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Database: UniProt/TrEMBL
Entry: I2DIA5_9BURK
LinkDB: I2DIA5_9BURK
Original site: I2DIA5_9BURK 
ID   I2DIA5_9BURK            Unreviewed;       362 AA.
AC   I2DIA5;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Catalase-related peroxidase {ECO:0000256|PIRNR:PIRNR000296};
DE            EC=1.11.1.- {ECO:0000256|PIRNR:PIRNR000296};
GN   ORFNames=MYA_0011 {ECO:0000313|EMBL:AFJ84381.1};
OS   Burkholderia sp. KJ006.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=416344 {ECO:0000313|EMBL:AFJ84381.1, ECO:0000313|Proteomes:UP000010108};
RN   [1] {ECO:0000313|EMBL:AFJ84381.1, ECO:0000313|Proteomes:UP000010108}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KJ006 {ECO:0000313|EMBL:AFJ84381.1,
RC   ECO:0000313|Proteomes:UP000010108};
RX   PubMed=22843575; DOI=10.1128/JB.00821-12;
RA   Kwak M.J., Song J.Y., Kim S.Y., Jeong H., Kang S.G., Kim B.K., Kwon S.K.,
RA   Lee C.H., Yu D.S., Park S.H., Kim J.F.;
RT   "Complete Genome Sequence of the Endophytic Bacterium Burkholderia sp.
RT   Strain KJ006.";
RL   J. Bacteriol. 194:4432-4433(2012).
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; CP003514; AFJ84381.1; -; Genomic_DNA.
DR   RefSeq; WP_014722112.1; NC_017920.1.
DR   AlphaFoldDB; I2DIA5; -.
DR   KEGG; buk:MYA_0011; -.
DR   PATRIC; fig|416344.3.peg.11; -.
DR   HOGENOM; CLU_045961_1_0_4; -.
DR   Proteomes; UP000010108; Chromosome 1.
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        16..40
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          24..362
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        69
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000296-1"
FT   BINDING         337
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   362 AA;  38299 MW;  5136D7C58DB11FE1 CRC64;
     MKQSSSSPPR EPGRGWWRWA VIGGAAAGVV VAFGYVGGWL APARLTPHRL VDALQTAGGG
     VHPGFRRNHA KGVCVTGYFE GSGAASAYSV APFFKPVRTP VVGRFALPGG NPYAPDSSVP
     IRSLALKLTA PDGEQWRTGM NAMPVFPVAT PKAFYEQLLA TAPDPATGKA DPAKVKAFFA
     AHPETAAFRA WVKGAKPSAS YVTESYYGLN AFYFVDAAGQ RHAVRWRVVP EQTAGAADVA
     TAADPNVLQQ DVTRRIAGGA QKWKMLVTLA EPGDPVDDAT KTWPAQRTTI DAGTLVLDRV
     EPQDSGPCRD VNYDPTVLPR GIQVSGDPLL AARSAAYADS YLRRTSEEAG VAGAARLTAE
     GR
//
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