ID   CATA_STRCO              Reviewed;         487 AA.
AC   Q9Z598;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=katA; OrderedLocusNames=SCO6204; ORFNames=SC2G5.25c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(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   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; AL939126; CAB36612.1; -; Genomic_DNA.
DR   PIR; T34858; T34858.
DR   RefSeq; NP_630307.1; NC_003888.3.
DR   RefSeq; WP_003972723.1; NZ_VNID01000009.1.
DR   AlphaFoldDB; Q9Z598; -.
DR   SMR; Q9Z598; -.
DR   STRING; 100226.SCO6204; -.
DR   GeneID; 1101645; -.
DR   KEGG; sco:SCO6204; -.
DR   PATRIC; fig|100226.15.peg.6317; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_2_0_11; -.
DR   InParanoid; Q9Z598; -.
DR   OMA; SPNNFVP; -.
DR   PhylomeDB; Q9Z598; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; 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:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
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   3: Inferred from homology;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW   Reference proteome.
FT   CHAIN           1..487
FT                   /note="Catalase"
FT                   /id="PRO_0000085011"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         337
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"
SQ   SEQUENCE   487 AA;  53911 MW;  604318B9128D8ABD CRC64;
     MSQRVLTTES GAPVADNQNS ASAGIGGPLL IQDQHLIEKL ARFNRERIPE RVVHARGSGA
     YGHFEVTDDV SGFTHADFLN TVGKRTEVFL RFSTVADSLG GADAVRDPRG FALKFYTEEG
     NYDLVGNNTP VFFIKDPIKF PDFIHSQKRD PFTGRQEPDN VFDFWAHSPE ATHQITWLMG
     DRGIPASYRH MDGFGSHTYQ WTNARGESFF VKYHFKTDQG IRCLTADEAA KLAGEDPTSH
     QTDLVQAIER GVYPSWTLHV QLMPVAEAAN YRFNPFDVTK VWPHADYPLK RVGRLVLDRN
     PDNVFAEVEQ AAFSPNNFVP GIGPSPDKML QGRLFAYADA HRYRLGVNHT QLAVNAPKAV
     PGGAANYGRD GLMAANPQGR YAKNYEPNSY DGPAETGTPL AAPLAVSGHT GTHEAPLHTK
     DDHFVQAGAL YRLMSEDEKQ RLVANLAGGL SQVSRNDVVE KNLAHFHAAD PEYGKRVEEA
     VRALRED