P00432 (CATA_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Catalase
EC=1.11.1.6

Gene names

Name:

CAT

Organism

Bos taurus (Bovine) [Reference proteome]

Taxonomic identifier

9913 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos

Protein attributes

Sequence length	527 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells.
Catalytic activity	2 H2O2 = O2 + 2 H2O.
Cofactor	Heme group. NADP.
Subunit structure	Homotetramer.
Subcellular location	Peroxisome.
Sequence similarities	Belongs to the catalase family.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Peroxisome
Ligand	Heme Iron Metal-binding NADP
Molecular function	Mitogen Oxidoreductase Peroxidase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	UV protection Inferred from electronic annotation. Source: Compara aerobic respiration Inferred from electronic annotation. Source: Compara cholesterol metabolic process Inferred from electronic annotation. Source: Compara hemoglobin metabolic process Inferred from electronic annotation. Source: Compara hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of NF-kappaB transcription factor activity Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of NF-kappaB transcription factor activity Inferred from electronic annotation. Source: Compara positive regulation of cell division Inferred from electronic annotation. Source: UniProtKB-KW positive regulation of phosphatidylinositol 3-kinase cascade Inferred from electronic annotation. Source: Compara protein homotetramerization Inferred from electronic annotation. Source: Compara triglyceride metabolic process Inferred from electronic annotation. Source: Compara
Cellular_component	mitochondrion Inferred from electronic annotation. Source: Compara peroxisomal membrane Inferred from electronic annotation. Source: Compara
Molecular_function	NADP binding Inferred from electronic annotation. Source: Compara aminoacylase activity Inferred from electronic annotation. Source: Compara catalase activity Inferred from electronic annotation. Source: EC heme binding Inferred from electronic annotation. Source: Compara metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 527

526

Catalase

PRO_0000084898

Sites

Active site

75

1

Ref.3

Active site

148

1

Metal binding

358

1

Iron (heme axial ligand) Ref.3

Amino acid modifications

Modified residue

2

1

Blocked amino end (Ala) Ref.2

Modified residue

517

1

Phosphoserine By similarity

Experimental info

Sequence conflict

213

1

N → D AA sequence Ref.2

Sequence conflict

226

1

N → D AA sequence Ref.2

Secondary structure

1

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527

Helix Strand Turn

Details...

