ID A0A164IUT8_9NOCA Unreviewed; 505 AA.
AC A0A164IUT8;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN ORFNames=A2J03_10160 {ECO:0000313|EMBL:KZF01283.1};
OS Rhodococcus sp. EPR-157.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1813677 {ECO:0000313|EMBL:KZF01283.1, ECO:0000313|Proteomes:UP000077673};
RN [1] {ECO:0000313|EMBL:KZF01283.1, ECO:0000313|Proteomes:UP000077673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EPR-157 {ECO:0000313|EMBL:KZF01283.1,
RC ECO:0000313|Proteomes:UP000077673};
RA Ploux O.;
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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:KZF01283.1}.
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DR EMBL; LVCV01000550; KZF01283.1; -; Genomic_DNA.
DR RefSeq; WP_068379158.1; NZ_LVCV01000550.1.
DR AlphaFoldDB; A0A164IUT8; -.
DR OrthoDB; 3169619at2; -.
DR Proteomes; UP000077673; Unassembled WGS sequence.
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: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:UP000077673}.
FT DOMAIN 7..390
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..505
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 484..499
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 54
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 126
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 336
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 505 AA; 56503 MW; EFFA82290A900618 CRC64;
MTEPATTSNS GIPVPSDDQS LTAGTQGPIL LHDHYLIEKM AQFNRERVPE RVVHAKGAGA
FGELEITGDI SKFTKAKALQ PGAKTEMLAR FSTVAGEQGS PDTWRDPRGF SLKFYTEEGN
WDLVGNNTPV FFVKDPIKFQ DFIRSQKRMP DSGLRDHNMQ WDFWTLSPET AHQVTWLMGD
RGIPKSYRHM DGFGSHTFQL INDAGERNWV KFHFKTDQGV DFLTQEKADE LAGTSPDHHR
QDLFGSIKEG NFPSWTLKVQ IMPYDDAENY KFNPFDLTKV WSQKDYPLIE VGKMTLNRNP
ENFHAQIEQS SFEPSNLVPG IGASPDKMLL GRIFSYADAH RYRIGANYAQ LPVNAPKSPV
NSYSKDGAMR YSFNSADTPV YAPNSYGGPH ANTEKYGDDG SWDFEPRFVR TGYIEHPEDG
DFVQAGTLVR EVMDDAQRER LAGNIIGHAL NGVTEDVLAR VFEYWKNVDA DLGKKVEEGV
RAGQSGSAPT TSQSPTTPGD EAEKV
//