ID A0A3N2B992_9MICO Unreviewed; 568 AA.
AC A0A3N2B992;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Catalase {ECO:0000313|EMBL:ROR71821.1};
GN ORFNames=EDD31_0159 {ECO:0000313|EMBL:ROR71821.1};
OS Bogoriella caseilytica.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Bogoriellaceae;
OC Bogoriella.
OX NCBI_TaxID=56055 {ECO:0000313|EMBL:ROR71821.1, ECO:0000313|Proteomes:UP000280668};
RN [1] {ECO:0000313|EMBL:ROR71821.1, ECO:0000313|Proteomes:UP000280668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11294 {ECO:0000313|EMBL:ROR71821.1,
RC ECO:0000313|Proteomes:UP000280668};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC protect cells from the toxic effects of hydrogen peroxide.
CC {ECO:0000256|ARBA:ARBA00002974}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC 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:ROR71821.1}.
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DR EMBL; RKHK01000001; ROR71821.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2B992; -.
DR OrthoDB; 3169619at2; -.
DR Proteomes; UP000280668; 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; cd08154; catalase_clade_1; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
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:SF23; CATALASE-2; 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; 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:UP000280668}.
FT DOMAIN 9..405
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..29
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 56
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 134
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 344
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 568 AA; 64370 MW; DF42BBF8CD6933AF CRC64;
MADDDRTLTT RQGHPVQDNQ NQRTVGSRGP ATLENYHFLE KISHFDRERI PERVVHARGF
VAYGEFEATG QIGDEPASTY TRAKLFQTAG KKTPLAIRFS TVIGGRDSSE AARDPRGFAV
KFYTEDGNWD LVGNNLAIFF IRDAIKFPDV IHSLKPDPVT FRQEPNRILD FMSQTPESMH
MLTHLFSPRG IPATYRHMEG FGVNTYKMVN AAGETVLVKY HWIPRQGVAS LTEEEAAKVQ
GQELGSASKD LYEAIERGDY PQWDLYVQLM EDHDHPELDW DPLDDTKIWP EDQFPLRRVG
TMTLNENVKD FHNENEQIAM GTGVLVDGLD FSDDKMLVGR TFSYSDTQRY RVGPNYLQLP
VNSPKGRAGK VYTNQRGGEM SYGVDTAPGQ NPHVNYEPSI HNGLHEAEKQ PYHAPQISGR
LTRSDLDRTN DYLQARGRYN TMNDWERDEL INVLGAMMAE SERDVQERML WHMFMVHDDY
GQRIGEVIGM TAEDVKHLKP LPRQQLSEAE LERLAHLGSN GDVIDPTQWG HWTSSVRNHS
VTAEQVLSGE LGDLEYSTDK SLAGTAGQ
//
