ID A0A169C6F2_9MICO Unreviewed; 499 AA.
AC A0A169C6F2;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, 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 ORFNames=A6122_2641 {ECO:0000313|EMBL:AND17755.1};
OS Rathayibacter tritici.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Rathayibacter.
OX NCBI_TaxID=33888 {ECO:0000313|EMBL:AND17755.1, ECO:0000313|Proteomes:UP000077071};
RN [1] {ECO:0000313|EMBL:AND17755.1, ECO:0000313|Proteomes:UP000077071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 1953 {ECO:0000313|EMBL:AND17755.1,
RC ECO:0000313|Proteomes:UP000077071};
RA Park J., Lee H.-H., Lee S.-W., Seo Y.-S.;
RT "Complete genome sequence of Rathayibacter tritici NCPPB 1953.";
RL Submitted (MAY-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; CP015515; AND17755.1; -; Genomic_DNA.
DR RefSeq; WP_068256020.1; NZ_PSWT01000010.1.
DR AlphaFoldDB; A0A169C6F2; -.
DR STRING; 33888.A6122_2641; -.
DR KEGG; rtn:A6122_2641; -.
DR PATRIC; fig|33888.3.peg.2960; -.
DR OrthoDB; 3169619at2; -.
DR Proteomes; UP000077071; Chromosome.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000077071}.
FT DOMAIN 8..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 COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 55
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 499 AA; 55428 MW; 7756901F881CF0CB CRC64;
MTEERFTTTN SGAPVASDDH SLSVGADGPL ALHDHYLVEK LAQFNRERIP ERVVHAKGGG
AFGLFTTTAD VSAYTRAALF QPGVETEMLA RFSTVAGEQG SPDTWRDPRG FALKFYTSEG
NYDLVGNNTP VFFLRDGIKF PDFIRSQKRL PGSHLRDHDM QWDFWTLSPE SAHQVTWLMG
DRGLPSSWRH MDGFGSHTYQ WINAAGERFW VKYHFKTDQG VEILTQEQAD QIAGEDADFH
IRDLSSAIDR GDFPSWTLSV QVMPYEDAKS YRFNPFDLTK VWPHSDYPLI EVGTMTLDRN
PENYFAQIEQ AAFAPSNFVP GIAASPDKML LARIFSYADA HRYRVGTNHA QLPVNAPKSP
VHSYSKDGPM RFDFQKSEVP VYAPNSQGGA HADPARAAES AGWSTDGELT RAAATLHPED
DDFGQARTLY RDVLDDDARA RLVANIAGHV SKVTRPELRQ RVLQYWANVD SSLSQRVAEA
LEPSAPGADV SAEAVGIGA
//
