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Database: UniProt
Entry: A0A1M7IFQ2_9FLAO
LinkDB: A0A1M7IFQ2_9FLAO
Original site: A0A1M7IFQ2_9FLAO 
ID   A0A1M7IFQ2_9FLAO        Unreviewed;       495 AA.
AC   A0A1M7IFQ2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=SAMN05444407_11474 {ECO:0000313|EMBL:SHM39604.1};
OS   Chryseobacterium contaminans.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=1423959 {ECO:0000313|EMBL:SHM39604.1, ECO:0000313|Proteomes:UP000184069};
RN   [1] {ECO:0000313|EMBL:SHM39604.1, ECO:0000313|Proteomes:UP000184069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 27621 {ECO:0000313|EMBL:SHM39604.1,
RC   ECO:0000313|Proteomes:UP000184069};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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; FRBM01000014; SHM39604.1; -; Genomic_DNA.
DR   RefSeq; WP_066697062.1; NZ_MAYF01000301.1.
DR   AlphaFoldDB; A0A1M7IFQ2; -.
DR   STRING; 1423959.SAMN05444407_11474; -.
DR   OrthoDB; 9760293at2; -.
DR   Proteomes; UP000184069; Unassembled WGS sequence.
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;  56855 MW;  C054976F3B68F48C CRC64;
     MDSKKLTLSN GAPYFEHQDS QTVGPRGPVL LQDFVLQENL AHFVRERIPE RIVHAKGSGA
     YGTFTVTHDI SQYTKAKLFS KVGNSCRMFA RFSTVGGEKG SADTARDPRG FALKFYTEDG
     NWDLVGNNTP VFFIKDAKKF PDFIHTQKRV PKTNLKSATM MWDFWSLNPE SLHQVLILMS
     DRGTPYGYRH MHGFGSHTFS MINDKNERVW VKFHFKTKQG VKNFTDAEAV KMAGENPDFA
     QEDLCNAIEN GDFPKWTMYI QVMTEEQAKD FRWNPFDVTK VWFHDDFPLI EVGEMELNEV
     PVNYFAHVEQ STFSPSSLIN GISFSPDKML QGRLFSYPDA HRYRVGVNAH QLEVNRCPFA
     VNNYQRDGYM ADSSHYQDKP NYYPNSFDDI TPDASYKNYE YELDSAHVAN YNRNDNDSDH
     YTQPGLLYSK AMNAEDRNNL IQNIVGSMKG ITGPKREEII NRQLCHFFRA NIELGMKVAS
     QLNINIDANM MNHSK
//
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