ID A0A285L9U8_9NOCA Unreviewed; 357 AA.
AC A0A285L9U8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=Catalase-related peroxidase {ECO:0000256|PIRNR:PIRNR000296};
DE EC=1.11.1.- {ECO:0000256|PIRNR:PIRNR000296};
GN ORFNames=SAMN04244553_3247 {ECO:0000313|EMBL:SNY81644.1};
OS Nocardia amikacinitolerans.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=756689 {ECO:0000313|EMBL:SNY81644.1, ECO:0000313|Proteomes:UP000219565};
RN [1] {ECO:0000313|EMBL:SNY81644.1, ECO:0000313|Proteomes:UP000219565}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45537 {ECO:0000313|EMBL:SNY81644.1,
RC ECO:0000313|Proteomes:UP000219565};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) 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}.
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DR EMBL; OBEG01000003; SNY81644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285L9U8; -.
DR STRING; 1379680.GCA_001612615_04889; -.
DR OrthoDB; 255727at2; -.
DR Proteomes; UP000219565; 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 InterPro; IPR006311; TAT_signal.
DR PANTHER; PTHR11465; CATALASE; 1.
DR PANTHER; PTHR11465:SF9; CATALASE; 1.
DR Pfam; PF00199; Catalase; 2.
DR PIRSF; PIRSF000296; SrpA; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR PROSITE; PS51402; CATALASE_3; 1.
DR PROSITE; PS51318; TAT; 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:UP000219565};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 16..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..357
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 69
FT /evidence="ECO:0000256|PIRSR:PIRSR000296-1"
FT BINDING 335
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 357 AA; 37918 MW; EBBB523AB103BAFA CRC64;
MTDAQPNSFP LNRRTLLGGA AVAALGAAGI GGFLFTENRI GPWRLTARAL VDRLQDTAGG
SFPGCRRNHA KGVAVAGYFE SNGGGVELSK ASVFRAGLYR LAGRFSLAGG NPHMPDAPTA
PRGLGLRLFL PGGEEWRMAM INIPVFLDAT PQDFYERTLA FAPDPATGKP DAATMKQYLE
SHPKTAAALG VIEQGAPAPT FAASAFFGLN AFRFTDGEGS TVPVRWRLEP DDPPPATGPG
GGDSALFDGL VADLKARPLR WRLVVVVGEP GDPTDDATRM WPSDRRAVHV GTVVLDRVDT
ESADNVQDVN FDPLVLPNGI EPSDDPLLQA RSAAYSESYR RRAGESKPTG AVLVREV
//
