Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Catalase

Gene

CAT

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Promotes growth of cells.

Catalytic activityi

2 H2O2 = O2 + 2 H2O.PROSITE-ProRule annotation

Cofactori

Protein has several cofactor binding sites:

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei75PROSITE-ProRule annotation1 Publication1
Active sitei1481
Metal bindingi358Iron (heme axial ligand)1 Publication1

GO - Molecular functioni

  • aminoacylase activity Source: Ensembl
  • catalase activity Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • heme binding Source: GO_Central
  • metal ion binding Source: UniProtKB-KW
  • NADP binding Source: Ensembl
  • protein homodimerization activity Source: Ensembl
  • signaling receptor binding Source: Ensembl

GO - Biological processi

Keywordsi

Molecular functionMitogen, Oxidoreductase, Peroxidase
Biological processHydrogen peroxide
LigandHeme, Iron, Metal-binding, NADP

Enzyme and pathway databases

BRENDAi1.11.1.6 908
ReactomeiR-BTA-3299685 Detoxification of Reactive Oxygen Species
R-BTA-6798695 Neutrophil degranulation
R-BTA-9033241 Peroxisomal protein import
SABIO-RKiP00432

Protein family/group databases

PeroxiBasei5281 BtKat01

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase (EC:1.11.1.6)
Gene namesi
Name:CAT
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 15

Organism-specific databases

VGNCiVGNC:26792 CAT

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Peroxisome

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2227489

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity1 Publication
ChainiPRO_00000848982 – 527CatalaseAdd BLAST526

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2Blocked amino end (Ala); alternate1 Publication1
Modified residuei2N-acetylalanine; alternateBy similarity1
Modified residuei9PhosphoserineBy similarity1
Modified residuei13N6-succinyllysineBy similarity1
Modified residuei221N6-succinyllysineBy similarity1
Modified residuei233N6-acetyllysineBy similarity1
Modified residuei417PhosphoserineBy similarity1
Modified residuei434PhosphoserineBy similarity1
Modified residuei449N6-acetyllysine; alternateBy similarity1
Modified residuei449N6-succinyllysine; alternateBy similarity1
Modified residuei480N6-acetyllysine; alternateBy similarity1
Modified residuei480N6-succinyllysine; alternateBy similarity1
Modified residuei499N6-acetyllysineBy similarity1
Modified residuei511PhosphothreonineBy similarity1
Modified residuei517PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP00432
PeptideAtlasiP00432
PRIDEiP00432

Expressioni

Gene expression databases

BgeeiENSBTAG00000020980

Interactioni

Subunit structurei

Homotetramer.

GO - Molecular functioni

  • enzyme binding Source: UniProtKB
  • protein homodimerization activity Source: Ensembl
  • signaling receptor binding Source: Ensembl

Protein-protein interaction databases

IntActiP00432, 1 interactor
STRINGi9913.ENSBTAP00000027941

Structurei

Secondary structure

1527
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni7 – 10Combined sources4
Helixi11 – 18Combined sources8
Turni19 – 21Combined sources3
Beta strandi38 – 40Combined sources3
Beta strandi42 – 45Combined sources4
Helixi55 – 64Combined sources10
Beta strandi73 – 75Combined sources3
Beta strandi77 – 87Combined sources11
Turni92 – 94Combined sources3
Helixi98 – 100Combined sources3
Beta strandi106 – 114Combined sources9
Beta strandi116 – 118Combined sources3
Beta strandi124 – 128Combined sources5
Beta strandi131 – 138Combined sources8
Beta strandi141 – 151Combined sources11
Helixi158 – 160Combined sources3
Helixi161 – 168Combined sources8
Turni172 – 174Combined sources3
Helixi179 – 188Combined sources10
Helixi190 – 192Combined sources3
Helixi193 – 199Combined sources7
Helixi202 – 204Combined sources3
Beta strandi205 – 209Combined sources5
Beta strandi220 – 223Combined sources4
Beta strandi229 – 238Combined sources10
Helixi247 – 256Combined sources10
Helixi260 – 270Combined sources11
Beta strandi276 – 284Combined sources9
Helixi286 – 291Combined sources6
Turni305 – 307Combined sources3
Beta strandi311 – 320Combined sources10
Helixi325 – 328Combined sources4
Turni329 – 331Combined sources3
Beta strandi343 – 345Combined sources3
Helixi349 – 365Combined sources17
Helixi370 – 372Combined sources3
Helixi374 – 376Combined sources3
Turni395 – 400Combined sources6
Beta strandi404 – 406Combined sources3
Helixi416 – 418Combined sources3
Beta strandi424 – 430Combined sources7
Beta strandi435 – 437Combined sources3
Helixi441 – 448Combined sources8
Helixi453 – 467Combined sources15
Helixi472 – 485Combined sources14
Helixi487 – 500Combined sources14

