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
//