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Database: UniProt
Entry: A0A0B6TXN3_9CORY
LinkDB: A0A0B6TXN3_9CORY
Original site: A0A0B6TXN3_9CORY 
ID   A0A0B6TXN3_9CORY        Unreviewed;       718 AA.
AC   A0A0B6TXN3;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
DE            EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
GN   Name=katE {ECO:0000313|EMBL:AJK69466.1};
GN   ORFNames=B840_09375 {ECO:0000313|EMBL:AJK69466.1};
OS   Corynebacterium marinum DSM 44953.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1224162 {ECO:0000313|EMBL:AJK69466.1, ECO:0000313|Proteomes:UP000031928};
RN   [1] {ECO:0000313|EMBL:AJK69466.1, ECO:0000313|Proteomes:UP000031928}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44953 {ECO:0000313|EMBL:AJK69466.1,
RC   ECO:0000313|Proteomes:UP000031928};
RA   Schaffert L., Albersmeier A., Kalinowski J., Ruckert C.;
RT   "Complete genome sequence of Corynebacterium marinum DSM 44953.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Serves to protect cells from the toxic effects of hydrogen
CC       peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
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|PIRNR:PIRNR038927,
CC         ECO:0000256|RuleBase:RU000498};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2};
CC   -!- SIMILARITY: Belongs to the catalase family. HPII subfamily.
CC       {ECO:0000256|ARBA:ARBA00010660}.
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DR   EMBL; CP007790; AJK69466.1; -; Genomic_DNA.
DR   RefSeq; WP_042621899.1; NZ_CP007790.1.
DR   AlphaFoldDB; A0A0B6TXN3; -.
DR   STRING; 1224162.B840_09375; -.
DR   KEGG; cmq:B840_09375; -.
DR   HOGENOM; CLU_010645_3_0_11; -.
DR   OrthoDB; 3169619at2; -.
DR   Proteomes; UP000031928; Chromosome.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd03132; GATase1_catalase; 1.
DR   Gene3D; 1.20.1370.20; -; 1.
DR   Gene3D; 3.40.50.880; -; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024712; Catalase_clade2.
DR   InterPro; IPR043156; Catalase_clade2_helical.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR041399; Catalase_large_C.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   PANTHER; PTHR42821; CATALASE; 1.
DR   PANTHER; PTHR42821:SF1; CATALASE-B; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   Pfam; PF18011; Catalase_C; 1.
DR   PIRSF; PIRSF038927; Catalase_clade2; 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|PIRNR:PIRNR038927};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW   ECO:0000256|PIRNR:PIRNR038927};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR038927};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRNR:PIRNR038927};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|PIRNR:PIRNR038927};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR038927};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031928}.
FT   DOMAIN          78..466
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   REGION          1..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..40
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        73..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        125
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT   ACT_SITE        197
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT   BINDING         122
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         161
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         210
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         408
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT   BINDING         412
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:PIRSR038927-2"
FT   BINDING         419
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ   SEQUENCE   718 AA;  77965 MW;  D0F886AEECFAF26F CRC64;
     MTPKKKPAKD RASDSLPVIP GAPAAQPPSL GEPTSPVKPL PPKEDQQHLA NVTATGSPFT
     AGADAGPDPR AQQGEYLTTS TGQRVPDTDH SLKAGPRGPV LLQDHHLREK ITHFDHERIP
     ERVVHARGAG AHGVFVGNGA AGDICSAAVF GKGKETEVFV RFSTVLGSRG SADTVRDTRG
     FATKFYTDEG TWDLVGNNMP VFFIQDGIKF PDVVHAAKPH PDREIPQAQS AHDTFWDFVS
     LHTEAQHHTI WNMSDRGIPR SYRMMEGFGV HTFRLSNAKG ETTLVKFHWK PKLGVHSLVW
     EEAQIAAGVD PDFHRRDLAD AIEAGAFPQW DLGVQVFPDT EEQMFEGIDL LDPTKLVPEE
     LAPVQVIGTM TLVANPTNYF EQTEQVAFHP GHLPPGIDVT ADPLLQGRLF SYIDTQLTRL
     GGPNFNQIPI NRPHTPVNDM LRDGFHQHAS HAGVAPYRPN SLDGGNPFPA TAAEGARIDV
     PVPLPESAIV REQPATFDDH FSHARLFYLS LSEVEQRHVA DAYSFELGKC YEENIKTRQL
     AALAQIDTDL AAAVAEKLGL PAPAKAKLAK VEPSPALSQI GQEWPVDGRQ VGILTTAGTP
     PKEVAELVAA IDAAGMVPLV VGEHGGKLGD VPISRTYDTA RSVEFDAVVV ADTPDRYEVD
     VMRAEVFHQC KAIVLLDSLE NVRVDTSAPG VVTVSSLSGA VDQLIPLMRG HRVWERQG
//
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