ID   A0A160FGV8_9BURK        Unreviewed;       484 AA.
AC   A0A160FGV8;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=AYM40_02325 {ECO:0000313|EMBL:ANB71332.1};
OS   Paraburkholderia phytofirmans OLGA172.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1417228 {ECO:0000313|EMBL:ANB71332.1, ECO:0000313|Proteomes:UP000076852};
RN   [1] {ECO:0000313|EMBL:ANB71332.1, ECO:0000313|Proteomes:UP000076852}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLGA172 {ECO:0000313|EMBL:ANB71332.1,
RC   ECO:0000313|Proteomes:UP000076852};
RX   PubMed=27063562; DOI=10.1016/j.gene.2016.04.018;
RA   Ricker N., Shen S.Y., Goordial J., Jin S., Fulthorpe R.R.;
RT   "PacBio SMRT assembly of a complex multi-replicon genome reveals
RT   chlorocatechol degradative operon in a region of genome plasticity.";
RL   Gene 586:239-247(2016).
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; CP014578; ANB71332.1; -; Genomic_DNA.
DR   RefSeq; WP_063494807.1; NZ_CP014578.1.
DR   AlphaFoldDB; A0A160FGV8; -.
DR   STRING; 1804984.AYM40_02325; -.
DR   KEGG; buz:AYM40_02325; -.
DR   Proteomes; UP000076852; Chromosome 1.
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:UP000076852}.
FT   DOMAIN          7..392
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..22
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   484 AA;  54589 MW;  456DDD6B0D4BCCB1 CRC64;
     MSERKLTNAA GAPIADNQNS MTAGARGPVV LQDVWLLEKL AHFDREVIPE RRVHAKGSGA
     FGTLKVTHDV SRFTKAKVFA QLGKDTPLFM RFSTVAGERG AADAERDVRG FSIKFYTEEG
     NWDVVGNNTP VFFIRDPLKF PDFIHTQKRD PYTNMRSNIA AWDFWSRHPE SLHQVTILMS
     DRGIPQNYRQ MHGFGSHTYS FINADNERFW VKFHFKSMQG IENFTDAEAA QVVAQNRESA
     QHDLLTSIEA GNFPKWRFAI QVMPEAEAAN YRFNPFDITK VWSQKDYPLI DVGTIELNRN
     AANYFADVEQ AAFTPANVVP GIGFSPDRLL QGRLFSYGDT QRYRLGTNHH QIPVNAPRCP
     VHHSFHRDGA MRTDGNLGGN VNYEPSRFGD FGQDTSAAEP PLAAGTVDRY DHREDEDYYT
     QPGMLFALFD AAQRQRLFGN IARHINGVPQ EIVARQIEHF RRADPAYAEG VIAAMAELAE
     AGTK
//