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Database: UniProt
Entry: A0A1D8RT98_9GAMM
LinkDB: A0A1D8RT98_9GAMM
Original site: A0A1D8RT98_9GAMM 
ID   A0A1D8RT98_9GAMM        Unreviewed;       331 AA.
AC   A0A1D8RT98;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Catalase-related peroxidase {ECO:0000256|PIRNR:PIRNR000296};
DE            EC=1.11.1.- {ECO:0000256|PIRNR:PIRNR000296};
GN   ORFNames=A3Q34_05460 {ECO:0000313|EMBL:AOW76356.1};
OS   Colwellia sp. PAMC 20917.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Colwelliaceae; Colwellia.
OX   NCBI_TaxID=1816218 {ECO:0000313|EMBL:AOW76356.1, ECO:0000313|Proteomes:UP000177820};
RN   [1] {ECO:0000313|EMBL:AOW76356.1, ECO:0000313|Proteomes:UP000177820}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 20917 {ECO:0000313|EMBL:AOW76356.1,
RC   ECO:0000313|Proteomes:UP000177820};
RA   Kim H.-W.;
RT   "Complete genome sequence of Colwellia sp. PAMC 20917.";
RL   Submitted (MAR-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; CP014944; AOW76356.1; -; Genomic_DNA.
DR   RefSeq; WP_070374441.1; NZ_CP014944.1.
DR   AlphaFoldDB; A0A1D8RT98; -.
DR   STRING; 1816218.A3Q34_05460; -.
DR   KEGG; coz:A3Q34_05460; -.
DR   OrthoDB; 255727at2; -.
DR   Proteomes; UP000177820; Chromosome.
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   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:UP000177820};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..331
FT                   /note="Catalase-related peroxidase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5009437209"
FT   DOMAIN          9..328
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        55
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000296-1"
FT   BINDING         320
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   331 AA;  35806 MW;  C4CB2C56B499B0DD CRC64;
     MKHNLITSSI SAFFLIATAT ATSTAAATDK EVVANDFVEI FEKLGGKHPG YRKAHAKGLC
     ASGTFVPTPN QHFTGAALLS NGELPVSIRF SVGGSNPNSD EKAAGTRGMG MQIKLPDGSF
     HTFTGNNFPV FAGKNPEVFH GFLSTLLPDE NGKTDPAKTM AYIQQHPSVQ ANAIWNKTAK
     TAASFANTEF FGLHTFYFDQ PNQQKTKFRW TIEPNLGVKT LEKAEAAKMP TEFLADTFAQ
     QLKDETVSFN IMASLGEAQD SDIDPSQQWP SERPQVMLGT VTVNTSGSDA CKNTNFDPNM
     MSAGFTPSDD PVLRMRSPAY AISFGKRLSG Q
//
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