ID A0A2B8AMV1_9ACTN Unreviewed; 552 AA.
AC A0A2B8AMV1;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Catalase {ECO:0000313|EMBL:PGH47686.1};
GN ORFNames=CRI70_27055 {ECO:0000313|EMBL:PGH47686.1};
OS Streptomyces sp. Ru87.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2044307 {ECO:0000313|EMBL:PGH47686.1, ECO:0000313|Proteomes:UP000222409};
RN [1] {ECO:0000313|EMBL:PGH47686.1, ECO:0000313|Proteomes:UP000222409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ru87 {ECO:0000313|EMBL:PGH47686.1,
RC ECO:0000313|Proteomes:UP000222409};
RA Amin D.H., Borsetto C., Abolmaaty A., Tolba S., Abdallah N.A.,
RA Wellington E.M.H.;
RT "Draft genome sequence of Streptomyces sp. Ru87 isolated from Egyptian
RT soil.";
RL Submitted (OCT-2017) 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 -!- 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PGH47686.1}.
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DR EMBL; PDIX01000446; PGH47686.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2B8AMV1; -.
DR OrthoDB; 3169619at2; -.
DR Proteomes; UP000222409; Unassembled WGS sequence.
DR GO; GO:0004096; F:catalase activity; IEA:InterPro.
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; 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; 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 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 Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000222409}.
FT DOMAIN 19..412
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 66
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 144
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
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 552 AA; 63177 MW; 2C9CA7222136FA3C CRC64;
MTDASSKGAG RADDRPVLTN RQGHPVYDNQ NQRTVGARGP ATLENYQFLE KISHFDRERI
PERVVHARGV TAYGWFEAYG AWGDEPIDRY TRAKLFQERG RRTDVAVRFS TVIGGRDSSE
AARDPRGFAV KFYTEDGNWD LVGNNLAVFF IRDAIKFPDV IHALKPDPVT FEQQPRRIFD
FMSQTPECMH MLVNLFSPRG IPADYRHMQG FGVNTYKWVD AKGDTKLVKY TWMPKQGVRS
MTEEDAANVQ ADSTGHATKD LYEAVERGDY PEWELLVQMM DDHEHPELDF DPLDDTKTWP
EQDFPPKPVG RMVLDRMPAN YFAENEQISF GTGVLVDGLD FSDDKMLVGR TFSYSDTQRY
RVGPNYLQLP VNQAKHVEVH TNQRDGQMTY HVDGGAENTH INYEPSVMGG LREGHYPTHE
EQGPEIHGRL TRKRIPRTND YLQAGQRYLL LEDWERDELV GNFVTLLSQC DRPVQERMLW
HFLLVENDLG LRVGEGLGIS TADVAHLEPL PGQQLTDEDR ERLANLGKNP PRNVEGLTMT
HCVPDERHVV TR
//