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1TGUX-ray2.80A/B/C/D2-507[»]
1TH2X-ray2.80A/B/C/D2-507[»]
1TH3X-ray2.80A/B/C/D2-507[»]
1TH4X-ray2.98A/B/C/D2-507[»]
3J7Belectron microscopy3.20A/B/C/D1-527[»]
3NWLX-ray2.69A/B/C/D1-527[»]
3RE8X-ray1.90A/B/C/D4-502[»]
3RGPX-ray1.88A/B/C/D4-502[»]
3RGSX-ray1.99A/B/C/D4-502[»]
4BLCX-ray2.30A/B/C/D2-507[»]
5GKNelectron microscopy3.20A/B/C/D1-527[»]
7CATX-ray2.50A/B2-507[»]
8CATX-ray2.50A/B2-507[»]
ProteinModelPortaliP00432
SMRiP00432
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00432

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

eggNOGiKOG0047 Eukaryota
COG0753 LUCA
GeneTreeiENSGT00390000018100
HOGENOMiHOG000087852
HOVERGENiHBG003986
InParanoidiP00432
KOiK03781
OMAiHADFGRM
OrthoDBiEOG091G04V5
TreeFamiTF300540

Family and domain databases

InterProiView protein in InterPro
IPR018028 Catalase
IPR024708 Catalase_AS
IPR024711 Catalase_clade1/3
IPR011614 Catalase_core
IPR002226 Catalase_haem_BS
IPR010582 Catalase_immune_responsive
IPR020835 Catalase_sf
PANTHERiPTHR11465 PTHR11465, 1 hit
PfamiView protein in Pfam
PF00199 Catalase, 1 hit
PF06628 Catalase-rel, 1 hit
PIRSFiPIRSF038928 Catalase_clade1-3, 1 hit
PRINTSiPR00067 CATALASE
SMARTiView protein in SMART
SM01060 Catalase, 1 hit
SUPFAMiSSF56634 SSF56634, 1 hit
PROSITEiView protein in PROSITE
PS00437 CATALASE_1, 1 hit
PS00438 CATALASE_2, 1 hit
PS51402 CATALASE_3, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P00432-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADNRDPASD QMKHWKEQRA AQKPDVLTTG GGNPVGDKLN SLTVGPRGPL
60 70 80 90 100
LVQDVVFTDE MAHFDRERIP ERVVHAKGAG AFGYFEVTHD ITRYSKAKVF
110 120 130 140 150
EHIGKRTPIA VRFSTVAGES GSADTVRDPR GFAVKFYTED GNWDLVGNNT
160 170 180 190 200
PIFFIRDALL FPSFIHSQKR NPQTHLKDPD MVWDFWSLRP ESLHQVSFLF
210 220 230 240 250
SDRGIPDGHR HMNGYGSHTF KLVNANGEAV YCKFHYKTDQ GIKNLSVEDA
260 270 280 290 300
ARLAHEDPDY GLRDLFNAIA TGNYPSWTLY IQVMTFSEAE IFPFNPFDLT
310 320 330 340 350
KVWPHGDYPL IPVGKLVLNR NPVNYFAEVE QLAFDPSNMP PGIEPSPDKM
360 370 380 390 400
LQGRLFAYPD THRHRLGPNY LQIPVNCPYR ARVANYQRDG PMCMMDNQGG
410 420 430 440 450
APNYYPNSFS APEHQPSALE HRTHFSGDVQ RFNSANDDNV TQVRTFYLKV
460 470 480 490 500
LNEEQRKRLC ENIAGHLKDA QLFIQKKAVK NFSDVHPEYG SRIQALLDKY
510 520
NEEKPKNAVH TYVQHGSHLS AREKANL
Length:527
Mass (Da):59,915
Last modified:January 23, 2007 - v3
Checksum:i2F97E793153D7AF9
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti213N → D AA sequence (PubMed:7082009).Curated1
Sequence conflicti226N → D AA sequence (PubMed:7082009).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC103066 mRNA Translation: AAI03067.1
PIRiA00500 CSBO
RefSeqiNP_001030463.1, NM_001035386.2
UniGeneiBt.48925

Genome annotation databases

EnsembliENSBTAT00000027941; ENSBTAP00000027941; ENSBTAG00000020980
GeneIDi531682
KEGGibta:531682

Similar proteinsi

Entry informationi

Entry nameiCATA_BOVIN
AccessioniPrimary (citable) accession number: P00432
Secondary accession number(s): Q3SZ80
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 156 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health