Turn

7 – 10

4

Helix

11 – 18

8

Turn

19 – 21

3

Beta strand

38 – 40

3

Beta strand

42 – 45

4

Helix

55 – 64

10

Beta strand

73 – 75

3

Beta strand

77 – 87

11

Turn

92 – 94

3

Helix

98 – 100

3

Beta strand

106 – 114

9

Beta strand

116 – 118

3

Beta strand

124 – 128

5

Beta strand

131 – 138

8

Beta strand

141 – 151

11

Helix

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

Beta strand

205 – 209

5

Beta strand

220 – 223

4

Beta strand

229 – 238

10

Helix

247 – 256

10

Helix

260 – 270

11

Beta strand

276 – 284

9

Helix

286 – 291

6

Turn

305 – 307

3

Beta strand

311 – 320

10

Helix

325 – 328

4

Turn

329 – 331

3

Beta strand

343 – 345

3

Helix

349 – 365

17

Helix

370 – 372

3

Helix

374 – 376

3

Turn

395 – 400

6

Beta strand

404 – 406

3

Helix

416 – 418

3

Beta strand

424 – 430

7

Beta strand

435 – 437

3

Helix

441 – 448

8

Helix

453 – 467

15

Helix

472 – 485

14

Helix

487 – 500

14

Sequences

	Sequence		Length	Mass (Da)
	P00432 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 2F97E793153D7AF9	FASTA	527	59,915
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	NIH - Mammalian Gene Collection (MGC) project Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Hereford. Tissue: Rumen reticulum.
[2]	"The complete amino acid sequence of bovine liver catalase and the partial sequence of bovine erythrocyte catalase." Schroeder W.A., Shelton J.R., Shelton J.B., Robberson B., Apell G., Fang R.S., Bonaventura J. Arch. Biochem. Biophys. 214:397-421(1982) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-507. Tissue: Liver.
[3]	"Structure of beef liver catalase." Murthy M.R.N., Reid T.J. III, Sicignano A., Tanaka N., Rossmann M.G. J. Mol. Biol. 152:465-499(1981) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). Tissue: Liver.
[4]	"The refined structure of beef liver catalase at 2.5-A resolution." Fita I., Silva A.M., Murthy M.R.N., Rossmann M.G. Acta Crystallogr. B 42:497-515(1986) Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS). Tissue: Liver.
[5]	"Structure of orthorhombic crystals of beef liver catalase." Ko T.P., Day J., Malkin A.J., McPherson A. Acta Crystallogr. D 55:1383-1394(1999) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). Tissue: Liver.
[6]	"Comparison of beef liver and Penicillium vitale catalases." 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. J. Mol. Biol. 188:63-72(1986) [PubMed] [Europe PMC] [Abstract] Cited for: SIMILARITY TO P.VITALE CATALASE.
+	Additional computationally mapped references.

Web resources

Worthington enzyme manual

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BC103066 mRNA. Translation: AAI03067.1.

IPI

IPI00705932.

PIR

CSBO. A00500.

RefSeq

NP_001030463.1. NM_001035386.2.

UniGene

Bt.48925.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1TGU	X-ray	2.80	A/B/C/D	2-507	[»]
1TH2	X-ray	2.80	A/B/C/D	2-507	[»]
1TH3	X-ray	2.80	A/B/C/D	2-507	[»]
1TH4	X-ray	2.98	A/B/C/D	2-507	[»]
3NWL	X-ray	2.69	A/B/C/D	1-527	[»]
3RE8	X-ray	1.90	A/B/C/D	4-502	[»]
3RGP	X-ray	1.88	A/B/C/D	4-502	[»]
3RGS	X-ray	1.99	A/B/C/D	4-502	[»]
4BLC	X-ray	2.30	A/B/C/D	2-507	[»]
7CAT	X-ray	2.50	A/B	2-506	[»]
8CAT	X-ray	2.50	A/B	2-506	[»]

ProteinModelPortal

P00432.

SMR

P00432. Positions 4-502.

ModBase

Search...

Protein-protein interaction databases

STRING

9913.ENSBTAP00000027941.

Protein family/group databases

PeroxiBase

5281. BtKat01.

Proteomic databases

PaxDb

P00432.

PRIDE

P00432.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSBTAT00000027941; ENSBTAP00000027941; ENSBTAG00000020980.

GeneID

531682.

KEGG

bta:531682.

Organism-specific databases

CTD

847.

Phylogenomic databases

eggNOG

COG0753.

GeneTree

ENSGT00390000018100.

HOGENOM

HOG000087852.

HOVERGEN

HBG003986.

InParanoid

P00432.

KO

K03781.

OMA

HDITRYS.

OrthoDB

EOG45TCMV.

Enzyme and pathway databases

SABIO-RK

P00432.

Family and domain databases

Gene3D

2.40.180.10. 1 hit.

InterPro

IPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024708. Catalase_AS.
IPR024711. Catalase_clade1/3.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[Graphical view]

PANTHER

PTHR11465. PTHR11465. 1 hit.

Pfam

PF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]

PIRSF

PIRSF038928. Catalase_clade1-3. 1 hit.

PRINTS

PR00067. CATALASE.

SMART

SM01060. Catalase. 1 hit.
[Graphical view]

SUPFAM

SSF56634. Catalase_N. 1 hit.

PROSITE

PS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P00432.

NextBio

20875507.

Entry information

Entry name

CATA_BOVIN

Accession

Primary (citable) accession number: P00432
Secondary accession number(s): Q3SZ80

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 115 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program