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Q59337 (CATA_DEIRA) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein attributes

Sequence length536 AA.
Sequence statusComplete.
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. Ref.4

Catalytic activity

2 H2O2 = O2 + 2 H2O.

Cofactor

Heme group. Ref.4

Enzyme regulation

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

Subunit structure

Homotetramer. Ref.4

Subcellular location

Cytoplasm Probable.

Developmental stage

Up-regulated during stationary phase. Ref.3

Sequence similarities

Belongs to the catalase family.

Biophysicochemical properties

Temperature dependence:

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. Ref.4

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentCytoplasm
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncatalase activity

Inferred from direct assay PubMed 23365666. Source: CACAO

heme binding

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 536536Catalase
PRO_0000085014

Sites

Active site811 By similarity
Active site1591 By similarity
Metal binding3691Iron (heme axial ligand) By similarity

Experimental info

Sequence conflict1521G → A in BAA09937. Ref.1
Sequence conflict156 – 1583LVG → FVV in BAA09937. Ref.1
Sequence conflict2771H → R in BAA09937. Ref.1
Sequence conflict2931Q → K in BAA09937. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q59337 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: 6A60CB6A8F445A59

FASTA53660,513
        10         20         30         40         50         60 
MSDENNKGVG TAVQGVGGPR DGRTAPGEQG TTLTTRQGHP VHDNQNSRTV GSRGPMTLEN 

        70         80         90        100        110        120 
YQFIEKLSHF DRERIPERVV HARGVGAHGV FRATGKVGDE PVSKYTRAKL FQEDGKETPV 

       130        140        150        160        170        180 
FVRFSTVGHG THSPETLRDP RGFAVKFYTE DGNWDLVGNN LKIFFIRDAL KFPDLIHSQK 

       190        200        210        220        230        240 
PSPTTNIQSQ ERIFDFFAGS PEATHMITLL YSPWGIPASY RFMQGSGVNT YKWVNDQGEG 

       250        260        270        280        290        300 
VLVKYHWEPV QGVRNLTQMQ ADEVQATNFN HATQDLHDAI ERGDFPQWDL FVQIMEDGEH 

       310        320        330        340        350        360 
PELDFDPLDD TKIWPREQFP WRHVGQMTLN RNPENVFAET EQAAFGTGVL VDGLDFSDDK 

       370        380        390        400        410        420 
MLQGRTFSYS DTQRYRVGPN YLQLPINAPK KHVATNQRDG QMAYRVDTFE GQDQRVNYEP 

       430        440        450        460        470        480 
SLLSGPKEAP RRAPEHTPRV EGNLVRAAIE RPNPFGQAGM QYRNFADWER DELVSNLSGA 

       490        500        510        520        530 
LAGVDKRIQD KMLEYFTAAD ADYGQRVREG IQAKEAEMKG QKQEAPVYGT EASSLY 

« Hide

References

« Hide 'large scale' references
[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]"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1."
White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D., Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L., Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M., Vamathevan J.J., Lam P. expand/collapse author list , McDonald L.A., Utterback T.R., Zalewski C., Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D., Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C., Fraser C.M.
Science 286:1571-1577(1999) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D63898 Genomic DNA. Translation: BAA09937.1.
AE000513 Genomic DNA. Translation: AAF11546.1.
PIRB75329.
RefSeqNP_295721.1. NC_001263.1.

3D structure databases

ProteinModelPortalQ59337.
SMRQ59337. Positions 32-515.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243230.DR_1998.

Proteomic databases

PRIDEQ59337.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF11546; AAF11546; DR_1998.
GeneID1800077.
KEGGdra:DR_1998.
PATRIC21631656. VBIDeiRad64572_2221.

Phylogenomic databases

eggNOGCOG0753.
HOGENOMHOG000087852.
KOK03781.
OMAEATTMIM.
OrthoDBEOG6P5Z9F.

Enzyme and pathway databases

BioCycDRAD243230:GH46-2032-MONOMER.

Family and domain databases

Gene3D2.40.180.10. 1 hit.
InterProIPR018028. Catalase.
IPR020835. Catalase-like_dom.
IPR024711. Catalase_clade1/3.
IPR011614. Catalase_core.
IPR002226. Catalase_haem_BS.
IPR010582. Catalase_immune_responsive.
[Graphical view]
PANTHERPTHR11465. PTHR11465. 1 hit.
PfamPF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]
PIRSFPIRSF038928. Catalase_clade1-3. 1 hit.
PRINTSPR00067. CATALASE.
SMARTSM01060. Catalase. 1 hit.
[Graphical view]
SUPFAMSSF56634. SSF56634. 1 hit.
PROSITEPS00437. CATALASE_1. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCATA_DEIRA
AccessionPrimary (citable) accession number: Q59337
Entry history
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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families