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Database: UniProt
Entry: A0A0B7IBT5_9FLAO
LinkDB: A0A0B7IBT5_9FLAO
Original site: A0A0B7IBT5_9FLAO 
ID   A0A0B7IBT5_9FLAO        Unreviewed;       507 AA.
AC   A0A0B7IBT5;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   Name=katA {ECO:0000313|EMBL:CEN47398.1};
GN   ORFNames=CCAND38_430035 {ECO:0000313|EMBL:CEN47398.1};
OS   Capnocytophaga canis.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=1848903 {ECO:0000313|EMBL:CEN47398.1, ECO:0000313|Proteomes:UP000045051};
RN   [1] {ECO:0000313|EMBL:CEN47398.1, ECO:0000313|Proteomes:UP000045051}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CcD38 {ECO:0000313|EMBL:CEN47398.1,
RC   ECO:0000313|Proteomes:UP000045051};
RA   Xiang T., Song Y., Huang L., Wang B., Wu P.;
RL   Submitted (JAN-2015) 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; CDOI01000155; CEN47398.1; -; Genomic_DNA.
DR   RefSeq; WP_042344569.1; NZ_WLVI01000014.1.
DR   AlphaFoldDB; A0A0B7IBT5; -.
DR   Proteomes; UP000045051; 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:SF61; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000045051}.
FT   DOMAIN          6..390
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         336
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   507 AA;  58235 MW;  DAD070EC240604CA CRC64;
     MNNKLTTTTG APVANNQDTM TAGKRGPALL QDIWFLEKLA HFDRQVIPER VMHAKGSGAY
     GTFRVTHDIT KYTKASIFAE IGKETPMFVR FSTVAGERGA ADAERDIRGF AMKFYTDQGN
     WDLVGNNTPV FFFRDPLKFP DLNHAVKRDP RTNMRSADNN WDFWTLLPEA LHQVTIVMSD
     RGIPKSYRTM HGFGSHTFSF INKEGVRHWV KFHLISQQGI ENLTDEEAAK LVGMDRESHQ
     KDLYEAIENG NFPKWKMFVQ IMTEEQARNL DYNPFDLTKV WYKKDFPLIP VGEFELNRNP
     ENYFAEVEQS AFSPANVVPG IGFSPDRMLQ GRLFSYGDSH RYRLGVNHNQ IPVNAPKCPV
     HGYHRDGAMR VDGNYGSTKH YEPNSFGVWQ EQKEFQEPAL RIDGDAYNYD FREDDDDYFT
     QPRKLFQLMN DEQKKALFEN TARAIGPAQK FIQIRHIRNC YHADPAYAKG VADALGLTME
     EVLKYEHPAL NLGPVAHKKM ECPFGHK
//
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