ID M1UCR8_9CORY Unreviewed; 517 AA.
AC M1UCR8;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Catalase {ECO:0000313|EMBL:AGG65680.1};
GN ORFNames=H924_01120 {ECO:0000313|EMBL:AGG65680.1};
OS Corynebacterium callunae DSM 20147.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1121353 {ECO:0000313|EMBL:AGG65680.1, ECO:0000313|Proteomes:UP000011760};
RN [1] {ECO:0000313|EMBL:AGG65680.1, ECO:0000313|Proteomes:UP000011760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20147 {ECO:0000313|EMBL:AGG65680.1,
RC ECO:0000313|Proteomes:UP000011760};
RA Ruckert C., Albersmeier A., Kalinowski J.;
RT "The complete genome sequence of Corynebacterium callunae DSM 20147.";
RL Submitted (FEB-2013) 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; CP004354; AGG65680.1; -; Genomic_DNA.
DR RefSeq; WP_015650135.1; NZ_ATVF01000008.1.
DR AlphaFoldDB; M1UCR8; -.
DR STRING; 1121353.H924_01120; -.
DR KEGG; ccn:H924_01120; -.
DR PATRIC; fig|1121353.3.peg.234; -.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_010645_2_0_11; -.
DR OrthoDB; 3169619at2; -.
DR Proteomes; UP000011760; 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 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; 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; 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}.
FT DOMAIN 24..407
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 71
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 143
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 353
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 517 AA; 58708 MW; 411B3BDC41EC8A4C CRC64;
MSEKSAADQI LDRGMRAKVS GNTTRHNGAP VPSENISVTA GPQGPNILND IHLIEKLAHF
NRENVPERIP HAKGHGAFGE LHITEDVSEY TKADLFQPGK VTPMAARFST VAGEQGSPDT
WRDVHGFALR FYTEEGNYDI VGNNTPTFFL RDGMKFPDFI HSQKRLNKNG LRDADMQWDF
WTRTPESAHQ VTYVMGDRGT PKTSRHQDGF GSHTFQWINA EGKPVWVKYH FKTRQGWDCF
TDAEAAKVAG ENADYQREDL YNAIENGDYP IWDVKVQIMP FEDAENYRWN PFDLTKTWSQ
KDYPLIPVGY FILNRNPRNF FAQIEQIALD PGNIVPGIGL SPDRMLMARA FAYADQQRYR
IGANYRDLPV NRPLNDVNTY SREGAMQYVF DAEGEPSYNP NRYDKGAGYL DNGENSSSNH
TTYGQAQDIY VNPDPHGTDL TRAAYVKHED DDDFMQAGIL YREVLDDAAK ERLADNISNA
MQGISEATEP RVYEYWINVD ANLGARVKEL YLQKKGA
//
