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

katA

Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
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.1 Publication

Catalytic activityi

2 H2O2 = O2 + 2 H2O.

Cofactori

heme1 Publication

Enzyme regulationi

Strongly inhibited by sodium azide and sodium cyanide, and sligthly inhibited by 3-amino-1,2,4-triazole.1 Publication

Temperature dependencei

Optimum temperature is 30 degrees Celsius. Active over a temperature range from 20 to 70 degrees Celsius. Retains 100% of its initial activity following incubation at 40 degrees Celsius, and 82% of its activity following incubation at 50 degrees Celsius. The activity decreases significantly to 30% of the initial activity following incubation at 60 degrees Celsius.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei81By similarity1
Active sitei159By similarity1
Metal bindingi369Iron (heme axial ligand)By similarity1

GO - Molecular functioni

  • catalase activity Source: CACAO
  • heme binding Source: GO_Central
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase (EC:1.11.1.6)
Gene namesi
Name:katA
Ordered Locus Names:DR_1998
OrganismiDeinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Taxonomic identifieri243230 [NCBI]
Taxonomic lineageiBacteriaDeinococcus-ThermusDeinococciDeinococcalesDeinococcaceaeDeinococcus
Proteomesi
  • UP000002524 Componenti: Chromosome I

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000850141 – 536CatalaseAdd BLAST536

Expressioni

Developmental stagei

Up-regulated during stationary phase.1 Publication

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi243230.DR_1998.

Structurei

Secondary structure

1536
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi49 – 51Combined sources3
Helixi61 – 70Combined sources10
Beta strandi79 – 81Combined sources3
Beta strandi83 – 93Combined sources11
Beta strandi95 – 97Combined sources3
Helixi102 – 104Combined sources3
Helixi109 – 111Combined sources3
Beta strandi117 – 125Combined sources9
Beta strandi127 – 129Combined sources3
Beta strandi142 – 149Combined sources8
Beta strandi152 – 162Combined sources11
Helixi169 – 171Combined sources3
Helixi172 – 179Combined sources8
Turni183 – 185Combined sources3
Helixi190 – 198Combined sources9
Helixi201 – 203Combined sources3
Helixi204 – 210Combined sources7
Helixi213 – 215Combined sources3
Beta strandi216 – 218Combined sources3
Beta strandi231 – 234Combined sources4
Beta strandi240 – 249Combined sources10
Beta strandi253 – 255Combined sources3
Helixi258 – 265Combined sources8
Helixi271 – 281Combined sources11
Beta strandi287 – 298Combined sources12
Turni316 – 318Combined sources3
Beta strandi322 – 331Combined sources10
Helixi336 – 339Combined sources4
Turni340 – 342Combined sources3
Helixi360 – 376Combined sources17
Helixi381 – 383Combined sources3
Turni385 – 387Combined sources3
Beta strandi418 – 420Combined sources3
Helixi456 – 464Combined sources9
Helixi467 – 481Combined sources15
Helixi486 – 499Combined sources14
Helixi501 – 519Combined sources19
Beta strandi529 – 532Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4CABX-ray2.60A/B/C/D1-536[»]
ProteinModelPortaliQ59337.
SMRiQ59337.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.Curated

Phylogenomic databases

eggNOGiENOG4105CH6. Bacteria.
COG0753. LUCA.
HOGENOMiHOG000087852.
InParanoidiQ59337.
KOiK03781.
OMAiEAMHMIT.
OrthoDBiPOG091H0599.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. Catalase.
IPR020835. Catalase-like_dom.
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.
PS51402. CATALASE_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q59337-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDENNKGVG TAVQGVGGPR DGRTAPGEQG TTLTTRQGHP VHDNQNSRTV
60 70 80 90 100
GSRGPMTLEN YQFIEKLSHF DRERIPERVV HARGVGAHGV FRATGKVGDE
110 120 130 140 150
PVSKYTRAKL FQEDGKETPV FVRFSTVGHG THSPETLRDP RGFAVKFYTE
160 170 180 190 200
DGNWDLVGNN LKIFFIRDAL KFPDLIHSQK PSPTTNIQSQ ERIFDFFAGS
210 220 230 240 250
PEATHMITLL YSPWGIPASY RFMQGSGVNT YKWVNDQGEG VLVKYHWEPV
260 270 280 290 300
QGVRNLTQMQ ADEVQATNFN HATQDLHDAI ERGDFPQWDL FVQIMEDGEH
310 320 330 340 350
PELDFDPLDD TKIWPREQFP WRHVGQMTLN RNPENVFAET EQAAFGTGVL
360 370 380 390 400
VDGLDFSDDK MLQGRTFSYS DTQRYRVGPN YLQLPINAPK KHVATNQRDG
410 420 430 440 450
QMAYRVDTFE GQDQRVNYEP SLLSGPKEAP RRAPEHTPRV EGNLVRAAIE
460 470 480 490 500
RPNPFGQAGM QYRNFADWER DELVSNLSGA LAGVDKRIQD KMLEYFTAAD
510 520 530
ADYGQRVREG IQAKEAEMKG QKQEAPVYGT EASSLY
Length:536
Mass (Da):60,513
Last modified:May 30, 2000 - v2
Checksum:i6A60CB6A8F445A59
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti152G → A in BAA09937 (Ref. 1) Curated1
Sequence conflicti156 – 158LVG → FVV in BAA09937 (Ref. 1) Curated3
Sequence conflicti277H → R in BAA09937 (Ref. 1) Curated1
Sequence conflicti293Q → K in BAA09937 (Ref. 1) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63898 Genomic DNA. Translation: BAA09937.1.
AE000513 Genomic DNA. Translation: AAF11546.1.
PIRiB75329.
RefSeqiNP_295721.1. NC_001263.1.
WP_010888631.1. NZ_CP015081.1.

Genome annotation databases

EnsemblBacteriaiAAF11546; AAF11546; DR_1998.
GeneIDi1800077.
KEGGidra:DR_1998.
PATRICi21631656. VBIDeiRad64572_2221.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D63898 Genomic DNA. Translation: BAA09937.1.
AE000513 Genomic DNA. Translation: AAF11546.1.
PIRiB75329.
RefSeqiNP_295721.1. NC_001263.1.
WP_010888631.1. NZ_CP015081.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4CABX-ray2.60A/B/C/D1-536[»]
ProteinModelPortaliQ59337.
SMRiQ59337.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243230.DR_1998.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAF11546; AAF11546; DR_1998.
GeneIDi1800077.
KEGGidra:DR_1998.
PATRICi21631656. VBIDeiRad64572_2221.

Phylogenomic databases

eggNOGiENOG4105CH6. Bacteria.
COG0753. LUCA.
HOGENOMiHOG000087852.
InParanoidiQ59337.
KOiK03781.
OMAiEAMHMIT.
OrthoDBiPOG091H0599.

Family and domain databases

Gene3Di2.40.180.10. 1 hit.
InterProiIPR018028. Catalase.
IPR020835. Catalase-like_dom.
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.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCATA_DEIRA
AccessioniPrimary (citable) accession number: Q59337
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 30, 2000
Last modified: November 2, 2016
This is version 117 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, Complete proteome, 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.