ID A0A1G6IVX0_9BACL Unreviewed; 650 AA.
AC A0A1G6IVX0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=catalase {ECO:0000256|ARBA:ARBA00012314};
DE EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314};
GN ORFNames=SAMN04488112_10368 {ECO:0000313|EMBL:SDC10573.1};
OS Melghirimyces thermohalophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Melghirimyces.
OX NCBI_TaxID=1236220 {ECO:0000313|EMBL:SDC10573.1, ECO:0000313|Proteomes:UP000199387};
RN [1] {ECO:0000313|EMBL:SDC10573.1, ECO:0000313|Proteomes:UP000199387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45514 {ECO:0000313|EMBL:SDC10573.1,
RC ECO:0000313|Proteomes:UP000199387};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRSR:PIRSR038927-2};
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DR EMBL; FMZA01000003; SDC10573.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6IVX0; -.
DR STRING; 1236220.SAMN04488112_10368; -.
DR Proteomes; UP000199387; Unassembled WGS 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; 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; 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; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR PROSITE; PS00438; CATALASE_2; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038927-3};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038927-2};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR038927-2};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000199387}.
FT DOMAIN 2..390
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 46
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 86
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 135
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 332
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 336
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 343
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ SEQUENCE 650 AA; 74035 MW; 505E0F4308D2E376 CRC64;
MTTNEGRKRS QDQDQLKAGV RGPTLRQDYE FFEKMSHFVH EEIPERVVHA RGYSAHGEFE
CYQSMKHVTK AGFLQEAGKK TPLTVRFSTV QGPKGSYDTA RDLRCQGVKL YTEDGNLDLT
TIAMPVLINN DAMKFPDAMH AFQSKQDDDI PTATGAHDRF WDYVANNPEA LHMVQWIMSD
RGILRSYRMM ESWSINTYLF VNDQGKATFM RYVWKPVLGV HSLLQDEALT IGGLDPDFHR
RDLREAIDHG AYPEYELGVQ LIPMEDEFKY DFDVLDPAKF WPEELVPVQI IGKMTLNRNI
DNYFTESEQV AFNPANVVPG IDFSNDPVLQ GRLMAYRDAQ QHRLGSANYD ELPINRPVCP
FHNNQRRGYM RQRIDVDQVN YHQNSLANNT PYTTSPEEGG YEHYPKKVEG HVIRARSESF
KDYFSQPRIF WNSMTPVERQ HTIEAFSYQL GRVKSKSVRQ QNVNLLVNVD KEMACIIADN
IGVDRPSGSH VPLSTSYPSL SQANTPRNAK TQKVGVLIGN GFNGKEVTNV LNYLQQCVVF
VEVISETLGT VTGADGTEIK VDKTFLTTSP YLLDSLYVVG GQSKNETKFH QDITDFVNTA
YKHYKPIGVA TNAQSFFQKA AEGVVFAEAN PDFEEKFVAA IGQQRFWDRK
//
