ID A0A1Q5R6Q4_9BRAD Unreviewed; 331 AA.
AC A0A1Q5R6Q4;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Catalase-related peroxidase {ECO:0000256|PIRNR:PIRNR000296};
DE EC=1.11.1.- {ECO:0000256|PIRNR:PIRNR000296};
GN ORFNames=AC629_39320 {ECO:0000313|EMBL:OKO71362.1};
OS Bradyrhizobium sp. NAS80.1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1680159 {ECO:0000313|EMBL:OKO71362.1, ECO:0000313|Proteomes:UP000186592};
RN [1] {ECO:0000313|EMBL:OKO71362.1, ECO:0000313|Proteomes:UP000186592}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAS80.1 {ECO:0000313|EMBL:OKO71362.1,
RC ECO:0000313|Proteomes:UP000186592};
RA Granada C., Sant'Anna F.H., Passaglia L.;
RT "Genome of Bradyrhizobium sp. NAS80.1.";
RL Submitted (JUL-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:OKO71362.1}.
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DR EMBL; LGHL01000257; OKO71362.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5R6Q4; -.
DR Proteomes; UP000186592; Unassembled WGS sequence.
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:SF62; CATALASE T; 1.
DR Pfam; PF00199; Catalase; 1.
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.
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 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..331
FT /note="Catalase-related peroxidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5010382224"
FT DOMAIN 6..330
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 53
FT /evidence="ECO:0000256|PIRSR:PIRSR000296-1"
FT BINDING 322
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 331 AA; 34904 MW; 3CABAF542F67EA59 CRC64;
MRSFQRIAVG IAFSALMAAG ATGAGAEDEP LGVRLVNQMN ALYGQHAGVR ANHAKGAVFE
GTFTPAQGAD TFSSAAFLKG APTPLVVRFS NAGGVPDAPD THPSTDRIRG MAIKFRLSDG
SEQDIVCISA NGFPVATGED FLALLQAVGA SGPDAPKPTP VEKFLLTHPA ASAFVATPRP
VAVSYGTQPF FGVNAFKFTN AQGTSKFGRY RIVPESGPAY VSDEEATKRP PNALADNLRA
SLEKGPVKFH LLVQVAATDD PITDATKVWP DSRSTVELGE IAVIKALDTK KVENELLFLP
TNVTTGIDAS DDPIINTRTE AYAESFGRRT K
//
