ID   A0A077KQA6_9FLAO        Unreviewed;       495 AA.
AC   A0A077KQA6;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 31.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=CHSO_4690 {ECO:0000313|EMBL:BAP33727.1};
OS   Chryseobacterium sp. StRB126.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=878220 {ECO:0000313|EMBL:BAP33727.1, ECO:0000313|Proteomes:UP000031650};
RN   [1] {ECO:0000313|EMBL:BAP33727.1, ECO:0000313|Proteomes:UP000031650}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=StRB126 {ECO:0000313|EMBL:BAP33727.1,
RC   ECO:0000313|Proteomes:UP000031650};
RX   PubMed=25291777; DOI=10.1128/genomeA.00952-14;
RA   Morohoshi T., Wang W.Z., Someya N., Ikeda T.;
RT   "Complete Genome Sequence of Chryseobacterium sp. Strain StRB126, an N-
RT   Acylhomoserine Lactone-Degrading Bacterium Isolated from Potato Root.";
RL   Genome Announc. 2:e00952-14(2014).
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:0000256|ARBA:ARBA00000720,
CC         ECO:0000256|RuleBase:RU000498};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|PIRSR:PIRSR038928-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
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DR   EMBL; AP014624; BAP33727.1; -; Genomic_DNA.
DR   RefSeq; WP_045501352.1; NZ_AP014624.1.
DR   AlphaFoldDB; A0A077KQA6; -.
DR   KEGG; chz:CHSO_4690; -.
DR   HOGENOM; CLU_010645_4_1_10; -.
DR   OrthoDB; 9760293at2; -.
DR   Proteomes; UP000031650; Chromosome.
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   Gene3D; 2.40.180.10; Catalase core domain; 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; CATALASE; 1.
DR   PANTHER; PTHR11465:SF9; CATALASE; 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; Heme-dependent catalase-like; 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 {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038928-2};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW   ECO:0000256|RuleBase:RU000498};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR038928-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000498};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000498}.
FT   DOMAIN          7..391
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
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:0000256|PIRSR:PIRSR038928-2"
SQ   SEQUENCE   495 AA;  57029 MW;  F7C995C9E2D4D8BA CRC64;
     MDSKKLTLSN GAPYFEHQDS QTVGPRGPVL LQDFVLQENL AHFVRERIPE RIVHAKGSGA
     YGTFTVTHDI SQYTKAKLFS KVGNSCRMFA RFSTVGGEKG SADTARDPRG FALKFYTEDG
     NWDLVGNNTP VFFIKDAKKF PDFIHTQKRL PRTNLKSATM MWDFWSLNPE SLHQVLILMS
     DRGTPYGYRH MHGFGSHTFS MINDQNERVW VKFHFKTKQG VKNFTDEEAV KMAGENPDFA
     QEDLCNAIEN GDFPKWTMYI QVMTEEQAKD FRWNPFDITK VWFHDDFPLI EVGEMELNEV
     PVNYFAHVEQ STFSPSSLIN GISFSPDKML QGRLFSYPDA HRYRVGVNAH QLEVNRCPFA
     VNNYQRDGYM ADSSQYQDKP NYYPNSFDDI KPDVSYKNYE YELDSAHVAN YNRNDNDSDH
     YTQPGLLYSK AMNAEDRNNL IQNIIGSMKG ITGPKREEII NRQLCHFFRA NIELGMKVAS
     QLNINIDANM MNHSK
//