ID A0A1C5IM52_9ACTN Unreviewed; 495 AA.
AC A0A1C5IM52;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Catalase {ECO:0000313|EMBL:SCG58886.1};
GN ORFNames=GA0070613_3021 {ECO:0000313|EMBL:SCG58886.1};
OS Micromonospora inositola.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47865 {ECO:0000313|EMBL:SCG58886.1, ECO:0000313|Proteomes:UP000198221};
RN [1] {ECO:0000313|EMBL:SCG58886.1, ECO:0000313|Proteomes:UP000198221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43819 {ECO:0000313|EMBL:SCG58886.1,
RC ECO:0000313|Proteomes:UP000198221};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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}.
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DR EMBL; LT607754; SCG58886.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C5IM52; -.
DR OrthoDB; 3169619at2; -.
DR Proteomes; UP000198221; Chromosome i.
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:UP000198221}.
FT DOMAIN 11..405
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 58
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 136
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 346
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 495 AA; 56405 MW; F2B3FD14201529B7 CRC64;
MSDQAGKPIL TTRQGHPVHN NQQQRTVGSR GPATLENYHF LEKISHFDRE RIPERVVHAR
GFVAHGEFEA YGTIGDQPAA KYTRAKLFQT KGRKTPVTIR FSTVIGGRDS SEAARDPRGF
AVKFRTEDGN WDMVGNNLQV FFIRDAIKFP DVIHSLKPDP VTFRQEPNRI FDFMSNTPES
MHMLTWLFSP YGIPKNYRTM RGSGVNTYRL VNAEGEGVLV KFHWLTQQGE HNLTQAEADA
IQATELGHAS KDLYEAIERG EFPQWELNVQ IVSDDEHPEL DFDPLDDTKI WPEEQFPYLP
VGMMTLNRNI TDHHNENEQI AFGTGVLIDG IDFSDDKMLV GRTFSYSDTQ RYRVGPNYLQ
LPINRPREDV LVSTNQGGGQ MSYGVDNRGG NPHINFEPSS VAGLAEADDS YREYRPFVSG
QIMKAPIERQ SNYAQAGRRY REMADWERDD LILNLTTLLA QCDKHIQEKM VWHFSQCDEE
YGRRVAEGLG ISVSA
//