CATA_YEAST
ID CATA_YEAST Reviewed; 515 AA.
AC P15202; D6VSN6; E9P947;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=Peroxisomal catalase A;
DE EC=1.11.1.6;
GN Name=CTA1; OrderedLocusNames=YDR256C; ORFNames=YD9320A.06C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3046940; DOI=10.1111/j.1432-1033.1988.tb14263.x;
RA Cohen G., Rapatz W., Ruis H.;
RT "Sequence of the Saccharomyces cerevisiae CTA1 gene and amino acid sequence
RT of catalase A derived from it.";
RL Eur. J. Biochem. 176:159-163(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169867;
RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., Paulin L.,
RA Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., Prydz H.,
RA Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., Rieger M.,
RA Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., Scharfe M.,
RA Schmidt E.R., Schneider C., Scholler P., Schwarz S., Soler-Mira A.,
RA Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., Volckaert G.,
RA Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., Harris D.E.,
RA Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., Gentles S.,
RA Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., Niblett D.,
RA Odell C., Oliver K., Rajandream M.A., Richards C., Shore L., Walsh S.V.,
RA Barrell B.G., Dietrich F.S., Mulligan J.T., Allen E., Araujo R., Aviles E.,
RA Berno A., Carpenter J., Chen E., Cherry J.M., Chung E., Duncan M.,
RA Hunicke-Smith S., Hyman R.W., Komp C., Lashkari D., Lew H., Lin D.,
RA Mosedale D., Nakahara K., Namath A., Oefner P., Oh C., Petel F.X.,
RA Roberts D., Schramm S., Schroeder M., Shogren T., Shroff N., Winant A.,
RA Yelton M.A., Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., Greco T.,
RA Hallsworth K., Hawkins J., Hillier L.W., Jier M., Johnson D., Johnston L.,
RA Kirsten J., Kucaba T., Langston Y., Latreille P., Le T., Mardis E.,
RA Menezes S., Miller N., Nhan M., Pauley A., Peluso D., Rifkin L., Riles L.,
RA Taich A., Trevaskis E., Vignati D., Wilcox L., Wohldman P., Vaudin M.,
RA Wilson R., Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
RA Mewes H.-W., Zollner A., Zaccaria P.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
RL Nature 387:75-78(1997).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=17322287; DOI=10.1101/gr.6037607;
RA Hu Y., Rolfs A., Bhullar B., Murthy T.V.S., Zhu C., Berger M.F.,
RA Camargo A.A., Kelley F., McCarron S., Jepson D., Richardson A., Raphael J.,
RA Moreira D., Taycher E., Zuo D., Mohr S., Kane M.F., Williamson J.,
RA Simpson A.J.G., Bulyk M.L., Harlow E., Marsischky G., Kolodner R.D.,
RA LaBaer J.;
RT "Approaching a complete repository of sequence-verified protein-encoding
RT clones for Saccharomyces cerevisiae.";
RL Genome Res. 17:536-543(2007).
RN [5]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), ACTIVE SITES, AND COFACTOR.
RX PubMed=9931255; DOI=10.1006/jmbi.1998.2453;
RA Mate M.J., Zamocky M., Nykyri L.M., Herzog C., Alzari P.M., Betzel C.,
RA Koller F., Fita I.;
RT "Structure of catalase-A from Saccharomyces cerevisiae.";
RL J. Mol. Biol. 286:135-149(1999).
CC -!- FUNCTION: Occurs in almost all aerobically respiring organisms and
CC serves to protect cells from the toxic effects of hydrogen peroxide.
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 Evidence={ECO:0000269|PubMed:9931255};
CC -!- SUBUNIT: Homotetramer.
CC -!- INTERACTION:
CC P15202; P39940: RSP5; NbExp=2; IntAct=EBI-4061, EBI-16219;
CC -!- SUBCELLULAR LOCATION: Peroxisome.
CC -!- MISCELLANEOUS: This is one of two catalases in S.cerevisiae; the other
CC is catalase T, which is the cytoplasmic form.
