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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei75 – 751PROSITE-ProRule annotation1 Publication
Active sitei148 – 1481
Metal bindingi358 – 3581Iron (heme axial ligand)1 Publication

GO - Molecular functioni

  • aminoacylase activity Source: Ensembl
  • catalase activity Source: UniProtKB
  • enzyme binding Source: UniProtKB
  • heme binding Source: InterPro
  • 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.
ReactomeiREACT_289815. Purine catabolism.
REACT_296224. Detoxification of Reactive Oxygen Species.
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
ProteomesiUP000009136 Componenti: Chromosome 15

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Peroxisome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 527526CatalasePRO_0000084898Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21Blocked amino end (Ala)1 Publication
Modified residuei9 – 91PhosphoserineBy similarity
Modified residuei13 – 131N6-succinyllysineBy similarity
Modified residuei221 – 2211N6-succinyllysineBy similarity
Modified residuei233 – 2331N6-acetyllysineBy similarity
Modified residuei417 – 4171PhosphoserineBy similarity
Modified residuei434 – 4341PhosphoserineBy similarity
Modified residuei449 – 4491N6-acetyllysine; alternateBy similarity
Modified residuei449 – 4491N6-succinyllysine; alternateBy similarity
Modified residuei480 – 4801N6-acetyllysine; alternateBy similarity
Modified residuei480 – 4801N6-succinyllysine; alternateBy similarity
Modified residuei499 – 4991N6-acetyllysineBy similarity
Modified residuei511 – 5111PhosphothreonineBy similarity
Modified residuei517 – 5171PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP00432.
PRIDEiP00432.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000027941.

Structurei

Secondary structure

1
527
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni7 – 104Combined sources
Helixi11 – 188Combined sources
Turni19 – 213Combined sources
Beta strandi38 – 403Combined sources
Beta strandi42 – 454Combined sources
Helixi55 – 6410Combined sources
Beta strandi73 – 753Combined sources
Beta strandi77 – 8711Combined sources
Turni92 – 943Combined sources
Helixi98 – 1003Combined sources
Beta strandi106 – 1149Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi124 – 1285Combined sources
Beta strandi131 – 1388Combined sources
Beta strandi141 – 15111Combined sources
Helixi158 – 1603Combined sources
Helixi161 – 1688Combined sources
Turni172 – 1743Combined sources
Helixi179 – 18810Combined sources
Helixi190 – 1923Combined sources
Helixi193 – 1997Combined sources
Helixi202 – 2043Combined sources
Beta strandi205 – 2095Combined sources
Beta strandi220 – 2234Combined sources
Beta strandi229 – 23810Combined sources
Helixi247 – 25610Combined sources
Helixi260 – 27011Combined sources
Beta strandi276 – 2849Combined sources
Helixi286 – 2916Combined sources
Turni305 – 3073Combined sources
Beta strandi311 – 32010Combined sources
Helixi325 – 3284Combined sources
Turni329 – 3313Combined sources
Beta strandi343 – 3453Combined sources
Helixi349 – 36517Combined sources
Helixi370 – 3723Combined sources
Helixi374 – 3763Combined sources
Turni395 – 4006Combined sources
Beta strandi404 – 4063Combined sources
Helixi416 – 4183Combined sources
Beta strandi424 – 4307Combined sources
Beta strandi435 – 4373Combined sources
Helixi441 – 4488Combined sources
Helixi453 – 46715Combined sources
Helixi472 – 48514Combined sources
Helixi487 – 50014Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 4-502.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP00432.

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

eggNOGiCOG0753.
GeneTreeiENSGT00390000018100.
HOGENOMiHOG000087852.
HOVERGENiHBG003986.
InParanoidiP00432.
KOiK03781.
OMAiRNPRNFF.
OrthoDBiEOG7V7660.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti213 – 2131N → D AA sequence (PubMed:7082009).Curated
Sequence conflicti226 – 2261N → D AA sequence (PubMed:7082009).Curated

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
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. Positions 4-502.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000027941.

Chemistry

ChEMBLiCHEMBL2227489.

Protein family/group databases

PeroxiBasei5281. BtKat01.

Proteomic databases

PaxDbiP00432.
PRIDEiP00432.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi847.

Phylogenomic databases

eggNOGiCOG0753.
GeneTreeiENSGT00390000018100.
HOGENOMiHOG000087852.
HOVERGENiHBG003986.
InParanoidiP00432.
KOiK03781.
OMAiRNPRNFF.
OrthoDBiEOG7V7660.
TreeFamiTF300540.

Enzyme and pathway databases

BRENDAi1.11.1.6. 908.
ReactomeiREACT_289815. Purine catabolism.
REACT_296224. Detoxification of Reactive Oxygen Species.
SABIO-RKP00432.

Miscellaneous databases

EvolutionaryTraceiP00432.
NextBioi20875507.
PROiP00432.

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...

Publicationsi

« Hide 'large scale' publications
  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. 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. Cited for: SIMILARITY TO P.VITALE CATALASE.

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: May 27, 2015
This is version 134 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

External Data

Dasty 3

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 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.