ID A0A3A4F0K5_9MICC Unreviewed; 568 AA.
AC A0A3A4F0K5;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Catalase {ECO:0000313|EMBL:RJN31241.1};
GN ORFNames=D3250_10365 {ECO:0000313|EMBL:RJN31241.1};
OS Nesterenkonia natronophila.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Nesterenkonia.
OX NCBI_TaxID=2174932 {ECO:0000313|EMBL:RJN31241.1, ECO:0000313|Proteomes:UP000266615};
RN [1] {ECO:0000313|EMBL:RJN31241.1, ECO:0000313|Proteomes:UP000266615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M8 {ECO:0000313|EMBL:RJN31241.1,
RC ECO:0000313|Proteomes:UP000266615};
RA Menes R.J., Iriarte A.;
RT "Nesterenkonia natronophila sp. nov., an alkaliphilic actinobacteriume
RT isolated from a soda lake, and emended description of the genus
RT Nesterenkonia.";
RL Submitted (SEP-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:RJN31241.1}.
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DR EMBL; QYZP01000003; RJN31241.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A4F0K5; -.
DR OrthoDB; 3169619at2; -.
DR Proteomes; UP000266615; 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:UP000266615}.
FT DOMAIN 8..404
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..422
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 408..422
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 133
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 343
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; 64035 MW; 1274EC9AD7B7C650 CRC64;
MADDQILTTR QGHPVPNNQN QRTVGSRGPA TLENYHFLEK ISHFDRERIP ERVVHARGFV
AYGEFEATGK IGDEPASTYT RAKLFQEPGK TTDLAIRFST VIGGRDSTEV ARDPRGFAVK
FYTEDGNWDL VGNNLPVFFI RDALKFPDVI HSLKPDPITF RQEPNRIFDF MSQSPESMHM
LTHLFSPRGI PATYRHMEGF GVNTYKMVND QGETVLVKYH WLPRQGVASL TEGEAANVQA
QELGSASKDL YEAIERGDFP QWDLYVQIME DHDHPELEWD PLDDTKIWPE DDFPLRHVGT
MTLNRNIQDF HNENEQIAMG TGVLVDGLDF SDDKMLVGRT FSYSDTQRYR VGPNYLQIPV
NFPKGVNGRV HTHQRGGPMS YHTDVASGQN PHVNYEPSIH NGLEEAPEQP NNPPQISGQV
QQSTIERTND YVQARGRYST IEDWERDELV NVMGTLLSDC ESDVQQRMVW HFFMVHDDYG
KRVGEQLGIS AADVANLKPL PTQDFTEAED QRLKNLGNNG DSLDPAQWGG WTSSVKDHQV
AAEDVLSGSL GQLEYSTDKA TAGAASHS
//
