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Q59337

- CATA_DEIRA

UniProt

Q59337 - CATA_DEIRA

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Protein

Catalase

Gene
katA, DR_1998
Organism
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422)
Status
Reviewed - 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

Heme group.1 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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei81 – 811 By similarity
Active sitei159 – 1591 By similarity
Metal bindingi369 – 3691Iron (heme axial ligand) By similarity

GO - Molecular functioni

  1. catalase activity Source: CACAO
  2. heme binding Source: InterPro
  3. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. hydrogen peroxide catabolic process Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BioCyciDRAD243230:GH46-2032-MONOMER.

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
ProteomesiUP000002524: Chromosome I

Subcellular locationi

Cytoplasm Inferred

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 536536CatalasePRO_0000085014Add
BLAST

Proteomic databases

PRIDEiQ59337.

Expressioni

Developmental stagei

Up-regulated during stationary phase.1 Publication

Interactioni

Subunit structurei

Homotetramer.1 Publication

Protein-protein interaction databases

STRINGi243230.DR_1998.

Structurei

3D structure databases

ProteinModelPortaliQ59337.
SMRiQ59337. Positions 32-515.

Family & Domainsi

Sequence similaritiesi

Belongs to the catalase family.

Phylogenomic databases

eggNOGiCOG0753.
HOGENOMiHOG000087852.
KOiK03781.
OMAiEATTMIM.
OrthoDBiEOG6P5Z9F.

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

MSDENNKGVG TAVQGVGGPR DGRTAPGEQG TTLTTRQGHP VHDNQNSRTV    50
GSRGPMTLEN YQFIEKLSHF DRERIPERVV HARGVGAHGV FRATGKVGDE 100
PVSKYTRAKL FQEDGKETPV FVRFSTVGHG THSPETLRDP RGFAVKFYTE 150
DGNWDLVGNN LKIFFIRDAL KFPDLIHSQK PSPTTNIQSQ ERIFDFFAGS 200
PEATHMITLL YSPWGIPASY RFMQGSGVNT YKWVNDQGEG VLVKYHWEPV 250
QGVRNLTQMQ ADEVQATNFN HATQDLHDAI ERGDFPQWDL FVQIMEDGEH 300
PELDFDPLDD TKIWPREQFP WRHVGQMTLN RNPENVFAET EQAAFGTGVL 350
VDGLDFSDDK MLQGRTFSYS DTQRYRVGPN YLQLPINAPK KHVATNQRDG 400
QMAYRVDTFE GQDQRVNYEP SLLSGPKEAP RRAPEHTPRV EGNLVRAAIE 450
RPNPFGQAGM QYRNFADWER DELVSNLSGA LAGVDKRIQD KMLEYFTAAD 500
ADYGQRVREG IQAKEAEMKG QKQEAPVYGT EASSLY 536
Length:536
Mass (Da):60,513
Last modified:May 30, 2000 - v2
Checksum:i6A60CB6A8F445A59
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti152 – 1521G → A in BAA09937. 1 Publication
Sequence conflicti156 – 1583LVG → FVV in BAA09937. 1 Publication
Sequence conflicti277 – 2771H → R in BAA09937. 1 Publication
Sequence conflicti293 – 2931Q → K in BAA09937. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D63898 Genomic DNA. Translation: BAA09937.1.
AE000513 Genomic DNA. Translation: AAF11546.1.
PIRiB75329.
RefSeqiNP_295721.1. NC_001263.1.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D63898 Genomic DNA. Translation: BAA09937.1 .
AE000513 Genomic DNA. Translation: AAF11546.1 .
PIRi B75329.
RefSeqi NP_295721.1. NC_001263.1.

3D structure databases

ProteinModelPortali Q59337.
SMRi Q59337. Positions 32-515.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 243230.DR_1998.

Proteomic databases

PRIDEi Q59337.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAF11546 ; AAF11546 ; DR_1998 .
GeneIDi 1800077.
KEGGi dra:DR_1998.
PATRICi 21631656. VBIDeiRad64572_2221.

Phylogenomic databases

eggNOGi COG0753.
HOGENOMi HOG000087852.
KOi K03781.
OMAi EATTMIM.
OrthoDBi EOG6P5Z9F.

Enzyme and pathway databases

BioCyci DRAD243230:GH46-2032-MONOMER.

Family and domain databases

Gene3Di 2.40.180.10. 1 hit.
InterProi IPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024711. Catalase_clade1/3.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[Graphical view ]
PANTHERi PTHR11465. PTHR11465. 1 hit.
Pfami PF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view ]
PIRSFi PIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSi PR00067. CATALASE.
SMARTi SM01060. Catalase. 1 hit.
[Graphical view ]
SUPFAMi SSF56634. SSF56634. 1 hit.
PROSITEi PS00437. CATALASE_1. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and nucleotide sequence of radiation-inducible catalase gene from radioresistant bacterium, Deinococcus radiodurans."
    Narumi I., Watanabe H., Hossain A., Tanaka A., Kitayama S.
    Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
  3. "Induction of resistance to hydrogen peroxide and radiation in Deinococcus radiodurans."
    Wang P., Schellhorn H.E.
    Can. J. Microbiol. 41:170-176(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
    Strain: ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422.
  4. "Characterization of monofunctional catalase KatA from radioresistant bacterium Deinococcus radiodurans."
    Kobayashi I., Tamura T., Sghaier H., Narumi I., Yamaguchi S., Umeda K., Inagaki K.
    J. Biosci. Bioeng. 101:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR, SUBUNIT, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: KR1.

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: June 11, 2014
This is version 103 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

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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