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Database: UniProt/TrEMBL
Entry: A0A0E3S4L6_9EURY
LinkDB: A0A0E3S4L6_9EURY
Original site: A0A0E3S4L6_9EURY 
ID   A0A0E3S4L6_9EURY        Unreviewed;       505 AA.
AC   A0A0E3S4L6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=MSLAZ_1915 {ECO:0000313|EMBL:AKB75176.1};
OS   Methanosarcina lacustris Z-7289.
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=1434111 {ECO:0000313|EMBL:AKB75176.1, ECO:0000313|Proteomes:UP000033072};
RN   [1] {ECO:0000313|EMBL:AKB75176.1, ECO:0000313|Proteomes:UP000033072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z-7289 {ECO:0000313|EMBL:AKB75176.1,
RC   ECO:0000313|Proteomes:UP000033072};
RA   Henriksen J.R., Luke J., Reinhart S., Benedict M.N., Youngblut N.D.,
RA   Metcalf M.E., Whitaker R.J., Metcalf W.W.;
RT   "Methanogenic archaea and the global carbon cycle.";
RL   Submitted (JUL-2014) 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}.
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DR   EMBL; CP009515; AKB75176.1; -; Genomic_DNA.
DR   RefSeq; WP_048126505.1; NZ_CP009515.1.
DR   AlphaFoldDB; A0A0E3S4L6; -.
DR   STRING; 1434111.MSLAZ_1915; -.
DR   GeneID; 24806695; -.
DR   KEGG; mls:MSLAZ_1915; -.
DR   PATRIC; fig|1434111.4.peg.2514; -.
DR   HOGENOM; CLU_010645_2_0_2; -.
DR   OrthoDB; 53102at2157; -.
DR   Proteomes; UP000033072; Chromosome.
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}.
FT   DOMAIN          11..396
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        58
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
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:0000256|PIRSR:PIRSR038928-2"
SQ   SEQUENCE   505 AA;  57028 MW;  C1B4013428043E05 CRC64;
     MSEKKPSKVL TTGFGIPVGD DQNSLTAGER GPVLMQDVHL LDKLSHFDRE RIPERVVHAK
     GAGAGGYFEV TADVTKYTKA KFLSKVGKRT EVFARFSTVG GERGSADAAR DPRGFAIKFY
     TEDGNHDLTG NNTPVFFIRD PLKFPDFIHT QKRNPATNCK DPDMFWDFLS LTPESIHQVT
     ILFSDRGTPA TFRNMNGYSS HTYKWYNDKG EYFWVQYHFK TDQGIKNLTR QEAEKLSGTD
     PDHATRDLYA AIEKGDYPSW TLEMQIMTPE QAENYRFDIR DITKVWPHGD FPPIKVGKLV
     LNRNPTNYFA EVEQAAFSPA NLVPGIGISP DKMLQARVFS YHDTHIHRLG PNYHLIPVNA
     PKHSPETSYQ RDGFMRVDGN QGGGPNYWPN SFDGPAPNPA FLEPPFEVSG PAARTPYNYP
     NDDFVQPGNL YRDVMTEEDR EHLVGNIVSH LSGAQKRIQL RQTALFFKAD PDYGSRVAKG
     LGLDIKEVER LANMTKEERA KATEK
//
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