ID R9T6J9_METII Unreviewed; 497 AA.
AC R9T6J9;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN ORFNames=MMINT_12710 {ECO:0000313|EMBL:AGN26602.1};
OS Methanomassiliicoccus intestinalis (strain Issoire-Mx1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata;
OC Methanomassiliicoccales; Methanomassiliicoccaceae; Methanomassiliicoccus.
OX NCBI_TaxID=1295009 {ECO:0000313|EMBL:AGN26602.1, ECO:0000313|Proteomes:UP000014070};
RN [1] {ECO:0000313|EMBL:AGN26602.1, ECO:0000313|Proteomes:UP000014070}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Issoire-Mx1 {ECO:0000313|EMBL:AGN26602.1,
RC ECO:0000313|Proteomes:UP000014070};
RX PubMed=23846268; DOI=10.1128/genomeA.00453-13;
RA Borrel G., Harris H.M., Parisot N., Gaci N., Tottey W., Mihajlovski A.,
RA Deane J., Gribaldo S., Bardot O., Peyretaillade E., Peyret P.,
RA O'Toole P.W., Brugere J.F.;
RT "Genome sequence of 'Candidatus Methanomassiliicoccus intestinalis'
RT Issoire-Mx1, a third thermoplasmatales-related methanogenic archaeon from
RT human feces.";
RL Genome Announc. 1:142-142(2013).
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; CP005934; AGN26602.1; -; Genomic_DNA.
DR RefSeq; WP_020449127.1; NC_021353.1.
DR AlphaFoldDB; R9T6J9; -.
DR STRING; 1295009.MMINT_12710; -.
DR GeneID; 41323658; -.
DR KEGG; mer:MMINT_12710; -.
DR HOGENOM; CLU_010645_2_0_2; -.
DR InParanoid; R9T6J9; -.
DR OrthoDB; 53102at2157; -.
DR Proteomes; UP000014070; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000014070}.
FT DOMAIN 6..386
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 51
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 124
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 334
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 497 AA; 56549 MW; F70C98D6C9364062 CRC64;
MKGKLTTASG SPIDDDQASI TASGYTLIQD VHLTEKLAHF NRERIPERVV HAKGTGAHGY
FEVTNDLSKY TRAAFLSEVG KKTDIFVRFS IVNTERGGPD ADRDPRGFAV KFYTEEGNYD
IVANNTPVFF VRDAIKFPDF IHSQKRNPKN NLHDYDTYWD FLSLTPESIH QVTILFTDRG
TPKDYRHMDG FGTNTFMWYN EKNEYVWIKY TFKCDQGNET LTADEAIELK GKEADHATID
LYQEIENGNY PSWTVYVQIM TPEQAKKYEF DPFDATKVWY HGDFPLIPLG KIVLNKNPEN
YFDEVEQSAF APSNMVPGIG ASPDRMLQAR LFAYTDTQRY RLGPNFQQLK INAPRALNVY
QRDGPMSYGI VGTDPNYYPN SVPDAPAPDI SYTPPASIVD DEAMRHQVPI DDVDFAQARA
LYTRVLSDKD KDHLISNIAG HLGGAKESIQ YRQTALFYKV DEDYGTRVAE ALSLDINKIM
KLAAASQEER EKITMKM
//
