ID   CATE_PSEPU              Reviewed;         711 AA.
AC   P95539;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=Catalase HPII;
DE            EC=1.11.1.6;
GN   Name=katE; Synonyms=catC;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Miller C.D., Kim Y.C., Anderson A.J.;
RT   "A method to derive a promoter fusion and gene inactivation of the
RT   stationary-phase inducible catalase (catC) from Pseudomonas putida.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the catalase family. HPII subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U82622; AAB40866.1; -; Genomic_DNA.
DR   AlphaFoldDB; P95539; -.
DR   SMR; P95539; -.
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; cd03132; GATase1_catalase; 1.
DR   Gene3D; 1.20.1370.20; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024712; Catalase_clade2.
DR   InterPro; IPR043156; Catalase_clade2_helical.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR041399; Catalase_large_C.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   PANTHER; PTHR42821; PTHR42821; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   Pfam; PF18011; Catalase_C; 1.
DR   PIRSF; PIRSF038927; Catalase_clade2; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF52317; SSF52317; 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   Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW   Peroxidase.
FT   CHAIN           1..711
FT                   /note="Catalase HPII"
FT                   /id="PRO_0000084973"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..27
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        92
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        165
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         379
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   711 AA;  78129 MW;  0D134B629B203C21 CRC64;
     MPSKKTDAPK QSEAAGTQTP DRANTNAKLQ SLETFRSDAT GQALRTNQGV KIADNQNSLK
     AGARGPSLLE DFIMREKITH FDHERIPERI VHARGTGAHG YFQSYGNHAD LTKAGFLQDP
     DKITPVFVRF STVQGPRGSG DTVRDVRGFA VKFYTDEGNF DLVGNNMPVF FIQDAIKFPD
     FVHAVKPEPH NEIPTGGSAH DTFWDFVSLV PESAHMVMWA MSDRAIPRSL RMMEGFGVHT
     FRLINAEGVA SFVKFHWKPR QGVHSLLWDE AQKLAGKDTD FQRRDLWEAI ENGDYPEWEL
     GVQIVPEADE HKFDFDLLDP TKIIPEELVP VTPLGKMVLN RNPDNFFAEV EQVAFCPGHI
     VPGIDFTNDP LLQGRLFSYT DTQISRLGGP NFHQIPINRP VAPNHNNQRD ALHQHVVHKG
     RASYEPNSID GGWPKETPAA AQDGGFESYQ ERIDAHKIRQ RSESFGDHFS QARLFFQSMS
     PTEQQHIIKA YSFELGKVER EHIRAREVNE ILANIDLKLA AAVAANLGLP APKAGTVQVK
     GSQLAQSPAL SQMNHPGSVG IKGRKIAVLV ANGVDAASVD KLIKALEAHS ARPMLLGPTS
     APVKATDGKQ LPVEASMEGM PSIMFDGIVV PSGKASTDAL AASGLAKHFL LEGYKHLKAM
     VLTKELATGL GLKEDKGLLL ADDQKAVDAF VKAVEGHRVW EREAAAEAVP A