ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q59337

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name CATA_DEIRA
Primary accession number Q59337
Secondary accession numbers None
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on May 30, 2000 (Sequence version 2)
Annotations were last modified on    September 2, 2008 (Entry version 62)
Name and origin of the protein
Protein name Catalase
Synonym EC 1.11.1.6
Gene name
Name: katA
OrderedLocusNames: DR_1998
From
Deinococcus radiodurans [TaxID: 1299] [HAMAP proteome]
Taxonomy Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae; Deinococcus.
Protein existence 1: Evidence at protein level;
References
[1]
 NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 13939 / DSM 20539 / IFO 15346 / LMG 4051 / NCIB 9279 / R1;
Narumi I., Watanabe H., Hossain A., Tanaka A., Kitayama S.;
"Molecular cloning and nucleotide sequence of radiation-inducible catalase gene from radioresistant bacterium, Deinococcus radiodurans.";
Submitted (AUG-1995) to the EMBL/GenBank/DDBJ databases.
[2]
 NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13939 / DSM 20539 / IFO 15346 / LMG 4051 / NCIB 9279 / R1;
DOI=10.1126/science.286.5444.1571; PubMed=10567266 [NCBI, ExPASy, EBI, Israel, Japan]
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., 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.;
"Genome sequence of the radioresistant bacterium Deinococcus radiodurans R1.";
Science 286:1571-1577(1999).
[3]
 DEVELOPMENTAL STAGE.
STRAIN=ATCC 13939 / DSM 20539 / IFO 15346 / LMG 4051 / NCIB 9279 / R1;
PubMed=7720013 [NCBI, ExPASy, EBI, Israel, Japan]
Wang P., Schellhorn H.E.;
"Induction of resistance to hydrogen peroxide and radiation in Deinococcus radiodurans.";
Can. J. Microbiol. 41:170-176(1995).
[4]
 FUNCTION, COFACTOR, SUBUNIT, ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
STRAIN=KR1;
DOI=10.1263/jbb.101.315; PubMed=16716939 [NCBI, ExPASy, EBI, Israel, Japan]
Kobayashi I., Tamura T., Sghaier H., Narumi I., Yamaguchi S., Umeda K., Inagaki K.;
"Characterization of monofunctional catalase KatA from radioresistant bacterium Deinococcus radiodurans.";
J. Biosci. Bioeng. 101:315-321(2006).
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.
  • ENZYME REGULATION: Strongly inhibited by sodium azide and sodium cyanide, and sligthly inhibited by 3-amino-1,2,4-triazole.
  • 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;
  • SUBUNIT: Homotetramer.
  • SUBCELLULAR LOCATION: Cytoplasm (Probable).
  • DEVELOPMENTAL STAGE: Up-regulated during stationary phase.
  • SIMILARITY: Belongs to the catalase family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D63898; BAA09937.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AE000513; AAF11546.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR B75329; B75329.
RefSeq NP_295721.1; -.
3D structure databases
HSSP P46206; 1M7S. [HSSP ENTRY / PDB]
ModBase Q59337.
Enzyme and pathway databases
BioCyc DRAD243230:DR_1998-MON; -.
Family and domain databases
InterPro IPR002226; Catalase.
IPR011614; Catalase_N.
Graphical view of domain structure.
Gene3D G3DSA:2.40.180.10; Catalase_N; 1.
PANTHER PTHR11465; Catalase; 1.
Pfam PF00199; Catalase; 1.
Pfam graphical view of domain structure.
PRINTS PR00067; CATALASE.
ProDom PD000510; Catalase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00437; CATALASE_1; 1.
BLOCKS Q59337.
Genome annotation databases
GeneID 1800077; -.
GenomeReviews AE000513_GR; DR_1998.
KEGG dra:DR_1998; -.
NMPDR fig|243230.1.peg.2180; -.
TIGR DR_1998; -.
Phylogenomic databases
HOGENOM Q59337; -.
Other
ProtoNet Q59337.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Complete proteome; Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   536  536     Catalase. PRO_0000085014
ACT_SITE   81    81        By similarity. 
ACT_SITE   159   159        By similarity. 
METAL   369   369        Iron (heme axial ligand) (By similarity). 
CONFLICT   152   152        G -> A (in Ref. 1; BAA09937). 
CONFLICT   156   158        LVG -> FVV (in Ref. 1; BAA09937). 
CONFLICT   277   277        H -> R (in Ref. 1; BAA09937). 
CONFLICT   293   293        Q -> K (in Ref. 1; BAA09937). 
Sequence information
Length: 536 AA [This is the length of the unprocessed precursor] Molecular weight: 60513 Da [This is the MW of the unprocessed precursor] CRC64: 6A60CB6A8F445A59 [This is a checksum on the sequence] 
        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
Q59337 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA) 		Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Hosted by ca flag CBR Canada Mirror sites: Australia Brazil China Korea Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!