CATA1_ARATH
ID CATA1_ARATH Reviewed; 492 AA.
AC Q96528; O22529; Q9LDS9;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2002, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Catalase-1;
DE EC=1.11.1.6;
GN Name=CAT1; OrderedLocusNames=At1g20630; ORFNames=F2D10.11, F5M15.31;
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. Landsberg erecta;
RX PubMed=8819328; DOI=10.1104/pp.112.1.327;
RA Frugoli J.A., Zhong H.H., Nuccio M.L., McCourt P., McPeek M.A.,
RA Thomas T.L., McClung C.R.;
RT "Catalase is encoded by a multigene family in Arabidopsis thaliana (L.)
RT Heynh.";
RL Plant Physiol. 112:327-336(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9584109; DOI=10.1093/genetics/149.1.355;
RA Frugoli J.A., McPeek M.A., Thomas T.L., McClung C.R.;
RT "Intron loss and gain during evolution of the catalase gene family in
RT angiosperms.";
RL Genetics 149:355-365(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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 INDUCTION.
RX PubMed=17728292; DOI=10.1093/jxb/erm144;
RA Xing Y., Jia W., Zhang J.;
RT "AtMEK1 mediates stress-induced gene expression of CAT1 catalase by
RT triggering H2O2 production in Arabidopsis.";
RL J. Exp. Bot. 58:2969-2981(2007).
RN [7]
RP INDUCTION.
RX PubMed=18248592; DOI=10.1111/j.1365-313x.2008.03433.x;
RA Xing Y., Jia W., Zhang J.;
RT "AtMKK1 mediates ABA-induced CAT1 expression and H2O2 production via
RT AtMPK6-coupled signaling in Arabidopsis.";
RL Plant J. 54:440-451(2008).
RN [8]
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 [9]
RP INTERACTION WITH NCA1.
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. At least six or seven
CC isozymes are produced from a mixture of 3 gene products. Interacts with
CC NCA1 (PubMed:25700484). Interacts with LSD1 (PubMed:23958864).
CC {ECO:0000269|PubMed:23958864, ECO:0000269|PubMed:25700484}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: By hydrogen peroxide. By abscisic acid (ABA), drought, and
CC salt stress through the MKK1-MPK6 mediation.
CC {ECO:0000269|PubMed:17728292, ECO:0000269|PubMed:18248592}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF79625.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAF80611.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; U43340; AAB07026.1; -; mRNA.
DR EMBL; AF021937; AAC17731.1; -; Genomic_DNA.
DR EMBL; AC027665; AAF79625.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC069251; AAF80611.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002684; AEE29998.1; -; Genomic_DNA.
DR EMBL; AY136424; AAM97090.1; -; mRNA.
DR EMBL; BT010373; AAQ56816.1; -; mRNA.
DR RefSeq; NP_564121.1; NM_101914.4.
DR AlphaFoldDB; Q96528; -.
DR SMR; Q96528; -.
DR BioGRID; 23891; 9.
DR IntAct; Q96528; 4.
DR STRING; 3702.AT1G20630.1; -.
DR PeroxiBase; 5142; AtKat01.
DR iPTMnet; Q96528; -.
DR PaxDb; Q96528; -.
DR PRIDE; Q96528; -.
DR ProteomicsDB; 223883; -.
DR EnsemblPlants; AT1G20630.1; AT1G20630.1; AT1G20630.
DR GeneID; 838652; -.
DR Gramene; AT1G20630.1; AT1G20630.1; AT1G20630.
DR KEGG; ath:AT1G20630; -.
DR Araport; AT1G20630; -.
DR TAIR; locus:2034428; AT1G20630.
DR eggNOG; KOG0047; Eukaryota.
DR HOGENOM; CLU_010645_4_0_1; -.
DR OMA; SQTDKDH; -.
DR OrthoDB; 507937at2759; -.
DR PhylomeDB; Q96528; -.
DR PRO; PR:Q96528; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q96528; baseline and differential.
DR Genevisible; Q96528; AT.
DR GO; GO:0009941; C:chloroplast envelope; HDA:TAIR.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0022626; C:cytosolic ribosome; HDA:TAIR.
DR GO; GO:0005739; C:mitochondrion; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; HDA:TAIR.
DR GO; GO:0005777; C:peroxisome; HDA:TAIR.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004096; F:catalase activity; ISS:TAIR.
DR GO; GO:0050897; F:cobalt ion binding; HDA:TAIR.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
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; IGI:TAIR.
DR GO; GO:0009737; P:response to abscisic acid; IEP:TAIR.
DR GO; GO:0042542; P:response to hydrogen peroxide; IEP:TAIR.
DR GO; GO:0009416; P:response to light stimulus; IEP:TAIR.
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 Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase; Reference proteome.
FT CHAIN 1..492
FT /note="Catalase-1"
FT /id="PRO_0000084930"
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 CONFLICT 103
FT /note="F -> L (in Ref. 1; AAB07026)"
FT /evidence="ECO:0000305"
FT CONFLICT 332
FT /note="G -> F (in Ref. 1; AAB07026)"
FT /evidence="ECO:0000305"
FT CONFLICT 339..340
FT /note="KL -> NV (in Ref. 1; AAB07026)"
FT /evidence="ECO:0000305"
FT CONFLICT 423
FT /note="G -> R (in Ref. 1; AAB07026 and 2; AAC17731)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 492 AA; 56762 MW; 271E55FF7D6910EB CRC64;
MDPYRVRPSS AHDSPFFTTN SGAPVWNNNS SLTVGTRGPI LLEDYHLLEK LANFDRERIP
ERVVHARGAS AKGFFEVTHD ITQLTSADFL RGPGVQTPVI VRFSTVIHER GSPETLRDPR
GFAVKFYTRE GNFDLVGNNF PVFFVRDGMK FPDMVHALKP NPKSHIQENW RILDFFSHHP
ESLHMFSFLF DDLGIPQDYR HMEGAGVNTY MLINKAGKAH YVKFHWKPTC GIKCLSDEEA
IRVGGANHSH ATKDLYDSIA AGNYPQWNLF VQVMDPAHED KFDFDPLDVT KIWPEDILPL
QPVGRLVLNK NIDNFFNENE QIAFCPALVV PGIHYSDDKL LQTRIFSYAD SQRHRLGPNY
LQLPVNAPKC AHHNNHHDGF MNFMHRDEEV NYFPSRLDPV RHAEKYPTTP IVCSGNREKC
FIGKENNFKQ PGERYRSWDS DRQERFVKRF VEALSEPRVT HEIRSIWISY WSQADKSLGQ
KLATRLNVRP NF
