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Database: UniProt
Entry: A0A1C5IM52_9ACTN
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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
//
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