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Protein

Catalase

Gene

CAT

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Mitogen, Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, 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-74259. Purine catabolism.
SABIO-RKP00432.

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

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

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-protein interaction databases

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[»]
3J7Uelectron 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[»]
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.
OMAiWDYRADD.
OrthoDBiEOG091G04V5.
TreeFamiTF300540.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. 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]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]

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.

Cross-referencesi

Web resourcesi

Worthington enzyme manual

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.

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[»]
3J7Uelectron 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[»]
7CATX-ray2.50A/B2-507[»]
8CATX-ray2.50A/B2-507[»]
ProteinModelPortaliP00432.
SMRiP00432.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000027941.

Chemistry databases

ChEMBLiCHEMBL2227489.

Protein family/group databases

PeroxiBasei5281. BtKat01.

Proteomic databases

PaxDbiP00432.
PeptideAtlasiP00432.
PRIDEiP00432.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000027941; ENSBTAP00000027941; ENSBTAG00000020980.
GeneIDi531682.
KEGGibta:531682.

Organism-specific databases

CTDi847.

Phylogenomic databases

eggNOGiKOG0047. Eukaryota.
COG0753. LUCA.
GeneTreeiENSGT00390000018100.
HOGENOMiHOG000087852.
HOVERGENiHBG003986.
InParanoidiP00432.
KOiK03781.
OMAiWDYRADD.
OrthoDBiEOG091G04V5.
TreeFamiTF300540.

Enzyme and pathway databases

BRENDAi1.11.1.6. 908.
ReactomeiR-BTA-3299685. Detoxification of Reactive Oxygen Species.
R-BTA-6798695. Neutrophil degranulation.
R-BTA-74259. Purine catabolism.
SABIO-RKP00432.

Miscellaneous databases

EvolutionaryTraceiP00432.
PROiP00432.

Gene expression databases

BgeeiENSBTAG00000020980.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. 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]
PANTHERiPTHR11465. PTHR11465. 1 hit.
PfamiPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFiPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSiPR00067. CATALASE.
SMARTiSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMiSSF56634. SSF56634. 1 hit.
PROSITEiPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCATA_BOVIN
AccessioniPrimary (citable) accession number: P00432
Secondary accession number(s): Q3SZ80
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 147 of the entry and version 3 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.