ID   CATA2_ARATH             Reviewed;         492 AA.
AC   P25819; O49615;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   13-DEC-2001, sequence version 3.
DT   24-JAN-2024, entry version 190.
DE   RecName: Full=Catalase-2;
DE            EC=1.11.1.6;
GN   Name=CAT2; Synonyms=CAT; OrderedLocusNames=At4g35090;
GN   ORFNames=M4E13.140;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=16669103; DOI=10.1104/pp.99.4.1726;
RA   Chevalier C., Yamaguchi J., McCourt P.;
RT   "Nucleotide sequence of a cDNA for catalase from Arabidopsis thaliana.";
RL   Plant Physiol. 99:1726-1728(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=cv. Landsberg erecta;
RA   Zentgraf U., Zinkernagel I.;
RT   "A gene encoding a catalase isoform from Arabidopsis thaliana.";
RL   (er) Plant Gene Register PGR96-005(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=17951448; DOI=10.1105/tpc.107.050989;
RA   Reumann S., Babujee L., Ma C., Wienkoop S., Siemsen T., Antonicelli G.E.,
RA   Rasche N., Lueder F., Weckwerth W., Jahn O.;
RT   "Proteome analysis of Arabidopsis leaf peroxisomes reveals novel targeting
RT   peptides, metabolic pathways, and defense mechanisms.";
RL   Plant Cell 19:3170-3193(2007).
RN   [7]
RP   INTERACTION WITH LSD1.
RX   PubMed=23958864; DOI=10.1104/pp.113.225805;
RA   Li Y., Chen L., Mu J., Zuo J.;
RT   "LESION SIMULATING DISEASE1 interacts with catalases to regulate
RT   hypersensitive cell death in Arabidopsis.";
RL   Plant Physiol. 163:1059-1070(2013).
RN   [8]
RP   INTERACTION WITH NCA1, SUBCELLULAR LOCATION, AND SUBUNIT.
RX   PubMed=25700484; DOI=10.1105/tpc.114.135095;
RA   Li J., Liu J., Wang G., Cha J.Y., Li G., Chen S., Li Z., Guo J., Zhang C.,
RA   Yang Y., Kim W.Y., Yun D.J., Schumaker K.S., Chen Z., Guo Y.;
RT   "A chaperone function of NO CATALASE ACTIVITY1 is required to maintain
RT   catalase activity and for multiple stress responses in Arabidopsis.";
RL   Plant Cell 27:908-925(2015).
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   -!- SUBUNIT: Homotetramer and heterotetramer (PubMed:25700484). At least
CC       six or seven isozymes are produced from a mixture of 3 gene products.
CC       Interacts with NCA1 (PubMed:25700484). Interacts with LSD1
CC       (PubMed:23958864). {ECO:0000269|PubMed:23958864,
CC       ECO:0000269|PubMed:25700484}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25700484}.
CC       Peroxisome {ECO:0000269|PubMed:25700484}. Glyoxysome.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=1;
CC         Comment=A number of isoforms are produced. According to EST
CC         sequences.;
CC       Name=1;
CC         IsoId=P25819-1; Sequence=Displayed;
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; X64271; CAA45564.1; -; mRNA.
DR   EMBL; X94447; CAA64220.1; -; Genomic_DNA.
DR   EMBL; AL022023; CAA17773.1; -; Genomic_DNA.
DR   EMBL; AL161586; CAB80226.1; -; Genomic_DNA.
DR   EMBL; CP002687; AEE86462.1; -; Genomic_DNA.
DR   EMBL; AY074301; AAL66998.1; -; mRNA.
DR   EMBL; AY113854; AAM44902.1; -; mRNA.
DR   PIR; T05779; T05779.
DR   RefSeq; NP_195235.1; NM_119675.4. [P25819-1]
DR   AlphaFoldDB; P25819; -.
DR   SMR; P25819; -.
DR   BioGRID; 14943; 7.
DR   IntAct; P25819; 3.
DR   STRING; 3702.P25819; -.
DR   PeroxiBase; 5141; AtKat02.
DR   iPTMnet; P25819; -.
DR   SwissPalm; P25819; -.
