75`
`ACT_SITE`	`148 148`
`METAL`	`358 358`		`Iron (heme axial ligand).`
`MOD_RES`	`2 2`		`Blocked amino end (Ala).`
`MOD_RES`	`231 231`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`308 308`		`Phosphotyrosine (By similarity).`
`MOD_RES`	`517 517`		`Phosphoserine (By similarity).`
`CONFLICT`	`213 213`		`N -> D (in Ref. 2; AA sequence).`
`CONFLICT`	`226 226`		`N -> D (in Ref. 2; AA sequence).`
`TURN`	`7 10`	`4`
`HELIX`	`11 18`	`8`
`STRAND`	`43 45`	`3`
`HELIX`	`55 64`	`10`
`STRAND`	`73 75`	`3`
`STRAND`	`77 87`	`11`
`TURN`	`92 94`	`3`
`TURN`	`98 100`	`3`
`STRAND`	`106 114`	`9`
`STRAND`	`124 128`	`5`
`STRAND`	`131 138`	`8`
`STRAND`	`141 152`	`12`
`TURN`	`158 160`	`3`
`HELIX`	`161 168`	`8`
`TURN`	`172 174`	`3`
`HELIX`	`179 188`	`10`
`HELIX`	`190 192`	`3`
`HELIX`	`193 199`	`7`
`HELIX`	`202 204`	`3`
`STRAND`	`205 209`	`5`
`STRAND`	`220 223`	`4`
`STRAND`	`229 238`	`10`
`HELIX`	`247 256`	`10`
`HELIX`	`260 270`	`11`
`STRAND`	`276 284`	`9`
`HELIX`	`286 290`	`5`
`TURN`	`305 307`	`3`
`STRAND`	`310 320`	`11`
`HELIX`	`325 328`	`4`
`TURN`	`329 331`	`3`
`HELIX`	`349 365`	`17`
`HELIX`	`370 372`	`3`
`HELIX`	`374 376`	`3`
`TURN`	`395 400`	`6`
`STRAND`	`404 406`	`3`
`HELIX`	`416 418`	`3`
`STRAND`	`424 431`	`8`
`STRAND`	`435 437`	`3`
`HELIX`	`441 448`	`8`
`HELIX`	`453 467`	`15`
`HELIX`	`472 485`	`14`
`HELIX`	`487 500`	`14`

Sequence information

Length: 527 AA [This is the length of the unprocessed precursor]

Molecular weight: 59915 Da [This is the MW of the unprocessed precursor]

CRC64: 2F97E793153D7AF9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MADNRDPASD QMKHWKEQRA AQKPDVLTTG GGNPVGDKLN SLTVGPRGPL LVQDVVFTDE 

        70         80         90        100        110        120 
MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRYSKAKVF EHIGKRTPIA VRFSTVAGES 

       130        140        150        160        170        180 
GSADTVRDPR GFAVKFYTED GNWDLVGNNT PIFFIRDALL FPSFIHSQKR NPQTHLKDPD 

       190        200        210        220        230        240 
MVWDFWSLRP ESLHQVSFLF SDRGIPDGHR HMNGYGSHTF KLVNANGEAV YCKFHYKTDQ 

       250        260        270        280        290        300 
GIKNLSVEDA ARLAHEDPDY GLRDLFNAIA TGNYPSWTLY IQVMTFSEAE IFPFNPFDLT 

       310        320        330        340        350        360 
KVWPHGDYPL IPVGKLVLNR NPVNYFAEVE QLAFDPSNMP PGIEPSPDKM LQGRLFAYPD 

       370        380        390        400        410        420 
THRHRLGPNY LQIPVNCPYR ARVANYQRDG PMCMMDNQGG APNYYPNSFS APEHQPSALE 

       430        440        450        460        470        480 
HRTHFSGDVQ RFNSANDDNV TQVRTFYLKV LNEEQRKRLC ENIAGHLKDA QLFIQKKAVK 

       490        500        510        520 
NFSDVHPEYG SRIQALLDKY NEEKPKNAVH TYVQHGSHLS AREKANL

P00432 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