ID B0KUV7_PSEPG Unreviewed; 350 AA.
AC B0KUV7;
DT 18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=Catalase-related peroxidase {ECO:0000256|PIRNR:PIRNR000296};
DE EC=1.11.1.- {ECO:0000256|PIRNR:PIRNR000296};
GN OrderedLocusNames=PputGB1_2895 {ECO:0000313|EMBL:ABY98789.1};
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869 {ECO:0000313|EMBL:ABY98789.1, ECO:0000313|Proteomes:UP000002157};
RN [1] {ECO:0000313|EMBL:ABY98789.1, ECO:0000313|Proteomes:UP000002157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1 {ECO:0000313|EMBL:ABY98789.1,
RC ECO:0000313|Proteomes:UP000002157};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-2008) 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; CP000926; ABY98789.1; -; Genomic_DNA.
DR RefSeq; WP_012272525.1; NC_010322.1.
DR AlphaFoldDB; B0KUV7; -.
DR KEGG; ppg:PputGB1_2895; -.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_045961_1_0_6; -.
DR Proteomes; UP000002157; 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: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; 1.
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 Metal-binding {ECO:0000256|PIRNR:PIRNR000296,
KW ECO:0000256|PIRSR:PIRSR000296-2};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000296};
KW Peroxidase {ECO:0000256|PIRNR:PIRNR000296}.
FT DOMAIN 23..350
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 65
FT /evidence="ECO:0000256|PIRSR:PIRSR000296-1"
FT BINDING 332
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 350 AA; 37610 MW; 0418AB68B99AF62C CRC64;
MTMNSPLHGP AKALRLAAIG AVMLAAGAGF AYAAGWLGEP RLTPQRIIDT FEAQAGHYPG
YRKNHAKGLC VSGYFQPSGQ AANLSIARAF SQQRVPVIGR FAIGGANPFA PDTGIPVRSL
AVQLSTDDGQ VWRTGMNNPP VLAVSTPQGF YEQVLAGAPD PATGKPNPAK MQAFFAAHPE
SVAFRQWAAS YKPSDSFAST QYHSINAFRL IDSAGTAHPV RWQLEPQTAF AALPGQVDDK
QFLQHDLQQR LAQAPLRWTL RLVLAEPGDA VDDPARLWPA ERRSVDAGTL VLEHVDAPEQ
GACRDLNFDP LILPRGIEAS GDPILAARSA AYSESFNRRS RESLSTGARP
//