DR   PaxDb; 3702-AT4G35090-1; -.
DR   ProteomicsDB; 223867; -. [P25819-1]
DR   EnsemblPlants; AT4G35090.1; AT4G35090.1; AT4G35090. [P25819-1]
DR   GeneID; 829661; -.
DR   Gramene; AT4G35090.1; AT4G35090.1; AT4G35090. [P25819-1]
DR   KEGG; ath:AT4G35090; -.
DR   Araport; AT4G35090; -.
DR   TAIR; AT4G35090; CAT2.
DR   eggNOG; KOG0047; Eukaryota.
DR   InParanoid; P25819; -.
DR   OrthoDB; 3198922at2759; -.
DR   PhylomeDB; P25819; -.
DR   BioCyc; MetaCyc:AT4G35090-MONOMER; -.
DR   PRO; PR:P25819; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; P25819; baseline and differential.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR   GO; GO:0009514; C:glyoxysome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR   GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR   GO; GO:0005886; C:plasma membrane; HDA:TAIR.
DR   GO; GO:0010319; C:stromule; IDA:TAIR.
DR   GO; GO:0004096; F:catalase activity; IMP:TAIR.
DR   GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0008219; P:cell death; IMP:TAIR.
DR   GO; GO:0045454; P:cell redox homeostasis; IMP:TAIR.
DR   GO; GO:0006995; P:cellular response to nitrogen starvation; IEP:TAIR.
DR   GO; GO:0016036; P:cellular response to phosphate starvation; IEP:TAIR.
DR   GO; GO:0009970; P:cellular response to sulfate starvation; IEP:TAIR.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009648; P:photoperiodism; IMP:TAIR.
DR   GO; GO:0009409; P:response to cold; IEP:TAIR.
DR   GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
DR   GO; GO:0006979; P:response to oxidative stress; IMP:TAIR.
DR   CDD; cd08154; catalase_clade_1; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
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; CATALASE; 1.
DR   PANTHER; PTHR11465:SF23; CATALASE-2; 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; Heme-dependent catalase-like; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
DR   Genevisible; P25819; AT.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Glyoxysome; Heme; Hydrogen peroxide; Iron;
KW   Metal-binding; Oxidoreductase; Peroxidase; Peroxisome; Reference proteome.
FT   CHAIN           1..492
FT                   /note="Catalase-2"
FT                   /id="PRO_0000084931"
FT   ACT_SITE        65
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        138
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         348
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   VARIANT         421
FT                   /note="I -> V (in strain: cv. Landsberg erecta)"
FT   CONFLICT        39
FT                   /note="P -> L (in Ref. 1; CAA45564)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        109
FT                   /note="E -> A (in Ref. 1; CAA45564)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        154
FT                   /note="M -> I (in Ref. 1; CAA45564)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        243
FT                   /note="V -> L (in Ref. 1; CAA45564)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   492 AA;  56931 MW;  AB622230561FD79B CRC64;
     MDPYKYRPAS SYNSPFFTTN SGAPVWNNNS SMTVGPRGPI LLEDYHLVEK LANFDRERIP
     ERVVHARGAS AKGFFEVTHD ISNLTCADFL RAPGVQTPVI VRFSTVIHER GSPETLRDPR
     GFAVKFYTRE GNFDLVGNNF PVFFIRDGMK FPDMVHALKP NPKSHIQENW RILDFFSHHP
     ESLNMFTFLF DDIGIPQDYR HMDGSGVNTY MLINKAGKAH YVKFHWKPTC GVKSLLEEDA
     IRVGGTNHSH ATQDLYDSIA AGNYPEWKLF IQIIDPADED KFDFDPLDVT KTWPEDILPL
     QPVGRMVLNK NIDNFFAENE QLAFCPAIIV PGIHYSDDKL LQTRVFSYAD TQRHRLGPNY
     LQLPVNAPKC AHHNNHHEGF MNFMHRDEEV NYFPSRYDQV RHAEKYPTPP AVCSGKRERC
     IIEKENNFKE PGERYRTFTP ERQERFIQRW IDALSDPRIT HEIRSIWISY WSQADKSLGQ
     KLASRLNVRP SI
//