ID B2JP08_PARP8 Unreviewed; 353 AA.
AC B2JP08;
DT 10-JUN-2008, integrated into UniProtKB/TrEMBL.
DT 10-JUN-2008, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE RecName: Full=Catalase-related peroxidase {ECO:0000256|PIRNR:PIRNR000296};
DE EC=1.11.1.- {ECO:0000256|PIRNR:PIRNR000296};
DE Flags: Precursor;
GN OrderedLocusNames=Bphy_5484 {ECO:0000313|EMBL:ACC74561.1};
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC74561.1, ECO:0000313|Proteomes:UP000001192};
RN [1] {ECO:0000313|Proteomes:UP000001192}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815
RC {ECO:0000313|Proteomes:UP000001192};
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
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; CP001044; ACC74561.1; -; Genomic_DNA.
DR RefSeq; WP_012404725.1; NZ_CADFGH010000008.1.
DR AlphaFoldDB; B2JP08; -.
DR STRING; 391038.Bphy_5484; -.
DR KEGG; bph:Bphy_5484; -.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_045961_1_0_4; -.
DR OrthoDB; 255727at2; -.
DR Proteomes; UP000001192; Chromosome 2.
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 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:UP000001192};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..352
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 334..353
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 64
FT /evidence="ECO:0000256|PIRSR:PIRSR000296-1"
FT BINDING 329
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 353 AA; 37973 MW; F65CBDDA883FC520 CRC64;
MADRPGSQAS AVRSLILIAI IVGILAIAFV YTAGWLSPSR LTPVKIVNAL APPSGPALGF
RRNHAKGICF TGTFESSGAA AALSKAPMFA QGSYRVTGRF NLATPDAKAA DPSVRVRGLS
LRVVAPDGSE WRSAMIDAPF FPVATPQAFY ALLEASARKD DPDAMKAFIA AHPEFAAFGA
WATTAPWTAS YAQDQYNSLN SFIFTNAQGE DQTVRWSFVP AAKPEPMSVD ELKQRPADFL
ETDITQRVRN APQRWSMIVI VANPGDPTAD PSKAWPEDRR KVEAGTLVVS VIEPEPDGPC
RDINFDPTVL PAGIHVSDDP FPAARSAAYS VSFNRRSAED KDYPHTPAEG AKQ
//
