CATA_CANAL
ID CATA_CANAL Reviewed; 485 AA.
AC O13289; A0A1D8PDX2; O42616; Q5AAT2; Q9URJ7;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 5.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Peroxisomal catalase;
DE EC=1.11.1.6;
GN Name=CAT1; Synonyms=CTA1; OrderedLocusNames=CAALFM_C106810WA;
GN ORFNames=CaO19.13609, CaO19.6229;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 10261 / CBS 2718 / NBRC 1061;
RX PubMed=9573075; DOI=10.1128/iai.66.5.1953-1961.1998;
RA Wysong D.R., Christin L., Sugar A.M., Robbins P.W., Diamond R.D.;
RT "Cloning and sequencing of a Candida albicans catalase gene and effects of
RT disruption of this gene.";
RL Infect. Immun. 66:1953-1961(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND FUNCTION.
RC STRAIN=FC18;
RX PubMed=18352908; DOI=10.1111/j.1348-0421.2008.00006.x;
RA Nakagawa Y.;
RT "Catalase gene disruptant of the human pathogenic yeast Candida albicans is
RT defective in hyphal growth, and a catalase-specific inhibitor can suppress
RT hyphal growth of wild-type cells.";
RL Microbiol. Immunol. 52:16-24(2008).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
CC Required for hyphal growth. {ECO:0000269|PubMed:18352908}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10013};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; U40704; AAC39448.1; -; Genomic_DNA.
DR EMBL; AB006327; BAA21767.1; -; mRNA.
DR EMBL; AB006328; BAA21768.1; -; Genomic_DNA.
DR EMBL; CP017623; AOW26336.1; -; Genomic_DNA.
DR RefSeq; XP_718818.1; XM_713725.2.
DR AlphaFoldDB; O13289; -.
DR SMR; O13289; -.
DR BioGRID; 1222589; 1.
DR STRING; 237561.O13289; -.
DR MoonDB; O13289; Curated.
DR MoonProt; O13289; -.
DR PeroxiBase; 5253; CalKat01.
DR PRIDE; O13289; -.
DR GeneID; 3639495; -.
DR KEGG; cal:CAALFM_C106810WA; -.
DR CGD; CAL0000188148; CAT1.
DR VEuPathDB; FungiDB:C1_06810W_A; -.
DR eggNOG; KOG0047; Eukaryota.
DR HOGENOM; CLU_010645_2_0_1; -.
DR InParanoid; O13289; -.
DR OMA; WTCYVQV; -.
DR OrthoDB; 507937at2759; -.
DR PHI-base; PHI:106; -.
DR PHI-base; PHI:7209; -.
DR PRO; PR:O13289; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0009277; C:fungal-type cell wall; IDA:CAFA.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0004096; F:catalase activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051701; P:biological process involved in interaction with host; IDA:CAFA.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024711; Catalase_clade1/3.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR020835; Catalase_sf.
DR PANTHER; PTHR11465; PTHR11465; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF56634; SSF56634; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS00438; CATALASE_2; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 2: Evidence at transcript level;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Peroxisome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..485
FT /note="Peroxisomal catalase"
FT /id="PRO_0000084918"
FT ACT_SITE 53
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 126
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT BINDING 336
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000250"
FT CONFLICT 114
FT /note="F -> I (in Ref. 1; AAC39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 224
FT /note="T -> N (in Ref. 1; AAC39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="K -> R (in Ref. 1; AAC39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="L -> M (in Ref. 1; AAC39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="K -> E (in Ref. 1; AAC39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="R -> RP (in Ref. 1; AAC39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 366
FT /note="M -> S (in Ref. 1; AAC39448)"
FT /evidence="ECO:0000305"
FT CONFLICT 397
FT /note="L -> SF (in Ref. 1; AAC39448)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 485 AA; 54863 MW; A9E25AD096390C55 CRC64;
MAPTFTNSNG QPIPEPFATQ RVGQHGPLLL QDFNLIDSLA HFDRERIPER VVHAKGSGAY
GVFEVTDDIT DICAAKFLDT VGKKTRIFTR FSTVGGELGS ADTARDPRGF ATKFYTEEGN
LDLVYNNTPV FFIRDPSKFP HFIHTQKRNP ETHLKDANMF WDYLTSNEES IHQVMVLFSD
RGTPASYREM NGYSGHTYKW SNKKGEWFYV QVHFISDQGI KTLTNEEAGA LAGSNPDYAQ
EDLFKNIAAG NYPSWTAYIQ TMTEAEAKEA EFSVFDLTKV WPHKKYPLRR FGKFTLNENP
KNYFAEVEQA AFSPAHTVPY MEPSADPVLQ SRLFSYADTH RHRLGTNYTQ IPVNCPVTGA
VFNPHMRDGA MTVNGNLGSH PNYLASDKPV EFKQFSLQED QEVWNGAATP FHWKATPADF
KQAQELWKVL KRYPNQQEHL AHNIAVHAAG ADAAIQDRVF AYFGKVSQDL ADAIKKEVLE
LSPRK
