ID L1MLH8_9CORY Unreviewed; 524 AA.
AC L1MLH8;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN ORFNames=HMPREF9997_00450 {ECO:0000313|EMBL:EKX91789.1};
OS Corynebacterium durum F0235.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1035195 {ECO:0000313|EMBL:EKX91789.1, ECO:0000313|Proteomes:UP000010445};
RN [1] {ECO:0000313|EMBL:EKX91789.1, ECO:0000313|Proteomes:UP000010445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0235 {ECO:0000313|EMBL:EKX91789.1,
RC ECO:0000313|Proteomes:UP000010445};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) 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=1.11.1.6;
CC Evidence={ECO:0000256|ARBA:ARBA00000720,
CC ECO:0000256|RuleBase:RU000498};
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, ECO:0000256|RuleBase:RU000498}.
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:EKX91789.1}.
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DR EMBL; AMEM01000009; EKX91789.1; -; Genomic_DNA.
DR RefSeq; WP_006062702.1; NZ_KB290827.1.
DR AlphaFoldDB; L1MLH8; -.
DR STRING; 1035195.HMPREF9997_00450; -.
DR PATRIC; fig|1035195.3.peg.407; -.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_010645_2_0_11; -.
DR OrthoDB; 3169619at2; -.
DR Proteomes; UP000010445; Unassembled WGS sequence.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
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; IPR002226; Catalase_haem_BS.
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; PS00437; CATALASE_1; 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 ECO:0000256|RuleBase:RU000498};
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 ECO:0000256|RuleBase:RU000498};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000498};
KW Reference proteome {ECO:0000313|Proteomes:UP000010445}.
FT DOMAIN 35..418
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 82
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 154
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 364
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 524 AA; 58297 MW; 1A9EDE2944FED31A CRC64;
MPHTPPNNSQ PSAADPIVSA GRCPVAHGAA ASASTNLNGA PIASENHSVT QGQQGGISLH
DIHLIEKLAH FNRERIPERV VHAKGSGAFG ELVVTEDVSA YTCAALFQPG TVTPLLLRFS
TVAGEQGSPD AWRDVRGFSL KFYTSEGNYD IVGNNTPVFF LRDGIKFPDF IHSQKRMPGS
GLRDANMQWD FWTRTPESAH QVTYVMGDRG IPKSFRHMDG FGSHTYQWIN EAGERFWVKY
HFKTRQGWEF YTDEEAARVA GENADSSRSD LYDAIARGDF PTWDVKVQIM PVDEAASYRW
NPFDLTKTWS QKDYPLIPVG HFTLNRNPEN FFAQIEQAAF APSNLVRGIG FSPDKMLLAR
VFAYADAHRY RVGANSDQLP VNRPVCPVNS YSHDGPMTYQ FQGPDQPVYS PNGYGRPAGF
QDSGTSSDVD TNLGSAGNLG LWADTHGSEF VRDAYVKHPD DDDFMQAGIL VREVLDDAAR
ERLAGNISRA MNGVTPEVEQ RVYEYWTNVD PWLGNRVREL FTSA
//
