ID A0A0D0LKQ4_9NOCA Unreviewed; 552 AA.
AC A0A0D0LKQ4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Catalase {ECO:0000313|EMBL:KIQ19259.1};
GN ORFNames=RU01_06210 {ECO:0000313|EMBL:KIQ19259.1};
OS Rhodococcus sp. MEB064.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1587522 {ECO:0000313|EMBL:KIQ19259.1, ECO:0000313|Proteomes:UP000032087};
RN [1] {ECO:0000313|EMBL:KIQ19259.1, ECO:0000313|Proteomes:UP000032087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEB064 {ECO:0000313|EMBL:KIQ19259.1,
RC ECO:0000313|Proteomes:UP000032087};
RA Perisin M.A., Vetter M., Gilbert J.A., Bergelson J.;
RT "16Stimator: statistical estimation of ribosomal gene copy numbers from
RT draft genome assemblies.";
RL Submitted (DEC-2014) 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:KIQ19259.1}.
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DR EMBL; JXQS01000010; KIQ19259.1; -; Genomic_DNA.
DR RefSeq; WP_042573650.1; NZ_JXQS01000010.1.
DR AlphaFoldDB; A0A0D0LKQ4; -.
DR Proteomes; UP000032087; 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}.
FT DOMAIN 19..412
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 515..537
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 66
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 144
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 354
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 552 AA; 62272 MW; 094BB2932EBA448B CRC64;
MTDVASQGST PDDDRDILTD RQGHPVYDNQ NQRTVGSRGP ATLENYHFLE KISHFDRERI
PERVVHARGA VAYGYFEATG KWGDEPIERY TRAKLFAEAG KRTDLAIRFS TVIGGRDSSE
AARDPRGFAI KFYTEDGNWD LVGNNLGVFF IRDAIKFPDV IHSLKPDPVT FRQEPARIFD
FMSQTPEATH MLVNLFSPRG IPANYRTQQG FGVNTYKWVN AEGETRLVKY HWIPKAGVSS
LTEADAAVVQ GQDLGHASKD LYDHIESGDY PEWELRVQLM SDDEHPELNF DPLDDTKVWP
ENEFPPKVVG RMVLDRNVSN HFTENEQISF GTGVLVDGLD FSDDKMLVGR TFSYSDTQRY
RVGPNYLQLP VNQPKNASVA TNQQGGQMQY AVDRNGGNPH VNYEPSITGG LREAQYPTHD
EQGPEISGRL TRKRIDRTND YEQAGQRYQL MDQWEKDDLV ANLVANISEA TREVQERMVW
HFLMADDELG ARVGDGLSIT ADDVRGLEPL ASQTLSDEEN ERRGNLGKNG PRDVTGLEMT
HCVPNERDVK AG
//