CC -!- MISCELLANEOUS: Present with 623 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; X13028; CAA31443.1; -; Genomic_DNA.
DR EMBL; Z68329; CAA92713.1; -; Genomic_DNA.
DR EMBL; Z70202; CAA94095.1; -; Genomic_DNA.
DR EMBL; AY723786; AAU09703.1; -; Genomic_DNA.
DR EMBL; BK006938; DAA12096.1; -; Genomic_DNA.
DR PIR; S07868; CSBYP.
DR RefSeq; NP_010542.1; NM_001180564.1.
DR PDB; 1A4E; X-ray; 2.40 A; A/B/C/D=15-502.
DR PDBsum; 1A4E; -.
DR AlphaFoldDB; P15202; -.
DR SMR; P15202; -.
DR BioGRID; 32306; 60.
DR DIP; DIP-4320N; -.
DR IntAct; P15202; 8.
DR MINT; P15202; -.
DR STRING; 4932.YDR256C; -.
DR PeroxiBase; 5175; SceKat01.
DR iPTMnet; P15202; -.
DR PaxDb; P15202; -.
DR PRIDE; P15202; -.
DR EnsemblFungi; YDR256C_mRNA; YDR256C; YDR256C.
DR GeneID; 851843; -.
DR KEGG; sce:YDR256C; -.
DR SGD; S000002664; CTA1.
DR VEuPathDB; FungiDB:YDR256C; -.
DR eggNOG; KOG0047; Eukaryota.
DR GeneTree; ENSGT00390000018100; -.
DR HOGENOM; CLU_010645_2_0_1; -.
DR InParanoid; P15202; -.
DR OMA; WTCYVQV; -.
DR BioCyc; YEAST:YDR256C-MON; -.
DR Reactome; R-SCE-3299685; Detoxification of Reactive Oxygen Species.
DR Reactome; R-SCE-6798695; Neutrophil degranulation.
DR Reactome; R-SCE-9033241; Peroxisomal protein import.
DR EvolutionaryTrace; P15202; -.
DR PRO; PR:P15202; -.
DR Proteomes; UP000002311; Chromosome IV.
DR RNAct; P15202; protein.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005782; C:peroxisomal matrix; IDA:SGD.
DR GO; GO:0005777; C:peroxisome; IBA:GO_Central.
DR GO; GO:0004096; F:catalase activity; IDA:SGD.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001315; P:age-dependent response to reactive oxygen species; IMP:SGD.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IDA:SGD.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
DR GO; GO:0000302; P:response to reactive oxygen species; IMP:SGD.
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 1: Evidence at protein level;
KW 3D-structure; Acetylation; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW Oxidoreductase; Peroxidase; Peroxisome; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..515
FT /note="Peroxisomal catalase A"
FT /id="PRO_0000084928"
FT MOTIF 513..515
FT /note="Microbody targeting signal"
FT /evidence="ECO:0000255"
FT ACT_SITE 70
FT /evidence="ECO:0000269|PubMed:9931255"
FT ACT_SITE 143
FT /evidence="ECO:0000269|PubMed:9931255"
FT BINDING 355
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:0000269|PubMed:9931255"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CONFLICT 131
FT /note="F -> L (in Ref. 4; AAU09703)"
FT /evidence="ECO:0000305"
FT STRAND 31..34
FT /evidence="ECO:0007829|PDB:1A4E"
FT STRAND 36..39
FT /evidence="ECO:0007829|PDB:1A4E"
FT TURN 40..42
FT /evidence="ECO:0007829|PDB:1A4E"
FT HELIX 50..59
FT /evidence="ECO:0007829|PDB:1A4E"
