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Database: UniProt
Entry: A0A0T1WDJ5_9MYCO
LinkDB: A0A0T1WDJ5_9MYCO
Original site: A0A0T1WDJ5_9MYCO 
ID   A0A0T1WDJ5_9MYCO        Unreviewed;       488 AA.
AC   A0A0T1WDJ5;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Catalase {ECO:0000313|EMBL:KQY07026.1};
GN   ORFNames=ASD37_13065 {ECO:0000313|EMBL:KQY07026.1};
OS   Mycobacterium sp. Root135.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1736457 {ECO:0000313|EMBL:KQY07026.1, ECO:0000313|Proteomes:UP000051127};
RN   [1] {ECO:0000313|EMBL:KQY07026.1, ECO:0000313|Proteomes:UP000051127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root135 {ECO:0000313|EMBL:KQY07026.1,
RC   ECO:0000313|Proteomes:UP000051127};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQY07026.1, ECO:0000313|Proteomes:UP000051127}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root135 {ECO:0000313|EMBL:KQY07026.1,
RC   ECO:0000313|Proteomes:UP000051127};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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:KQY07026.1}.
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DR   EMBL; LMEZ01000005; KQY07026.1; -; Genomic_DNA.
DR   RefSeq; WP_056551557.1; NZ_LMEZ01000005.1.
DR   AlphaFoldDB; A0A0T1WDJ5; -.
DR   STRING; 1736457.ASD37_13065; -.
DR   OrthoDB; 3169619at2; -.
DR   Proteomes; UP000051127; 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: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; 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:UP000051127}.
FT   DOMAIN          11..397
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        58
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   BINDING         341
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   488 AA;  54983 MW;  1D2AF0C8BC21FDB8 CRC64;
     MAFEENTEPL TTAAGAPVVD NQNSMSAGPR GPLLLQDLWL IEKLAHFSRE VIPERRMHAK
     GAGAFGTFKV TGDISAYTTA ALFNQVGNPC EMFARYSTVA GERGAADAER DIRGFALRFY
     TTQGNWDVVG NNTPVFFHRD PLKFPDLNRA VKRDPRTNLR DPENNWGFWT GLPESLHQVT
     YVMGDRGIPA SYRHMHGFGS HTFSLINADG IRHWVKFHFR TQQGIDNLTD QQAQTVIGAD
     RESHGRDLFD AIERGEFPRW TLFIQVMPED DARTYRFHPF DLTKVWSQQD YPLIEVGEYE
     LNRNPDNYFA EVEQAAFSPA NLVPGISYSP DKMLQGRLFS YGDAARYRVG VNHHQIPVNY
     PRGAARVNTY HRDGAMRVDG NQGGVPGMEP NSFGRWPDQP AYADPPQGIG NTADHFDFRE
     DDDNYFEQPG NLFRLMTGEE QQRLFDNTAR AIKGARSVTV NKHIENCTRA DPAYGEGVRK
     ACEAIGAL
//
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