ID E4TAY4_RIEAD Unreviewed; 509 AA.
AC E4TAY4;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Catalase {ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN ORFNames=RA0C_0243 {ECO:0000313|EMBL:AFD55251.1};
OS Riemerella anatipestifer (strain ATCC 11845 / DSM 15868 / JCM 9532 / NCTC
OS 11014).
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Riemerella.
OX NCBI_TaxID=693978 {ECO:0000313|EMBL:AFD55251.1, ECO:0000313|Proteomes:UP000010093};
RN [1] {ECO:0000313|EMBL:AFD55251.1, ECO:0000313|Proteomes:UP000010093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15868 {ECO:0000313|Proteomes:UP000010093};
RX PubMed=22628503; DOI=10.1128/JB.00366-12;
RA Wang X., Zhu D., Wang M., Cheng A., Jia R., Zhou Y., Chen Z., Luo Q.,
RA Liu F., Wang Y., Chen X.Y.;
RT "Complete genome sequence of Riemerella anatipestifer reference strain.";
RL J. Bacteriol. 194:3270-3271(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; CP003388; AFD55251.1; -; Genomic_DNA.
DR RefSeq; WP_004919270.1; NC_017045.1.
DR AlphaFoldDB; E4TAY4; -.
DR GeneID; 66847726; -.
DR KEGG; rai:RA0C_0243; -.
DR KEGG; ran:Riean_0041; -.
DR PATRIC; fig|693978.17.peg.251; -.
DR HOGENOM; CLU_010645_2_0_10; -.
DR Proteomes; UP000010093; 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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..509
FT /note="Catalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003186999"
FT DOMAIN 24..407
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 377..414
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 377..404
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 71
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 144
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 354
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 509 AA; 58166 MW; AB9114AA704FECF4 CRC64;
MKKTFIGLGL LLSVSAYMGQ QTLTTNFGAP VGDNQNSLTV GNNGAVLLQD IHLVEKLAAF
DRERIPERVV HPRGAGAYGE FECKVDMSPY TKARLFSEVG VKTPVFVRFS TVIHGTGSPE
TLRDPRGFAT KFYTKEGNYD IVGNNLPVFF IRDAIKFPDM VHSLKPSPIT NRQDPNRYLD
FFSHIPESTH MLMRLYSDYG IPANYREMDG SSVHAFKWIN NNGEVVYVKY TWKSKQGERN
LSMEEASKIQ GMDFQHATTD LYDNIKKGNY PQWDLYVQIL KPSDFDKLDY FPLDATKIWN
ETDAKPMLIG TMTLNKIPDN YFEHVEQSAF SPGTLIPGIE PSEDKLLQGR LFSYFDTQRH
RVGANFQKLA VNRPIVSVNS NNQDGPMSER GTKSDTNYQP SRINNKPDDA KYKQSKREYS
NVFITQDKID KPNDFKQAGD FYRSLDKKNQ ENLLKNLLAD LKQVTNKDIQ KIITGHFYMA
DNSLGKKIAS ELKLTREDVE SIFHKKYKK
//
