ID A0A0D1LCQ3_9MYCO Unreviewed; 351 AA.
AC A0A0D1LCQ3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE RecName: Full=Catalase-related peroxidase {ECO:0000256|PIRNR:PIRNR000296};
DE EC=1.11.1.- {ECO:0000256|PIRNR:PIRNR000296};
GN ORFNames=TL10_28415 {ECO:0000313|EMBL:KIU13716.1};
OS Mycolicibacterium llatzerense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=280871 {ECO:0000313|EMBL:KIU13716.1, ECO:0000313|Proteomes:UP000032221};
RN [1] {ECO:0000313|EMBL:KIU13716.1, ECO:0000313|Proteomes:UP000032221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CLUC14 {ECO:0000313|EMBL:KIU13716.1,
RC ECO:0000313|Proteomes:UP000032221};
RA Greninger A.L., Langelier C., Cunningham G., Chiu C.Y., Miller S.;
RT "Genome sequence of Mycobacterium llatzerense and Mycobacterium immunogenum
RT recovered from brain abscess.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has an organic peroxide-dependent peroxidase activity.
CC {ECO:0000256|PIRNR:PIRNR000296}.
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|PIRNR:PIRNR000296};
CC -!- SIMILARITY: Belongs to the catalase family.
CC {ECO:0000256|PIRNR:PIRNR000296}.
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:KIU13716.1}.
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DR EMBL; JXST01000069; KIU13716.1; -; Genomic_DNA.
DR RefSeq; WP_043399310.1; NZ_LXSC01000007.1.
DR AlphaFoldDB; A0A0D1LCQ3; -.
DR STRING; 280871.TL10_28415; -.
DR PATRIC; fig|280871.6.peg.5896; -.
DR Proteomes; UP000032221; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd08153; srpA_like; 1.
DR Gene3D; 1.20.1280.120; -; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR024168; Catalase_SrpA-type_pred.
DR PANTHER; PTHR11465; CATALASE; 1.
DR PANTHER; PTHR11465:SF9; CATALASE; 1.
DR Pfam; PF00199; Catalase; 2.
DR PIRSF; PIRSF000296; SrpA; 1.
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|PIRNR:PIRNR000296, ECO:0000256|PIRSR:PIRSR000296-2};
KW Iron {ECO:0000256|PIRNR:PIRNR000296, ECO:0000256|PIRSR:PIRSR000296-2};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR000296,
KW ECO:0000256|PIRSR:PIRSR000296-2};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000296};
KW Peroxidase {ECO:0000256|PIRNR:PIRNR000296};
KW Reference proteome {ECO:0000313|Proteomes:UP000032221};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 20..351
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 66
FT /evidence="ECO:0000256|PIRSR:PIRSR000296-1"
FT BINDING 330
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:PIRSR000296-2"
SQ SEQUENCE 351 AA; 37071 MW; D492846FA186E46C CRC64;
MDGPSWRGTP LTRRSILVGL GAVGAFLAVD LGLVAYTSRA GTLTRQTFLD GFQKVFGDHP
GFRKNHAKGV SVVGHFMSNG NAAALSRAAV FGPGEAPVAG RFSLAGGNPT VADTPGAARG
LGLAIGFPGT GQWRTAMLNI PVFLDNSPQG FYDRLLASKP LAGTGKPDPK VMADFLSRHP
ETAAAMALVK KSPPAPGFAD STFWGLNTFY LVNHSGARTP VRWSFVPQQT ALPPKSDDPN
ALFDALILQL KKAPLQWNLR LTVGRDSDPI DPTLPWPADR QVIDAGVLTL TEAQTDAAGN
ARDINFDPLV LPDGIEPSDD PLLSARSAVY AGSYRARTTE PKTAPAVQVT P
//
