ID   CATA_METBF              Reviewed;         505 AA.
AC   O93662; Q46EA1;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   03-AUG-2022, entry version 129.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=kat; OrderedLocusNames=Mbar_A0814;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10382262; DOI=10.1007/s002030050716;
RA   Shima S., Netrusov A., Sordel M., Wicke M., Hartmann G.C., Thauer R.K.;
RT   "Purification, characterization, and primary structure of a monofunctional
RT   catalase from Methanosarcina barkeri.";
RL   Arch. Microbiol. 171:317-323(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC       protect cells from the toxic effects of hydrogen peroxide.
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:0000255|PROSITE-ProRule:PRU10013};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ005939; CAA06774.1; -; Genomic_DNA.
DR   EMBL; CP000099; AAZ69791.1; -; Genomic_DNA.
DR   RefSeq; WP_011305841.1; NC_007355.1.
DR   AlphaFoldDB; O93662; -.
DR   SMR; O93662; -.
DR   STRING; 269797.Mbar_A0814; -.
DR   PeroxiBase; 8411; MbaKat01.
DR   PRIDE; O93662; -.
DR   EnsemblBacteria; AAZ69791; AAZ69791; Mbar_A0814.
DR   GeneID; 3626836; -.
DR   KEGG; mba:Mbar_A0814; -.
DR   eggNOG; arCOG03310; Archaea.
DR   HOGENOM; CLU_010645_2_0_2; -.
DR   OMA; HVWPQKQ; -.
DR   OrthoDB; 15877at2157; -.
DR   BRENDA; 1.11.1.6; 3250.
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   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; PTHR11465; 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; SSF56634; 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; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT   CHAIN           1..505
FT                   /note="Catalase"
FT                   /id="PRO_0000085019"
FT   ACT_SITE        58
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         341
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:0000250"
SQ   SEQUENCE   505 AA;  57066 MW;  2A27C4BEC47BE854 CRC64;
     MGEKNSSKVL TTGFGIPVGD DQNSLTAGNR GPVLMQDVHL LDKLSHFDHE RIPERVVHAK
     GAGAGGYFEV TADVTKYTKA KFLSEIGKRT EVFVRFSTVG GEKGSADSAR DPRGFAVKFY
     TEDGNYDLVG NNTPVFFIRD PLKFPDFIHT QKRNPATNCK DPDMFWDFLS LTPESIHQVT
     ILFSDRGTPA TYRNMNGYSS HTYKWYNEKG EYFWVQYHFK TDQGIKNLTL EEAEKIGGSD
     PDHATRDLYE AIKKGDYPSW TLEMQIMTPE QAEDYRFDIR DITKVWPHGD FPTMKIGKLV
     LNRNPTNYFA EVEQAAFSPA NLVPGIGISP DKMLQGRVFS YHDTHIHRLG PNYNLIPVNA
     PKYSPENSYQ RDGFMRVDAN GGSGPNYWPN SFGGPSPDSV YLEPPFGVSG LAARTLYTHP
     NDDFVQAGNL YRDVMTDYDR ENLVGNIVSH LSAAQKRIQL RQTALFFKAD RDYGSRVAKG
     LELDIKEVER LANMTNEERA RATER