ID A0A2S4Y145_9ACTN Unreviewed; 335 AA.
AC A0A2S4Y145;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Catalase-peroxidase {ECO:0000313|EMBL:POX42491.1};
DE Flags: Fragment;
GN ORFNames=C3486_04175 {ECO:0000313|EMBL:POX42491.1};
OS Streptomyces sp. Ru73.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2080748 {ECO:0000313|EMBL:POX42491.1, ECO:0000313|Proteomes:UP000236956};
RN [1] {ECO:0000313|EMBL:POX42491.1, ECO:0000313|Proteomes:UP000236956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ru73 {ECO:0000313|EMBL:POX42491.1,
RC ECO:0000313|Proteomes:UP000236956};
RA Suneja G., Sharma R.;
RT "Genome sequencing of cellulose degrading bacteria.";
RL Submitted (FEB-2018) 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=1.11.1.21;
CC Evidence={ECO:0000256|ARBA:ARBA00001378};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000256|ARBA:ARBA00001970};
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:POX42491.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PQSQ01000006; POX42491.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S4Y145; -.
DR Proteomes; UP000236956; 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 Gene3D; 1.10.520.10; -; 1.
DR Gene3D; 1.10.420.10; Peroxidase, domain 2; 1.
DR InterPro; IPR000763; Catalase_peroxidase.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR019794; Peroxidases_AS.
DR InterPro; IPR019793; Peroxidases_heam-ligand_BS.
DR PANTHER; PTHR30555:SF0; CATALASE-PEROXIDASE; 1.
DR PANTHER; PTHR30555; HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE; 1.
DR Pfam; PF00141; peroxidase; 1.
DR PRINTS; PR00460; BPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; Heme-dependent peroxidases; 1.
DR PROSITE; PS00435; PEROXIDASE_1; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 4: Predicted;
KW Heme {ECO:0000256|ARBA:ARBA00022617};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000313|EMBL:POX42491.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000236956}.
FT DOMAIN 144..280
FT /note="Plant heme peroxidase family profile"
FT /evidence="ECO:0000259|PROSITE:PS50873"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 335
FT /evidence="ECO:0000313|EMBL:POX42491.1"
SQ SEQUENCE 335 AA; 36385 MW; 3509C580AB6A5B7E CRC64;
MSENHDAIVT DPKTEGEAGG CPVAHTARAP HPTQGGGNRQ WWPERLNLKI LAKNQPVANP
MGEDFDYAKA FESLDLAAVK RDIQEVLTTS QDWWPADFGH YGPLMIRMAW HSAGTYRISD
GRGGAGSGQQ RFAPLNSWPD NGNLDKARRL LWPVKKKYGK NISWADLLIL TGNVALESMG
AKTFGFAGGR VDAWEPEDDV YWGPETTWLG DERYTGDREL EEPLGAVQMG LIYVNPEGPN
GNPDPLASAR DIRETFRRMA MNDEETVALI AGGHTFGKTH GAGPADAVGA DPEAAGFEEQ
GLGWKNSYGT GKGADAITSG LEVTWTSTPT KWSMG
//
