ID G8X4G5_FLACA Unreviewed; 497 AA.
AC G8X4G5;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN OrderedLocusNames=FCOL_02725 {ECO:0000313|EMBL:AEW85390.1};
OS Flavobacterium columnare (strain ATCC 49512 / CIP 103533 / TG 44/87).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1041826 {ECO:0000313|EMBL:AEW85390.1, ECO:0000313|Proteomes:UP000005638};
RN [1] {ECO:0000313|Proteomes:UP000005638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49512 / CIP 103533 / TG 44/87
RC {ECO:0000313|Proteomes:UP000005638};
RA Tekedar H.C., Karsi A., Gillaspy A.F., Dyer D., Benton N.R., Zaitshik J.,
RA Vamenta S., Banes M.M., Gulsoy N., Aboko-Cole M., Waldbieser G.C.,
RA Lawrence M.L.;
RT "Complete genome sequence of Flavobacterium columnare ATCC 49512.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEW85390.1, ECO:0000313|Proteomes:UP000005638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49512 / CIP 103533 / TG 44/87
RC {ECO:0000313|Proteomes:UP000005638};
RX PubMed=22535941; DOI=10.1128/JB.00281-12;
RA Tekedar H.C., Karsi A., Gillaspy A.F., Dyer D.W., Benton N.R., Zaitshik J.,
RA Vamenta S., Banes M.M., Gulsoy N., Aboko-Cole M., Waldbieser G.C.,
RA Lawrence M.L.;
RT "Genome Sequence of the Fish Pathogen Flavobacterium columnare ATCC
RT 49512.";
RL J. Bacteriol. 194:2763-2764(2012).
CC -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC protect cells from the toxic effects of hydrogen peroxide.
CC {ECO:0000256|ARBA:ARBA00002974}.
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|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; CP003222; AEW85390.1; -; Genomic_DNA.
DR RefSeq; WP_014164673.1; NC_016510.2.
DR AlphaFoldDB; G8X4G5; -.
DR STRING; 1041826.FCOL_02725; -.
DR GeneID; 60759599; -.
DR KEGG; fco:FCOL_02725; -.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_010645_2_0_10; -.
DR Proteomes; UP000005638; 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; cd08154; catalase_clade_1; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
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:SF23; CATALASE-2; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000005638};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..497
FT /note="Catalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003518597"
FT DOMAIN 24..405
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 71
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 144
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 352
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 497 AA; 56699 MW; EC8CC3850C06FF97 CRC64;
MRKSFVTCAS LIISISAFAQ NPLTTSGGAP VNGDLQSLTL GPNGPVLLED VHLIEKLQHF
SRERIPERVM HPRGTGAQGY FILTKNISDL TKAKIFTEVD KKTPVLVRFS SVIHSKGSPE
TARDPRGFAV KFYTEEGNWD LVGNHIPTFF IRDAIKFPDF THANKPSPIT DLQDENRIFD
YFSKTPEATQ TLTWLMSDNG TPKSYREMDG FGVNTFKFIN DKGDISWVKF HFKSLQGIKN
LTAEEVVQVQ GKDFSHMTRD LYNNIAAGNF PKWDLYVQII PNKDINKYDF NIFDDTKQWF
NVEEIKVGTL VLDRIPANFF QYTESAAFAP SRVVPGIGFS PDKMLQGRNF SYADAQMYRL
GKNHQLLPAN RPLVKVNNYH IDGAMNFEER TGDTNYFPSH NNPTYTEFKA DDKRLLDGYM
VREEIKDSKD FYQAGILYRS YSKQEKDNLI KNWTSNLSKV KDKKVQATMV SFLYKADQEY
GTRVGNALGL SKDSYNK
//
