Reviewed, UniProtKB/Swiss-Prot Q59337 (CATA_DEIRA)

Names and origin

Protein names

Recommended name:
    Catalase
    EC=1.11.1.6

Gene names

Name:	katA
Ordered Locus Names:	DR_1998

Organism

Deinococcus radiodurans [Complete proteome] [HAMAP]

Taxonomic identifier

1299 [NCBI]

Taxonomic lineage

Bacteria › Deinococcus-Thermus › Deinococci › Deinococcales › Deinococcaceae › Deinococcus

Protein attributes

Sequence length	536 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
Catalytic activity	2 H(2)O(2) = O(2) + 2 H(2)O.
Cofactor	Heme group.
Enzyme regulation	Strongly inhibited by sodium azide and sodium cyanide, and sligthly inhibited by 3-amino-1,2,4-triazole.
Subunit structure	Homotetramer.
Subcellular location	CytoplasmProbable.
Developmental stage	Up-regulated during stationary phase.
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.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Cytoplasm
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	catalase activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 536	536	Catalase		PRO_0000085014
Sites
	Active site	81	1	By similarity
	Active site	159	1	By similarity
	Metal binding	369	1	Iron (heme axial ligand) By similarity
Experimental info
	Sequence conflict	152	1	G → A in BAA09937. Ref.1
	Sequence conflict	156 – 158	3	LVG → FVV in BAA09937. Ref.1
	Sequence conflict	277	1	H → R in BAA09937. Ref.1
	Sequence conflict	293	1	Q → K in BAA09937. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q59337-1 [UniParc]. Last modified May 30, 2000. Version 2. Checksum: 6A60CB6A8F445A59	FASTA	536	60,513
	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

References

	« Hide 'large scale' referencesShow '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 / IFO 15346 / LMG 4051 / NCIB 9279 / R1.
[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. , 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: 10567266] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 13939 / DSM 20539 / IFO 15346 / LMG 4051 / NCIB 9279 / R1.
[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: 7720013] [Abstract] Cited for: DEVELOPMENTAL STAGE. Strain: ATCC 13939 / DSM 20539 / IFO 15346 / LMG 4051 / NCIB 9279 / R1.
[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: 16716939] [Abstract] Cited for: FUNCTION, COFACTOR, SUBUNIT, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES. Strain: KR1.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D63898 Genomic DNA. Translation: BAA09937.1. AE000513 Genomic DNA. Translation: AAF11546.1.
PIR	B75329.
RefSeq	NP_295721.1.
3D structure databases
HSSP	HSSP built from PDB template 1M7S based on UniProtKB P46206.
ModBase	Search...
Genome annotation databases
GeneID	1800077.
GenomeReviews	Gene locus DR_1998 in contig AE000513_GR.
KEGG	dra:DR_1998.
NMPDR	fig|243230.1.peg.2180.
TIGR	DR_1998.
Phylogenomic databases
HOGENOM	Q59337.
Enzyme and pathway databases
BioCyc	DRAD243230:DR_1998-MON.
Family and domain databases
InterPro	IPR002226. Catalase. IPR011614. Catalase_N. [Graphical view]
Gene3D	G3DSA:2.40.180.10. Catalase_N. 1 hit.
PANTHER	PTHR11465. Catalase. 1 hit.
Pfam	PF00199. Catalase. 1 hit. [Graphical view]
PRINTS	PR00067. CATALASE.
ProDom	PD000510. Catalase. 1 hit. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00437. CATALASE_1. 1 hit. PS51402. CATALASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CATA_DEIRA

Accession

Primary (citable) accession number: Q59337

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 30, 2000
Last modified:	November 25, 2008
This is version 65 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)