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Reviewed, UniProtKB/Swiss-Prot P29422 (CATA_MICLU)

Last modified June 16, 2009. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Catalase
    EC=1.11.1.6
Gene names
Name: katA
OrganismMicrococcus luteus (Micrococcus lysodeikticus)
Taxonomic identifier1270 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeMicrococcaceaeMicrococcus

Protein attributes

Sequence length503 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.

Catalytic activity

2 H2O2 = O2 + 2 H2O.

Cofactor

Heme group.

NADPH.

Subunit structure

Homotetramer.

Subcellular location

Cytoplasm.

Sequence similarities

Belongs to the catalase family.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentCytoplasm
   LigandHeme
Iron
Metal-binding
NADP
   Molecular functionOxidoreductase
Peroxidase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncatalase activity

Inferred from electronic annotation. Source: EC

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 503503Catalase
PRO_0000084990

Sites

Active site611
Active site1331
Metal binding3431Iron (heme axial ligand)

Secondary structure

............................................................................. 503
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29422-1 [UniParc].

Last modified December 6, 2002. Version 2.
Checksum: 8C60ADEFC0E46A09

FASTA50356,906
        10         20         30         40         50         60 
MEHQKTTPHA TGSTRQNGAP AVSDRQSLTV GSEGPIVLHD THLLETHQHF NRMNIPERRP 

        70         80         90        100        110        120 
HAKGSGAFGE FEVTEDVSKY TKALVFQPGT KTETLLRFST VAGELGSPDT WRDVRGFALR 

       130        140        150        160        170        180 
FYTEEGNYDL VGNNTPIFFL RDPMKFTHFI RSQKRLPDSG LRDATMQWDF WTNNPESAHQ 

       190        200        210        220        230        240 
VTYLMGPRGL PRTWREMNGY GSHTYLWVNA QGEKHWVKYH FISQQGVHNL SNDEATKIAG 

       250        260        270        280        290        300 
ENADFHRQDL FESIAKGDHP KWDLYIQAIP YEEGKTYRFN PFDLTKTISQ KDYPRIKVGT 

       310        320        330        340        350        360 
LTLNRNPENH FAQIESAAFS PSNTVPGIGL SPDRMLLGRA FAYHDAQLYR VGAHVNQLPV 

       370        380        390        400        410        420 
NRPKNAVHNY AFEGQMWYDH TGDRSTYVPN SNGDSWSDET GPVDDGWEAD GTLTREAQAL 

       430        440        450        460        470        480 
RADDDDFGQA GTLVREVFSD QERDDFVETV AGALKGVRQD VQARAFEYWK NVDATIGQRI 

       490        500 
EDEVKRHEGD GIPGVEAGGE ARM 

« Hide

References

[1]"Three-dimensional structure of catalase from Micrococcus lysodeikticus at 1.5-A resolution."
Murshudov G.N., Melik-Adamyan W.R., Grebenko A.I., Barynin V.V., Vagin A.A., Vainshtein B.K., Dauter Z., Wilson K.S.
FEBS Lett. 312:127-131(1992) [PubMed: 1426241] [Abstract]
Cited for: PRELIMINARY PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
[2]"The structures of Micrococcus lysodeikticus catalase, its ferryl intermediate (compound II) and NADPH complex."
Murshudov G.N., Grebenko A.I., Brannigan J.A., Antson A.A., Barynin V.V., Dodson G.G., Dauter Z., Wilson K.S., Melik-Adamyan W.R.
Acta Crystallogr. D 58:1972-1982(2002) [PubMed: 12454454] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (0.88 ANGSTROMS).

Cross-references

Sequence databases

AJ438208 Genomic DNA. Translation: CAD27348.1.
PIRS27264.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1GWEX-ray0.88A1-502[»]
1GWFX-ray1.96A1-502[»]
1GWHX-ray1.74A1-502[»]
1HBZX-ray1.50A6-502[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA1.11.1.6. 873.

Family and domain databases

InterProIPR002226. Catalase.
IPR010582. Catalase-rel_immune_responsive.
IPR011614. Catalase_N.
IPR018028. Catalase_rel_subgroup.
[Graphical view]
Gene3DG3DSA:2.40.180.10. Catalase_N. 1 hit.
PANTHERPTHR11465. Catalase. 1 hit.
PfamPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PRINTSPR00067. CATALASE.
ProDomPD000510. Catalase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCATA_MICLU
AccessionPrimary (citable) accession number: P29422
Secondary accession number(s): Q8RK91
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: December 6, 2002
Last modified: June 16, 2009
This is version 72 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents