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Database: UniProt/TrEMBL
Entry: S4YLA2_SERPL
LinkDB: S4YLA2_SERPL
Original site: S4YLA2_SERPL 
ID   S4YLA2_SERPL            Unreviewed;       478 AA.
AC   S4YLA2;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE            EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN   ORFNames=M621_17390 {ECO:0000313|EMBL:AGP45301.1};
OS   Serratia plymuthica S13.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Serratia.
OX   NCBI_TaxID=1348660 {ECO:0000313|EMBL:AGP45301.1, ECO:0000313|Proteomes:UP000014900};
RN   [1] {ECO:0000313|EMBL:AGP45301.1, ECO:0000313|Proteomes:UP000014900}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S13 {ECO:0000313|EMBL:AGP45301.1};
RX   PubMed=23929484;
RA   Muller H., Furnkranz M., Grube M., Berg G.;
RT   "Genome Sequence of Serratia plymuthica Strain S13, an Endophyte with
RT   Germination- and Plant-Growth-Promoting Activity from the Flower of Styrian
RT   Oil Pumpkin.";
RL   Genome Announc. 1:e00594-13(2013).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6;
CC         Evidence={ECO:0000256|ARBA:ARBA00000720,
CC         ECO:0000256|RuleBase:RU000498};
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413;
CC         Evidence={ECO:0000256|ARBA:ARBA00001971,
CC         ECO:0000256|PIRSR:PIRSR038928-2};
CC   -!- SIMILARITY: Belongs to the catalase family.
CC       {ECO:0000256|ARBA:ARBA00005329, ECO:0000256|RuleBase:RU000498}.
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DR   EMBL; CP006566; AGP45301.1; -; Genomic_DNA.
DR   RefSeq; WP_004947182.1; NC_021659.1.
DR   AlphaFoldDB; S4YLA2; -.
DR   KEGG; sry:M621_17390; -.
DR   PATRIC; fig|1348660.3.peg.3420; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_2_0_6; -.
DR   Proteomes; UP000014900; Chromosome.
DR   GO; GO:0004096; F:catalase activity; IEA:UniProtKB-EC.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR   CDD; cd08156; catalase_clade_3; 1.
DR   Gene3D; 2.40.180.10; Catalase core domain; 1.
DR   InterPro; IPR018028; Catalase.
DR   InterPro; IPR040333; Catalase_3.
DR   InterPro; IPR024708; Catalase_AS.
DR   InterPro; IPR024711; Catalase_clade1/3.
DR   InterPro; IPR011614; Catalase_core.
DR   InterPro; IPR002226; Catalase_haem_BS.
DR   InterPro; IPR010582; Catalase_immune_responsive.
DR   InterPro; IPR020835; Catalase_sf.
DR   PANTHER; PTHR11465; CATALASE; 1.
DR   PANTHER; PTHR11465:SF61; CATALASE; 1.
DR   Pfam; PF00199; Catalase; 1.
DR   Pfam; PF06628; Catalase-rel; 1.
DR   PIRSF; PIRSF038928; Catalase_clade1-3; 1.
DR   PRINTS; PR00067; CATALASE.
DR   SMART; SM01060; Catalase; 1.
DR   SUPFAM; SSF56634; Heme-dependent catalase-like; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
DR   PROSITE; PS00438; CATALASE_2; 1.
DR   PROSITE; PS51402; CATALASE_3; 1.
PE   3: Inferred from homology;
KW   Heme {ECO:0000256|ARBA:ARBA00022617, ECO:0000256|PIRSR:PIRSR038928-2};
KW   Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW   ECO:0000256|RuleBase:RU000498};
KW   Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR038928-2};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR038928-2};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000256|RuleBase:RU000498};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|RuleBase:RU000498}.
FT   DOMAIN          7..391
FT                   /note="Catalase core"
FT                   /evidence="ECO:0000259|SMART:SM01060"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
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:PIRSR038928-2"
SQ   SEQUENCE   478 AA;  54754 MW;  81E1161A88A2976B CRC64;
     MSKKGLTTAA GAPVVDNNNV ITAGKRGPML LQDVWFLEKL AHFDREVIPE RRMHAKGSGA
     YGTFTVTHDI TRYTRAKIFA EIGKQTDMFI RFSTVAGERG AADAERDIRG FAMKFYTDEG
     NWDLVGNDTP VFYLRDPLKF PDLNHVVKRD PHTNLRNPVY KWDFFSHLPE SLHQLTIDFS
     DRGIPKSYRH MHGFGSHTFS FINANNERFW VKFHFRCEQG IENLMDDEAE AIIAKDRESS
     QRDLFDAIKR GDFPRWKLQI QIMPEHEASQ TPYNPFDLTK VWPHGDYPLI DVGFFELNRN
     PDNYFSEVEQ VAMNPANVVP GVSFSPDKML QGRLFSYGDA HRYRLGVNHH QIPVNGAKCP
     FHNYHRDGAM RVDGNSGNGA TYEPNSFGLF QEQPDFSEPP LSIEGAADHW NHREDKDYFS
     QPRALFNLLS AEEHQRMFTR IAGELSQVPE QIQRRQVDLF TQVHPDYGAG VASALGLK
//
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