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Database: UniProt
Entry: A0A2A2E109_9PSED
LinkDB: A0A2A2E109_9PSED
Original site: A0A2A2E109_9PSED 
ID   A0A2A2E109_9PSED        Unreviewed;       363 AA.
AC   A0A2A2E109;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Catalase-related peroxidase {ECO:0000256|PIRNR:PIRNR000296};
DE            EC=1.11.1.- {ECO:0000256|PIRNR:PIRNR000296};
GN   ORFNames=BZL43_06750 {ECO:0000313|EMBL:PAU60540.1};
OS   Pseudomonas sp. PICF141.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1949067 {ECO:0000313|EMBL:PAU60540.1, ECO:0000313|Proteomes:UP000217819};
RN   [1] {ECO:0000313|EMBL:PAU60540.1, ECO:0000313|Proteomes:UP000217819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PICF141 {ECO:0000313|EMBL:PAU60540.1,
RC   ECO:0000313|Proteomes:UP000217819};
RA   Gomez-Lama C., Legarda-Cristobal G., Trivino J.C., Mercado-Blanco J.;
RT   "Genome sequences of Pseudomonas strains PIC25, PIC105 and PICF141
RT   indigenous of the olive (Olea europaea L.) cv. Picual rhizosphere and
RT   effective biological control agents against Verticillium dahliae.";
RL   Submitted (JAN-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}.
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:PAU60540.1}.
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DR   EMBL; MUNM01000033; PAU60540.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2E109; -.
DR   OrthoDB; 255727at2; -.
DR   Proteomes; UP000217819; 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; 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   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   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        20..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          51..362
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        73
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000296-1"
FT   BINDING         340
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   363 AA;  38815 MW;  67EA0B3549DE7EB0 CRC64;
     MVDRSSTTGP SRPPLSGASL TLRLTGIAVV VAALAGAFAY VNGTLDPQRL TPKDLVNVLE
     KNNGVHPGFR RNHAKGVCVI GHFESSNQAR EYSSAQVFSE ARTPVVGRFA LPAGNPYAPD
     NSVPIRSLAL RFSQANGQQW RTGMNSMPVF PVGTPEAFYQ LQQAQSPDPA TGKPNPAAVS
     AFFGSHPEAA PFLAWIKTAK PSASYATETY NSVNAFYLVN AAGQRQAVRW SMTPLAQDAA
     GATAAEGSDF LEKDLVQRLS AGPLRWQLNI TLANPGDPTN DASKVWPDGR KVLNAGTLVL
     ESTQPQLNGE CRDINYDPLV LPSGIEGSDD PLLAARSAGY ARSYLRRASE VKQLPNAKQE
     SQQ
//
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