ID   CAT1_COMTR              Reviewed;          57 AA.
AC   P83657;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 72.
DE   RecName: Full=Catalase-1;
DE            EC=1.11.1.6;
DE   Flags: Fragments;
OS   Comamonas terrigena.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Comamonas.
OX   NCBI_TaxID=32013;
RN   [1] {ECO:0000305}
RP   PROTEIN SEQUENCE, CATALYTIC ACTIVITY, AND MASS SPECTROMETRY.
RC   STRAIN=N3H {ECO:0000269|PubMed:15177292};
RX   PubMed=15177292; DOI=10.1016/j.pep.2004.03.001;
RA   Zamocky M., Godocikova J., Gasperik J., Koller F., Polek B.;
RT   "Expression, purification, and sequence analysis of catalase-1 from the
RT   soil bacterium Comamonas terrigena N3H.";
RL   Protein Expr. Purif. 36:115-123(2004).
RN   [2] {ECO:0000305}
RP   CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, AND INDUCTION.
RC   STRAIN=N3H {ECO:0000269|PubMed:12094731};
RX   PubMed=12094731; DOI=10.1007/bf02817644;
RA   Zamocky M., Polek B., Godocikova J., Koller F.;
RT   "Oxidative stress-induced expression of catalases in Comamonas terrigena.";
RL   Folia Microbiol. (Praha) 47:235-240(2002).
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC       protect cells from the toxic effects of hydrogen peroxide.
CC       {ECO:0000305}.
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         ECO:0000269|PubMed:12094731, ECO:0000269|PubMed:15177292};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000269|PubMed:12094731};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Active from pH 6.0 to 10.0.;
CC       Temperature dependence:
CC         Activity decreases at temperatures above 55 degrees Celsius.;
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12094731}.
CC   -!- INDUCTION: Constitutively expressed. Inducible by oxidative stress in
CC       the exponential phase of bacterial growth.
CC       {ECO:0000269|PubMed:12094731}.
CC   -!- MASS SPECTROMETRY: Mass=55417; Method=MALDI;
CC       Evidence={ECO:0000269|PubMed:15177292};
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   AlphaFoldDB; P83657; -.
DR   SMR; P83657; -.
DR   PeroxiBase; 4280; CterKat01.
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:0042542; P:response to hydrogen peroxide; IDA:UniProtKB.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR020835; Catalase_sf.
DR   Pfam; PF00199; Catalase; 1.
DR   SUPFAM; SSF56634; SSF56634; 2.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Oxidoreductase; Peroxidase.
FT   CHAIN           1..>57
FT                   /note="Catalase-1"
FT                   /id="PRO_0000084984"
FT   BINDING         37
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|UniProtKB:P42321"
FT   NON_CONS        13..14
FT                   /evidence="ECO:0000303|PubMed:15177292"
FT   NON_CONS        32..33
FT                   /evidence="ECO:0000303|PubMed:15177292"
FT   NON_CONS        42..43
FT                   /evidence="ECO:0000303|PubMed:15177292"
FT   NON_TER         57
FT                   /evidence="ECO:0000303|PubMed:15177292"
SQ   SEQUENCE   57 AA;  6099 MW;  22AC1B93B4F3D72E CRC64;
     THCLTTAAGA PVARFSTVAG ERGAADAERD IRRLFSYGDA ARRLGVNHQH IPVNAPR