ID A0A345XWY8_9ACTN Unreviewed; 486 AA.
AC A0A345XWY8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Catalase {ECO:0000313|EMBL:AXK36154.1};
GN ORFNames=DVA86_29750 {ECO:0000313|EMBL:AXK36154.1};
OS Streptomyces armeniacus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=83291 {ECO:0000313|EMBL:AXK36154.1, ECO:0000313|Proteomes:UP000254425};
RN [1] {ECO:0000313|EMBL:AXK36154.1, ECO:0000313|Proteomes:UP000254425}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15676 {ECO:0000313|EMBL:AXK36154.1,
RC ECO:0000313|Proteomes:UP000254425};
RA Labana P., Gosse J.T., Boddy C.N.;
RT "Draft genome of the type strain Streptomyces armeniacus ATCC 15676.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP031320; AXK36154.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A345XWY8; -.
DR Proteomes; UP000254425; Chromosome.
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; 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; 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; 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 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:UP000254425}.
FT DOMAIN 6..388
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 53
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 125
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 335
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 486 AA; 55138 MW; 10BD3D91A9B22202 CRC64;
MTEHTTNNAG IPVESDEHSL TVGSDGPILL QDHYLIEKMA QFNRERVPER VVHAKGGGAY
GTFEVTNDVS QFTKADLFQP GKRTGMLARF STVAGEQGSP DTWRDPRGFA LKFYTEHGNY
DLVGNNTPIF FVRDPIKFQD FIRSQKRRPD SGLRDNDMQW DFWTLSPESA HMVTWLMGDR
GVPRTWRHMN GYGSHTYLWV NGGGEKFWVK YHIKTDQGID FLTQTEADDL AGADGDYHRR
DLYEAIRLGE APSWTMHVQV MPFADAPDYR FNPFDLTKVW PHGDYPLIEV GRMTLDRNPE
DFFIHIEQAA FEPANLVPGI GPSPDKMLLG RLHSYPDTHR YRIGPNYAQL PPNRPQVPVR
SYAKDGPMRY EPSHTARPYA PNSYGGPAAD TARFGEPAGW ATEGEMVREA YKPRRDDDDW
GQAGTMVRQV LDDAARERLV GNVSGHLLGG VSRPVLDRAL QYWRNIDKDL GDRIATTVEE
GAERPR
//