ID A0A1S2P1C7_9ACTN Unreviewed; 490 AA.
AC A0A1S2P1C7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN ORFNames=BIV24_24465 {ECO:0000313|EMBL:OIJ87527.1};
OS Streptomyces colonosanans.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1428652 {ECO:0000313|EMBL:OIJ87527.1, ECO:0000313|Proteomes:UP000179935};
RN [1] {ECO:0000313|EMBL:OIJ87527.1, ECO:0000313|Proteomes:UP000179935}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MUSC 93 {ECO:0000313|EMBL:OIJ87527.1,
RC ECO:0000313|Proteomes:UP000179935};
RA Lee L.-H., Ser H.-L., Law J.W.-F.;
RT "Genome sequence of Streptomyces sp. MUSC 93.";
RL Submitted (OCT-2016) 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}.
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:OIJ87527.1}.
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DR EMBL; MLYP01000064; OIJ87527.1; -; Genomic_DNA.
DR RefSeq; WP_071368589.1; NZ_MLYP01000064.1.
DR AlphaFoldDB; A0A1S2P1C7; -.
DR STRING; 1428652.BIV24_24465; -.
DR OrthoDB; 3169619at2; -.
DR Proteomes; UP000179935; 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; 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:UP000179935}.
FT DOMAIN 13..397
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 60
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 133
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 343
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 490 AA; 54752 MW; 13F47A5A20AB9019 CRC64;
MTQEAHVSQG PLTTEAGAPV ADNQNSETAG VGGPVLVQDQ LLLEKLAHFN RERIPERVVH
ARGAGAYGTF TVTADVTRYT RAAFLSEVGK QTETFLRFST VAGNLGAADA VRDPRGFALK
FYTEEGNYDL VGNNTPVFFI KDAIKFPDFI HTQKRDPYTG SQEADNVWDF WGLSPESTHQ
VTWLFGDRGI PASYRHMNGY GSHTYQWNNE AGEVFWVKYH FKTDQGIKNL TQEEAVKLAG
EDPDSHQRDL REAIERGEFP TWTVQVQIMP AADAATYRFN PFDLTKVWPH EDYPPIEIGK
LELNRNPENI FAEVEQSIFS PAHFVPGIGP SPDKMLQGRL FAYGDAHRYR VGINADHLPV
NRPHATEART NSRDGFLYDG RHKGAKNYEP NSFGGPFQTD KPLWQSTSNF TAGTGNHEAP
VHSEDNDFVQ AGNLYRLMSE GEKERLIANL AGFISKVSRD DIAERAIGNF RQADGDFGKR
LEAAVQVLRG
//
