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Database: UniProt
Entry: A0A0A2MLX3_9FLAO
LinkDB: A0A0A2MLX3_9FLAO
Original site: A0A0A2MLX3_9FLAO 
ID   A0A0A2MLX3_9FLAO        Unreviewed;       494 AA.
AC   A0A0A2MLX3;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Catalase {ECO:0000313|EMBL:KGO92488.1};
GN   ORFNames=Q766_11940 {ECO:0000313|EMBL:KGO92488.1};
OS   Flavobacterium subsaxonicum WB 4.1-42 = DSM 21790.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1121898 {ECO:0000313|EMBL:KGO92488.1, ECO:0000313|Proteomes:UP000030111};
RN   [1] {ECO:0000313|EMBL:KGO92488.1, ECO:0000313|Proteomes:UP000030111}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WB 4.1-42 {ECO:0000313|EMBL:KGO92488.1,
RC   ECO:0000313|Proteomes:UP000030111};
RA   Zeng Z., Chen C.;
RL   Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KGO92488.1}.
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DR   EMBL; JRLY01000009; KGO92488.1; -; Genomic_DNA.
DR   RefSeq; WP_026991479.1; NZ_JRLY01000009.1.
DR   AlphaFoldDB; A0A0A2MLX3; -.
DR   STRING; 1121898.GCA_000422725_03513; -.
DR   eggNOG; COG0753; Bacteria.
DR   OrthoDB; 9760293at2; -.
DR   Proteomes; UP000030111; Unassembled WGS sequence.
DR   GO; GO:0004096; F:catalase activity; IEA:InterPro.
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; 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; 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   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   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030111}.
FT   DOMAIN          7..391
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        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   494 AA;  56403 MW;  A4DEA0BB6E11AEEA CRC64;
     MSQDKLTTAS GRPYYEDEDS QTVGARGPIL LQDVILHEKM AHFNRERIPE RVVHAKGSAA
     FGTFTVTHDI TKYTKAKIFS EVGKQTGMFL RFSTVGGEKG SPDTERDPRG FALKFYTEDG
     NWDLVGNNTP VFFIKDPKKF SDFIHTQKRD PQTNMKSATM MWDFWSLNPE SLHQVLILMS
     DRGTPVGYRH MHGFGSHTFS LINADNERFY VKFHFITAQG IRNFTDADAA EMKSKDLDFA
     QRDLFENIQQ GNYPKWHLKI QVMPEAEAKT YHINPFDVTK VWPHADYPLM DVGEMELNRN
     PQNYYQDVEQ AAFAPAHIVD GIGYSPDKML QGRLLSYPDA QRYRLGTNYE QIPVNRCPYM
     TNNYQRDGLM RVDGNGGSNA NYYPNSFDNI VADHSYKEPA LELDSLTADW YDRNGPGEND
     HYSQPGNLFK LMDEQAKQNT ISNIVGAMSG IAGPKRDEII NRQLCHWFRA DINLGLGVAK
     GLNIQIDPAM FRQQ
//
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