ID A0A090IE38_9GAMM Unreviewed; 504 AA.
AC A0A090IE38;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN Name=katB {ECO:0000313|EMBL:CED60311.1};
GN ORFNames=MVIS_2364 {ECO:0000313|EMBL:CED60311.1};
OS Moritella viscosa.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Moritellaceae; Moritella.
OX NCBI_TaxID=80854 {ECO:0000313|EMBL:CED60311.1, ECO:0000313|Proteomes:UP000032438};
RN [1] {ECO:0000313|Proteomes:UP000032438}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Hjerde E.;
RL Submitted (SEP-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 -!- 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|RuleBase:RU000498};
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, ECO:0000256|RuleBase:RU000498}.
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DR EMBL; LN554852; CED60311.1; -; Genomic_DNA.
DR RefSeq; WP_045110554.1; NZ_FRDW01000070.1.
DR AlphaFoldDB; A0A090IE38; -.
DR STRING; 80854.MVIS_2364; -.
DR GeneID; 61297407; -.
DR KEGG; mvs:MVIS_2364; -.
DR PATRIC; fig|80854.5.peg.2518; -.
DR HOGENOM; CLU_010645_2_0_6; -.
DR Proteomes; UP000032438; Chromosome complete 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; cd08154; catalase_clade_1; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
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: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; 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:UP000032438};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..504
FT /note="Catalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001857339"
FT DOMAIN 26..407
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
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 504 AA; 56642 MW; AB2E521BC406901F CRC64;
MNFNKKYLVI ALSMSLAFNA AAVTLTRDNG APVGDNQNSM TAGKNGSVLL EDVQLIQKLQ
RFARERIPER VVHARGTGAH GVFVATQDFS GITAAAPFAD KGKETPVFVR FSSVMHSKGS
PETLRDPRGF ATKFYTDEGN WDLVGLNMPV FFIRDAIKFP DMVHSLKPSP VTNIQDPNRV
FDFFSNEPGS THMLTWLYSD NGTPASYRKM DGFGVHAYKM INESGEVNYV KFHWKSLQGI
DNLDLDEVAN VQSKDFQHLT RDLYDSIAEE QYPQWDLYIK VMNPSDLNNF QYNPLDVTKM
WTNIPETKVG TMTLNRMPTN FFQETEQVAM SPANLIQGIE PSEDRLLQGR IFSYSDTQMY
RLGANHQQLP INRPTVNVVN YNQDGAHNMG VTMSDVNYQP SSEGVVEDKK ARHSTPSLTG
HVQQLAIDKQ SNFAQAGELY RSFTVQEQHN LIRNLSGDLG AVKNESVKYT MLSFFYKADT
EYGTQLTKAV NGDLAKVIKM AMSL
//