FT STRAND 72..82
FT /evidence="ECO:0007829|PDB:1A4E"
FT TURN 87..89
FT /evidence="ECO:0007829|PDB:1A4E"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:1A4E"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:1A4E"
FT STRAND 111..113
FT /evidence="ECO:0007829|PDB:1A4E"
FT STRAND 119..123
FT /evidence="ECO:0007829|PDB:1A4E"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:1A4E"
FT STRAND 136..147
FT /evidence="ECO:0007829|PDB:1A4E"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:1A4E"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:1A4E"
FT HELIX 174..181
FT /evidence="ECO:0007829|PDB:1A4E"
FT HELIX 184..189
FT /evidence="ECO:0007829|PDB:1A4E"
FT HELIX 190..197
FT /evidence="ECO:0007829|PDB:1A4E"
FT HELIX 199..201
FT /evidence="ECO:0007829|PDB:1A4E"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:1A4E"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:1A4E"
FT STRAND 217..220
FT /evidence="ECO:0007829|PDB:1A4E"
FT STRAND 226..237
FT /evidence="ECO:0007829|PDB:1A4E"
FT HELIX 244..253
FT /evidence="ECO:0007829|PDB:1A4E"
FT HELIX 257..267
FT /evidence="ECO:0007829|PDB:1A4E"
FT STRAND 273..281
FT /evidence="ECO:0007829|PDB:1A4E"
FT HELIX 283..287
FT /evidence="ECO:0007829|PDB:1A4E"
FT STRAND 289..291
FT /evidence="ECO:0007829|PDB:1A4E"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:1A4E"
FT STRAND 308..317
FT /evidence="ECO:0007829|PDB:1A4E"
FT HELIX 322..325
FT /evidence="ECO:0007829|PDB:1A4E"
FT TURN 326..328
FT /evidence="ECO:0007829|PDB:1A4E"
FT STRAND 340..342
FT /evidence="ECO:0007829|PDB:1A4E"
FT HELIX 346..362
FT /evidence="ECO:0007829|PDB:1A4E"
FT HELIX 367..369
FT /evidence="ECO:0007829|PDB:1A4E"
FT HELIX 371..373
FT /evidence="ECO:0007829|PDB:1A4E"
FT TURN 395..398
FT /evidence="ECO:0007829|PDB:1A4E"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:1A4E"
FT STRAND 429..432
FT /evidence="ECO:0007829|PDB:1A4E"
FT STRAND 438..440
FT /evidence="ECO:0007829|PDB:1A4E"
FT HELIX 441..454
FT /evidence="ECO:0007829|PDB:1A4E"
FT HELIX 459..471
FT /evidence="ECO:0007829|PDB:1A4E"
FT HELIX 476..487
FT /evidence="ECO:0007829|PDB:1A4E"
FT HELIX 491..501
FT /evidence="ECO:0007829|PDB:1A4E"
SQ SEQUENCE 515 AA; 58555 MW; 22DFCC599D79801F CRC64;
MSKLGQEKNE VNYSDVREDR VVTNSTGNPI NEPFVTQRIG EHGPLLLQDY NLIDSLAHFN
RENIPQRNPH AHGSGAFGYF EVTDDITDIC GSAMFSKIGK RTKCLTRFST VGGDKGSADT
VRDPRGFATK FYTEEGNLDW VYNNTPVFFI RDPSKFPHFI HTQKRNPQTN LRDADMFWDF
LTTPENQVAI HQVMILFSDR GTPANYRSMH GYSGHTYKWS NKNGDWHYVQ VHIKTDQGIK
NLTIEEATKI AGSNPDYCQQ DLFEAIQNGN YPSWTVYIQT MTERDAKKLP FSVFDLTKVW
PQGQFPLRRV GKIVLNENPL NFFAQVEQAA FAPSTTVPYQ EASADPVLQA RLFSYADAHR
YRLGPNFHQI PVNCPYASKF FNPAIRDGPM NVNGNFGSEP TYLANDKSYT YIQQDRPIQQ
HQEVWNGPAI PYHWATSPGD VDFVQARNLY RVLGKQPGQQ KNLAYNIGIH VEGACPQIQQ
RVYDMFARVD KGLSEAIKKV AEAKHASELS SNSKF
