ID A0A0Q5CJS2_9BURK Unreviewed; 360 AA.
AC A0A0Q5CJS2;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, 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=ASF61_14895 {ECO:0000313|EMBL:KQQ32338.1};
OS Duganella sp. Leaf126.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ32338.1, ECO:0000313|Proteomes:UP000051032};
RN [1] {ECO:0000313|EMBL:KQQ32338.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ32338.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ32338.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ32338.1};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQQ32338.1}.
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DR EMBL; LMNW01000034; KQQ32338.1; -; Genomic_DNA.
DR RefSeq; WP_056159750.1; NZ_LMNW01000034.1.
DR AlphaFoldDB; A0A0Q5CJS2; -.
DR STRING; 1736266.ASF61_14895; -.
DR Proteomes; UP000051032; 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 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 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 36..360
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 63
FT /evidence="ECO:0000256|PIRSR:PIRSR000296-1"
FT BINDING 333
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 360 AA; 38654 MW; 3C5829DE26895349 CRC64;
MSTPNPRRGS MLLLLPIAAI VAVLAALFAW VGGWFGNHQL TPQKMMDFAQ ASGKQQPGFR
RAHSKGVCFA GTFAAAPGAA TLSKARAFSQ PSIPVIGRFS ASSNNPYTPD GASPVRGMAV
QLKTNDGQEW RIAMNSFPFF AASTPQAFQA MNEAGKPDPA TGKPDPEKMK ALLAAHPEIA
AFMAWAKSAP KSDSLGNTRF NGVNAFRLTN AQGEQRMVRW SMRPRLPVVA LTPEQLKTAD
PDFLMKDLDR RLANGPLVWD LVAQIAAPGD PVTDPSKAWP DSRPEATIGT LTMVHAEPQA
TGPCRDLNFD PLILPDGIAG SDDPVLRARS AAYSVSFNRR EREIAEGKSA YPVNPHGSAR
//
