O77229 (CATA_DICDI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Catalase-A
EC=1.11.1.6

Gene names

Name:	catA
Synonyms:	cat
ORF Names:	DDB_G0274595

Organism

Dictyostelium discoideum (Slime mold)

Taxonomic identifier

44689 [NCBI]

Taxonomic lineage

Eukaryota › Amoebozoa › Mycetozoa › Dictyosteliida › Dictyostelium

Protein attributes

Sequence length	496 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level

General annotation (Comments)

Function	Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Ref.4
Catalytic activity	2 H2O2 = O2 + 2 H2O.
Cofactor	Heme group By similarity.
Subcellular location	Peroxisome By similarity.
Developmental stage	Expressed throughout growth and development. Exclusively localized in the prestalk cells. Ref.1
Disruption phenotype	Cells are resistant to methanol, acriflavine and thiabendazole. Ref.4
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 Reference proteome
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from direct assay Ref.1. Source: dictyBase response to methanol Inferred from mutant phenotype Ref.4. Source: dictyBase
Cellular component	peroxisome Inferred from direct assay Ref.1. Source: dictyBase phagocytic vesicle Inferred from direct assay. Source: dictyBase
Molecular function	catalase activity Inferred from direct assay Ref.1. Source: dictyBase 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 – 496	496	Catalase-A		PRO_0000084911
Regions
	Motif	494 – 496	3	Microbody targeting signal Potential
Sites
	Active site	54	1	By similarity
	Active site	128	1	By similarity
	Metal binding	338	1	Iron (heme axial ligand) By similarity
Experimental info
	Sequence conflict	67	1	P → T in AAC36743. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O77229 [UniParc]. Last modified December 4, 2007. Version 2. Checksum: 254CA4D38E698C9F	FASTA	496	55,680
	10 20 30 40 50 60 MSAPVLTTSS GSPIDNNLNS MTAGVNGPIL IQDFTLIDKL AHFDRERIPE RVVHAKGAGA 70 80 90 100 110 120 HGYFEVPSSD VPKWCKAKFL NKVGKRTPIF TRFSTVGGEK GSSDSERDPR GFAVKFYTEE 130 140 150 160 170 180 GNFDMVGNNT PVFFIRDPSK FPDFIHTQKR NPQTNCKDPN MFWDFLGQTP ESTHQVSILF 190 200 210 220 230 240 SDRGTPKSYR HMHGFSSHTL KFVNAQGKPY WVKLHFTSET GIQNYTAEEA AKMSMNDPDS 250 260 270 280 290 300 ATRDLFETIA KGGEPAWKVS IQLMEFEDAL KYRFNPFDVT KIWSHKDYPL IQIGRMVLNR 310 320 330 340 350 360 NPENYFAEVE QAAFSPSHMV PGIEPSPDKM LQGRLFSYPD THRHRLGVNY QQIPVNCPFA 370 380 390 400 410 420 VKGGVKNYQR DGFMAVNGNG GKGPNYQPNS FGGPEPHPEF AQHKFDVSGF AARQPYNHPN 430 440 450 460 470 480 DDFVQPGDLY RLMSEDAKSR FVSNLVGHMS GVTIKEIQVR AVSNFYKADK DLGARLCKGL 490 GIDVNDVIKF AARSNL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Differential developmental expression and cell type specificity of Dictyostelium catalases and their response to oxidative stress and UV-light." Garcia M.X.U., Foote C., van Es S., Devreotes P.N., Alexander S., Alexander H. Biochim. Biophys. Acta 1492:295-310(2000) [PubMed: 11004503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE. Strain: AX3.
[2]	"Sequence and analysis of chromosome 2 of Dictyostelium discoideum." Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T., Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R., Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A., Noegel A.A. Nature 418:79-85(2002) [PubMed: 12097910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[3]	"The genome of the social amoeba Dictyostelium discoideum." Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R., Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B., Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T., Lehmann R., Hamlin N. , Davies R., Gaudet P., Fey P., Pilcher K., Chen G., Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N., Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E., Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N., Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D., Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T., Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D., Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A., Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M., Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A., Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y., Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C., Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R., Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A. Nature 435:43-57(2005) [PubMed: 15875012] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: AX4.
[4]	"Methanol and acriflavine resistance in Dictyostelium are caused by loss of catalase." Garcia M.X.U., Roberts C., Alexander H., Stewart A.M., Harwood A., Alexander S., Insall R.H. Microbiology 148:333-340(2002) [PubMed: 11782526] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF090443 mRNA. Translation: AAC36743.1. AAFI02000012 Genomic DNA. Translation: EAL70190.1.
RefSeq	XP_643894.1. XM_638802.1.
3D structure databases
ProteinModelPortal	O77229.
SMR	O77229. Positions 2-481.
ModBase	Search...
Protein-protein interaction databases
STRING	O77229.
Protein family/group databases
PeroxiBase	4096. DdKat01.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblProtists	DDB0185123; DDB0185123; DDB_G0274595.
GeneID	8619320.
GenomeReviews	Gene locus catA in contig CM000151_GR.
KEGG	ddi:DDB_G0274595.
Organism-specific databases
dictyBase	DDB_G0274595. catA.
Phylogenomic databases
eggNOG	KOG0047.
GeneTree	EPrGT00050000005287.
HOGENOM	HBG339355.
OMA	VEPANFA.
PhylomeDB	O77229.
ProtClustDB	CLSZ2430996.
Family and domain databases
InterPro	IPR018028. Catalase. IPR020835. Catalase-like_dom. IPR024708. Catalase_AS. IPR024711. Catalase_clade1/3. IPR011614. Catalase_core. IPR002226. Catalase_haem_BS. IPR010582. Catalase_immune_responsive. [Graphical view]
Gene3D	G3DSA:2.40.180.10. Catalase_N. 1 hit.
KO	K03781.
PANTHER	PTHR11465. Catalase. 1 hit.
Pfam	PF00199. Catalase. 1 hit. PF06628. Catalase-rel. 1 hit. [Graphical view]
PIRSF	PIRSF038928. Catalase_clade1-3. 1 hit.
PRINTS	PR00067. CATALASE.
SMART	SM01060. Catalase. 1 hit. [Graphical view]
SUPFAM	SSF56634. Catalase_N. 1 hit.
PROSITE	PS00437. CATALASE_1. 1 hit. PS00438. CATALASE_2. 1 hit. PS51402. CATALASE_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CATA_DICDI

Accession

Primary (citable) accession number: O77229
Secondary accession number(s): Q556B6, Q86A71

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 4, 2007
Last modified:	January 25, 2012
This is version 71 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)