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Database: UniProt
Entry: A0A0F4QSW6_9GAMM
LinkDB: A0A0F4QSW6_9GAMM
Original site: A0A0F4QSW6_9GAMM 
ID   A0A0F4QSW6_9GAMM        Unreviewed;       310 AA.
AC   A0A0F4QSW6;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=Catalase-related peroxidase {ECO:0000256|PIRNR:PIRNR000296};
DE            EC=1.11.1.- {ECO:0000256|PIRNR:PIRNR000296};
GN   ORFNames=TW85_18940 {ECO:0000313|EMBL:KJZ10801.1};
OS   Marinomonas sp. S3726.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=579484 {ECO:0000313|EMBL:KJZ10801.1, ECO:0000313|Proteomes:UP000033747};
RN   [1] {ECO:0000313|EMBL:KJZ10801.1, ECO:0000313|Proteomes:UP000033747}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S3726 {ECO:0000313|EMBL:KJZ10801.1,
RC   ECO:0000313|Proteomes:UP000033747};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT   bacteria.";
RL   BMC Genomics 16:158-158(2015).
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:KJZ10801.1}.
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DR   EMBL; JXYC01000025; KJZ10801.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F4QSW6; -.
DR   PATRIC; fig|579484.3.peg.3886; -.
DR   Proteomes; UP000033747; Unassembled WGS sequence.
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   Gene3D; 1.20.1280.120; -; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR020835; Catalase_sf.
DR   InterPro; IPR024168; Catalase_SrpA-type_pred.
DR   PANTHER; PTHR11465; CATALASE; 1.
DR   PANTHER; PTHR11465:SF9; CATALASE; 1.
DR   PIRSF; PIRSF000296; SrpA; 1.
DR   SUPFAM; SSF56634; Heme-dependent catalase-like; 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:UP000033747}.
FT   ACT_SITE        40
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000296-1"
FT   BINDING         299
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   310 AA;  34285 MW;  432F61D205E37938 CRC64;
     MGAVLVAVQA LPAMADKTAL STVNSFEKLF GVTEGERRNH SKGFCFTGTL QPMDKRMTLY
     STSPLFKYES QVIGRLSHKG GNFHATDNKP AEYGMGLSIK PATGKPHMMS MNTLDFFPVS
     TPEAFAELMK AKAEGKAAVK AFKESSKELQ NFKAHNATKT KTLTPYEGTQ FNSINSFYLE
     NDLGKKTAIR WSFKPVNEQG VVLEPTHNFF YQNLQKNLAA GEISWDMVIT LANKEDAIDN
     AAIPWKGNHT QIIGARLKVT AISHQEAGTC KNLNFDPLVL SDGFHPSNDP LLQARRNAYA
     ISFGRRLSEQ
//
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