ID   B2GHN7_KOCRD            Unreviewed;       508 AA.
AC   B2GHN7;
DT   10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT   10-JUN-2008, sequence version 1.
DT   02-SEP-2026, entry version 92.
DE   RecName: Full=Catalase {ECO:0000256|PROSITE-ProRule:PRU10013, ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|PROSITE-ProRule:PRU10013, ECO:0000256|RuleBase:RU000498};
GN   Name=katA {ECO:0000313|EMBL:BAG28876.1};
GN   OrderedLocusNames=KRH_05290 {ECO:0000313|EMBL:BAG28876.1};
OS   Kocuria rhizophila (strain ATCC 9341 / DSM 348 / NBRC 103217 / DC2201).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Micrococcaceae; Kocuria.
OX   NCBI_TaxID=378753 {ECO:0000313|EMBL:BAG28876.1, ECO:0000313|Proteomes:UP000008838};
RN   [1] {ECO:0000313|EMBL:BAG28876.1, ECO:0000313|Proteomes:UP000008838}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 9341 / DSM 348 / NBRC 103217 / DC2201
RC   {ECO:0000313|Proteomes:UP000008838};
RX   PubMed=18408034; DOI=10.1128/JB.01853-07;
RA   Takarada H., Sekine M., Kosugi H., Matsuo Y., Fujisawa T., Omata S.,
RA   Kishi E., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT   "Complete genome sequence of the soil actinomycete Kocuria rhizophila.";
RL   J. Bacteriol. 190:4139-4146(2008).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = O2 + 2 H2O; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00049254, ECO:0000256|PROSITE-
CC         ProRule:PRU10013, 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; AP009152; BAG28876.1; -; Genomic_DNA.
DR   RefSeq; WP_012397602.1; NC_010617.1.
DR   AlphaFoldDB; B2GHN7; -.
DR   SMR; B2GHN7; -.
DR   STRING; 378753.KRH_05290; -.
DR   KEGG; krh:KRH_05290; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_2_0_11; -.
DR   OrthoDB; 3169619at2; -.
DR   Proteomes; UP000008838; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:InterPro.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IEA:TreeGrafter.
DR   CDD; cd08156; catalase_clade_3; 1.
DR   FunFam; 2.40.180.10:FF:000001; Catalase; 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:UP000008838}.
FT   DOMAIN          12..394
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          483..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..15
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        22..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        59
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1,
FT                   ECO:0000256|PROSITE-ProRule:PRU10013"
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   508 AA;  57502 MW;  A369F04D91334AF6 CRC64;
     MTESTPHATG STTQAGIPAV SDRNSLTTGP NGSIVLHDHQ LVETLQHFNR MNIPERRPHA
     KGAGAFGTFE VTEDVSQWTK ADFLQPGKKT EMLARFSTVA GELGSPDTWR DVRGFALKFY
     TEEGNFDMVG NNTPIFFVRD PMKFPHFIRS QKRLPDSGLR DGTMQWDFWT NNPESAHQVT
     YLMGERGLPK TWRHMNGYGS HTYMLVNAEG EKFWVKWHFE SRQGVESLSN EEAERLAGAD
     GDVHRRDLFE AIERGEYPKW DLYFQIMPYE EAKTYRFNPF DLTKTWSKKD YPRHKVGTMT
     LNRNPENFFA QIEQAAFSPA NMVPGTGNSP DKMLLGRTFA YADAQLYRVG TNFQQLPVNR
     PINEVHTYNF EGSMTYHHSG ARRVYAPNSF GDSWSDETGP VDNGWEDDGA LVREAYTLRQ
     DDDDFGQPGT LIREVFNDAQ RARFVQTVAG ALDGVAEPVL SNAFQYWKNV DENIGQRIEE
     AVKSNAASPE VPGMGVDEDP TSNSEISE
//