Reviewed, UniProtKB/Swiss-Prot P17336 (CATA_DROME)

Names and origin

Protein names

Recommended name:
    Catalase
    EC=1.11.1.6

Gene names

Name:	Cat
ORF Names:	CG6871

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	506 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic activity	2 H2O2 = O2 + 2 H2O.
Cofactor	Heme group.
Subunit structure	Homotetramer.
Subcellular location	Peroxisome.
Sequence similarities	Belongs to the catalase family.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Peroxisome
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	determination of adult life span Traceable author statement. Source: FlyBase hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	peroxisome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	catalase activity Inferred from direct assay. Source: FlyBase heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 506	506	Catalase		PRO_0000084912
Regions
	Motif	504 – 506	3	Microbody targeting signal Potential
Sites
	Active site	73	1	By similarity
	Active site	146	1	By similarity
	Metal binding	356	1	Iron (heme axial ligand) By similarity
Experimental info
	Sequence conflict	5	1	D → Y Ref.1
	Sequence conflict	12	1	I → N Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P17336-1 [UniParc]. Last modified October 1, 1996. Version 2. Checksum: 396377DC5F784ECE	FASTA	506	57,150
	10 20 30 40 50 60 MAGRDAASNQ LIDYKNSQTV SPGAITTGNG APIGIKDASQ TVGPRGPILL QDVNFLDEMS 70 80 90 100 110 120 HFDRERIPER VVHAKGAGAF GYFEVTHDIT QYCAAKIFDK VKKRTPLAVR FSTVGGESGS 130 140 150 160 170 180 ADTARDPRGF AVKFYTEDGV WDLVGNNTPV FFIRDPILFP SFIHTQKRNP QTHLKDPDMF 190 200 210 220 230 240 WDFLTLRPES AHQVCILFSD RGTPDGYCHM NGYGSHTFKL INAKGEPIYA KFHFKTDQGI 250 260 270 280 290 300 KNLDVKTADQ LASTDPDYSI RDLYNRIKTC KFPSWTMYIQ VMTYEQAKKF KYNPFDVTKV 310 320 330 340 350 360 WSQKEYPLIP VGKMVLDRNP KNYFAEVEQI AFSPAHLVPG VEPSPDKMLH GRLFSYSDTH 370 380 390 400 410 420 RHRLGPNYLQ IPVNCPYKVK IENFQRDGAM NVTDNQDGAP NYFPNSFNGP QECPRARALS 430 440 450 460 470 480 SCCPVTGDVY RYSSGDTEDN FGQVTDFWVH VLDKCAKKRL VQNIAGHLSN ASQFLQERAV 490 500 KNFTQVHADF GRMLTEELNL AKSSKF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular analysis of the Drosophila catalase gene." Orr W.C., Orr E.C., Legan S.K., Sohal R.S. Arch. Biochem. Biophys. 330:251-258(1996) [PubMed: 8660653] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"cDNA and deduced amino acid sequence of Drosophila catalase." Orr E.C., Bewley G.C., Orr W.C. Nucleic Acids Res. 18:3663-3663(1990) [PubMed: 2362827] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[4]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[5]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Embryo.
[6]	"Identification of Drosophila wing imaginal disc proteins by two-dimensional gel analysis and microsequencing." Santaren J.F., van Damme J., Puype M., Vandekerckhove J., Garcia-Bellido A. Exp. Cell Res. 206:220-226(1993) [PubMed: 8500545] [Abstract] Cited for: PROTEIN SEQUENCE OF 76-92. Strain: Vallecas. Tissue: Wing imaginal disk.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	U00145 Genomic DNA. Translation: AAC13738.1. X52286 mRNA. Translation: CAA36529.1. Sequence problems. AE014296 Genomic DNA. Translation: AAF49228.1. AY084154 mRNA. Translation: AAL89892.1.
PIR	CSFF. S12725.
RefSeq	NP_536731.1.
UniGene	Dm.6950
3D structure databases
HSSP	HSSP built from PDB template 1F4J based on UniProtKB P04040.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:18768N.
IntAct	P17336. 3 interactions.
Genome annotation databases
Ensembl	FBgn0000261. Drosophila melanogaster. [Contig view]
GeneID	40048.
KEGG	dme:Dmel_CG6871.
NMPDR	fig|7227.3.peg.10459.
Organism-specific databases
FlyBase	FBgn0000261. Cat.
Phylogenomic databases
HOGENOM	P17336.
OMA	P17336. NCPFRAR.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-017262-MON.
BRENDA	1.11.1.6. 48.
Gene expression databases
ArrayExpress	P17336.
GermOnline	CG6871. Drosophila melanogaster.
Family and domain databases
InterPro	IPR002226. Catalase. IPR010582. Catalase-rel_immune_responsive. IPR011614. Catalase_N. IPR018028. Catalase_rel_subgroup. [Graphical view]
Gene3D	G3DSA:2.40.180.10. Catalase_N. 1 hit.
PANTHER	PTHR11465. Catalase. 1 hit.
Pfam	PF00199. Catalase. 1 hit. PF06628. Catalase-rel. 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. PS00438. CATALASE_2. 1 hit. PS51402. CATALASE_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	816735.

Entry information

Entry name

CATA_DROME

Accession

Primary (citable) accession number: P17336
Secondary accession number(s): Q9VVT1

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1990
Last sequence update:	October 1, 1996
Last modified:	June 16, 2009
This is version 89 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project