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Protein

Catalase

Gene

katA

Organism
Micrococcus luteus (Micrococcus lysodeikticus)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

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 sitei61 – 611
Active sitei133 – 1331
Metal bindingi343 – 3431Iron (heme axial ligand)

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding, NADP

Enzyme and pathway databases

SABIO-RKP29422.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase (EC:1.11.1.6)
Gene namesi
Name:katA
OrganismiMicrococcus luteus (Micrococcus lysodeikticus)
Taxonomic identifieri1270 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesMicrococcaceaeMicrococcus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 503503CatalasePRO_0000084990Add
BLAST

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

STRINGi465515.MlutN2_010100004891.

Structurei

Secondary structure

1
503
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 203Combined sources
Turni31 – 333Combined sources
Helixi41 – 5010Combined sources
Beta strandi63 – 7311Combined sources
Turni78 – 803Combined sources
Helixi84 – 863Combined sources
Beta strandi91 – 999Combined sources
Beta strandi101 – 1033Combined sources
Beta strandi111 – 1133Combined sources
Beta strandi116 – 1238Combined sources
Beta strandi126 – 13611Combined sources
Helixi143 – 1453Combined sources
Helixi146 – 1538Combined sources
Turni157 – 1593Combined sources
Helixi164 – 1729Combined sources
Helixi175 – 1773Combined sources
Helixi178 – 1858Combined sources
Helixi187 – 1893Combined sources
Beta strandi190 – 1923Combined sources
Helixi194 – 1963Combined sources
Beta strandi205 – 2084Combined sources
Beta strandi214 – 22310Combined sources
Helixi232 – 24110Combined sources
Helixi245 – 25511Combined sources
Beta strandi261 – 27010Combined sources
Helixi273 – 2764Combined sources
Turni290 – 2923Combined sources
Beta strandi296 – 30510Combined sources
Helixi310 – 3134Combined sources
Turni314 – 3163Combined sources
Helixi334 – 35017Combined sources
Helixi355 – 3573Combined sources
Helixi359 – 3613Combined sources
Beta strandi386 – 3894Combined sources
Beta strandi391 – 3933Combined sources
Helixi428 – 4369Combined sources
Helixi440 – 45415Combined sources
Helixi459 – 47214Combined sources
Helixi474 – 48512Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GWEX-ray0.88A1-502[»]
1GWFX-ray1.96A1-502[»]
1GWHX-ray1.74A1-502[»]
1HBZX-ray1.50A6-502[»]
ProteinModelPortaliP29422.
SMRiP29422. Positions 6-503.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29422.

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

eggNOGiENOG4105CH6. Bacteria.
COG0753. LUCA.

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.

P29422-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEHQKTTPHA TGSTRQNGAP AVSDRQSLTV GSEGPIVLHD THLLETHQHF
60 70 80 90 100
NRMNIPERRP HAKGSGAFGE FEVTEDVSKY TKALVFQPGT KTETLLRFST
110 120 130 140 150
VAGELGSPDT WRDVRGFALR FYTEEGNYDL VGNNTPIFFL RDPMKFTHFI
160 170 180 190 200
RSQKRLPDSG LRDATMQWDF WTNNPESAHQ VTYLMGPRGL PRTWREMNGY
210 220 230 240 250
GSHTYLWVNA QGEKHWVKYH FISQQGVHNL SNDEATKIAG ENADFHRQDL
260 270 280 290 300
FESIAKGDHP KWDLYIQAIP YEEGKTYRFN PFDLTKTISQ KDYPRIKVGT
310 320 330 340 350
LTLNRNPENH FAQIESAAFS PSNTVPGIGL SPDRMLLGRA FAYHDAQLYR
360 370 380 390 400
VGAHVNQLPV NRPKNAVHNY AFEGQMWYDH TGDRSTYVPN SNGDSWSDET
410 420 430 440 450
GPVDDGWEAD GTLTREAQAL RADDDDFGQA GTLVREVFSD QERDDFVETV
460 470 480 490 500
AGALKGVRQD VQARAFEYWK NVDATIGQRI EDEVKRHEGD GIPGVEAGGE

ARM
Length:503
Mass (Da):56,906
Last modified:December 6, 2002 - v2
Checksum:i8C60ADEFC0E46A09
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ438208 Genomic DNA. Translation: CAD27348.1.
PIRiS27264.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ438208 Genomic DNA. Translation: CAD27348.1.
PIRiS27264.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GWEX-ray0.88A1-502[»]
1GWFX-ray1.96A1-502[»]
1GWHX-ray1.74A1-502[»]
1HBZX-ray1.50A6-502[»]
ProteinModelPortaliP29422.
SMRiP29422. Positions 6-503.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi465515.MlutN2_010100004891.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiENOG4105CH6. Bacteria.
COG0753. LUCA.

Enzyme and pathway databases

SABIO-RKP29422.

Miscellaneous databases

EvolutionaryTraceiP29422.

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

  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], X-RAY CRYSTALLOGRAPHY (0.88 ANGSTROMS).

Entry informationi

Entry nameiCATA_MICLU
AccessioniPrimary (citable) accession number: P29422
Secondary accession number(s): Q8RK91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: December 6, 2002
Last modified: December 9, 2015
This is version 100 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.