ID A0A161J1X3_9GAMM Unreviewed; 362 AA.
AC A0A161J1X3;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Catalase-related peroxidase {ECO:0000256|PIRNR:PIRNR000296};
DE EC=1.11.1.- {ECO:0000256|PIRNR:PIRNR000296};
GN ORFNames=ATSB10_00410 {ECO:0000313|EMBL:AND67495.1};
OS Dyella thiooxydans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=445710 {ECO:0000313|EMBL:AND67495.1, ECO:0000313|Proteomes:UP000077255};
RN [1] {ECO:0000313|EMBL:AND67495.1, ECO:0000313|Proteomes:UP000077255}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATSB10 {ECO:0000313|EMBL:AND67495.1,
RC ECO:0000313|Proteomes:UP000077255};
RA Lee Y., Hwangbo K., Chung H., Yoo J., Kim K.Y., Sa T.M., Um Y.,
RA Madhaiyan M.;
RT "Complete genome sequencing and analysis of ATSB10, Dyella thiooxydans
RT isolated from rhizosphere soil of sunflower (Helianthus annuus L.).";
RL Submitted (FEB-2016) 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}.
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DR EMBL; CP014841; AND67495.1; -; Genomic_DNA.
DR RefSeq; WP_063669887.1; NZ_CP014841.1.
DR AlphaFoldDB; A0A161J1X3; -.
DR STRING; 445710.ATSB10_00410; -.
DR KEGG; dtx:ATSB10_00410; -.
DR PATRIC; fig|445710.3.peg.41; -.
DR OrthoDB; 255727at2; -.
DR Proteomes; UP000077255; Chromosome.
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:UP000077255};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..359
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 342..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 67
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 362 AA; 38785 MW; 524576727EC2A6DE CRC64;
MHDPQPLSRP PRNGLRWALI AGAVVVAGGA FAYVGGWLTS HRLTAQRLVD ELQRNGGGVH
PGYRRNHAKG VCVAGYFEGN GNASAYSTAS VFAVGRTPVV GRFAIPGGNP YAPDGSVPIR
SLALRFNLPN GQQWRTGMNS MPVFPVATPQ AFYAQQVASR KDPATGKPDP AKLAAFFAAH
PETAAFRAWA KTARPSASFI TESYYGLDAF YFIDAQGGRH AVRWRMAPEA TDTNPAPAGD
DNYLVSDLKQ RLARGPQRWH LLVTLAAPGD PTDDATKVWP ADRTTIDAGT LVLTGEQPQD
NGPCRDINYD PTVLPAGIAI SDDPLLPARS AAYADSYLRR TREEAHVPGT TAPTHAPPEA
AR
//
