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
//