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Database: UniProt
Entry: A0A164IUT8_9NOCA
LinkDB: A0A164IUT8_9NOCA
Original site: A0A164IUT8_9NOCA 
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
//
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