ID   CATA_MICLU              Reviewed;         503 AA.
AC   P29422; Q8RK91;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2002, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=katA;
OS   Micrococcus luteus (Micrococcus lysodeikticus).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Micrococcus.
OX   NCBI_TaxID=1270;
RN   [1]
RP   PRELIMINARY PROTEIN SEQUENCE, AND X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
RX   PubMed=1426241; DOI=10.1016/0014-5793(92)80919-8;
RA   Murshudov G.N., Melik-Adamyan W.R., Grebenko A.I., Barynin V.V.,
RA   Vagin A.A., Vainshtein B.K., Dauter Z., Wilson K.S.;
RT   "Three-dimensional structure of catalase from Micrococcus lysodeikticus at
RT   1.5-A resolution.";
RL   FEBS Lett. 312:127-131(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND X-RAY CRYSTALLOGRAPHY (0.88
RP   ANGSTROMS).
RX   PubMed=12454454; DOI=10.1107/s0907444902016566;
RA   Murshudov G.N., Grebenko A.I., Brannigan J.A., Antson A.A., Barynin V.V.,
RA   Dodson G.G., Dauter Z., Wilson K.S., Melik-Adamyan W.R.;
RT   "The structures of Micrococcus lysodeikticus catalase, its ferryl
RT   intermediate (compound II) and NADPH complex.";
RL   Acta Crystallogr. D 58:1972-1982(2002).
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC       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   -!- COFACTOR:
CC       Name=NADPH; Xref=ChEBI:CHEBI:57783;
CC   -!- SUBUNIT: Homotetramer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ438208; CAD27348.1; -; Genomic_DNA.
DR   PIR; S27264; S27264.
DR   PDB; 1GWE; X-ray; 0.88 A; A=1-502.
DR   PDB; 1GWF; X-ray; 1.96 A; A=1-502.
DR   PDB; 1GWH; X-ray; 1.74 A; A=1-502.
DR   PDB; 1HBZ; X-ray; 1.50 A; A=6-502.
DR   PDBsum; 1GWE; -.
DR   PDBsum; 1GWF; -.
DR   PDBsum; 1GWH; -.
DR   PDBsum; 1HBZ; -.
DR   AlphaFoldDB; P29422; -.
DR   SMR; P29422; -.
DR   STRING; 1232675.GCA_000309825_00557; -.
DR   DrugBank; DB02235; L-methionine (R)-S-oxide.
DR   PRIDE; P29422; -.
DR   SABIO-RK; P29422; -.
DR   EvolutionaryTrace; P29422; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd08156; catalase_clade_3; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR040333; Catalase_3.
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; Cytoplasm; Direct protein sequencing; Heme;
KW   Hydrogen peroxide; Iron; Metal-binding; NADP; Oxidoreductase; Peroxidase.
FT   CHAIN           1..503
FT                   /note="Catalase"
FT                   /id="PRO_0000084990"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        61
FT   ACT_SITE        133
FT   BINDING         343
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   STRAND          18..20
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   TURN            31..33
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   HELIX           41..50
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   STRAND          63..73
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   TURN            78..80
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   HELIX           84..86
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   STRAND          91..99
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   STRAND          101..103
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   STRAND          111..113
FT                   /evidence="ECO:0007829|PDB:1HBZ"
FT   STRAND          116..123
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   STRAND          126..136
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   HELIX           146..153
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   TURN            157..159
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   HELIX           164..172
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   HELIX           175..177
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   HELIX           178..185
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   HELIX           187..189
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   STRAND          190..192
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   HELIX           194..196
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   STRAND          205..208
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   STRAND          214..223
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   HELIX           232..241
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   HELIX           245..255
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   STRAND          261..270
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   HELIX           273..276
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   TURN            290..292
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   STRAND          296..305
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   HELIX           310..313
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   TURN            314..316
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   HELIX           334..350
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   HELIX           355..357
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   HELIX           359..361
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   STRAND          386..389
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   STRAND          391..393
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   HELIX           428..436
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   HELIX           440..454
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   HELIX           459..472
FT                   /evidence="ECO:0007829|PDB:1GWE"
FT   HELIX           474..485
FT                   /evidence="ECO:0007829|PDB:1GWE"
SQ   SEQUENCE   503 AA;  56906 MW;  8C60ADEFC0E46A09 CRC64;
     MEHQKTTPHA TGSTRQNGAP AVSDRQSLTV GSEGPIVLHD THLLETHQHF NRMNIPERRP
     HAKGSGAFGE FEVTEDVSKY TKALVFQPGT KTETLLRFST VAGELGSPDT WRDVRGFALR
     FYTEEGNYDL VGNNTPIFFL RDPMKFTHFI RSQKRLPDSG LRDATMQWDF WTNNPESAHQ
     VTYLMGPRGL PRTWREMNGY GSHTYLWVNA QGEKHWVKYH FISQQGVHNL SNDEATKIAG
     ENADFHRQDL FESIAKGDHP KWDLYIQAIP YEEGKTYRFN PFDLTKTISQ KDYPRIKVGT
     LTLNRNPENH FAQIESAAFS PSNTVPGIGL SPDRMLLGRA FAYHDAQLYR VGAHVNQLPV
     NRPKNAVHNY AFEGQMWYDH TGDRSTYVPN SNGDSWSDET GPVDDGWEAD GTLTREAQAL
     RADDDDFGQA GTLVREVFSD QERDDFVETV AGALKGVRQD VQARAFEYWK NVDATIGQRI
     EDEVKRHEGD GIPGVEAGGE ARM