ID A0A2S1LCY0_9FLAO Unreviewed; 712 AA.
AC A0A2S1LCY0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
DE EC=1.11.1.6 {ECO:0000256|ARBA:ARBA00012314, ECO:0000256|PIRNR:PIRNR038927};
GN Name=katE {ECO:0000313|EMBL:AWG21612.1};
GN ORFNames=FFWV33_08730 {ECO:0000313|EMBL:AWG21612.1};
OS Flavobacterium faecale.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Flavobacterium.
OX NCBI_TaxID=1355330 {ECO:0000313|EMBL:AWG21612.1, ECO:0000313|Proteomes:UP000244527};
RN [1] {ECO:0000313|EMBL:AWG21612.1, ECO:0000313|Proteomes:UP000244527}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WV33 {ECO:0000313|EMBL:AWG21612.1,
RC ECO:0000313|Proteomes:UP000244527};
RA Lee P.C.;
RT "Compelte genome sequence of WV33.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Serves to protect cells from the toxic effects of hydrogen
CC peroxide. {ECO:0000256|PIRNR:PIRNR038927}.
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|PIRNR:PIRNR038927,
CC ECO:0000256|RuleBase:RU000498};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC Evidence={ECO:0000256|ARBA:ARBA00001971,
CC ECO:0000256|PIRNR:PIRNR038927, ECO:0000256|PIRSR:PIRSR038927-2};
CC -!- SIMILARITY: Belongs to the catalase family. HPII subfamily.
CC {ECO:0000256|ARBA:ARBA00010660}.
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DR EMBL; CP020918; AWG21612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S1LCY0; -.
DR KEGG; ffa:FFWV33_08730; -.
DR OrthoDB; 9760293at2; -.
DR Proteomes; UP000244527; Chromosome.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0020037; F:heme binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro.
DR CDD; cd03132; GATase1_catalase; 1.
DR Gene3D; 1.20.1370.20; -; 1.
DR Gene3D; 3.40.50.880; -; 1.
DR Gene3D; 2.40.180.10; Catalase core domain; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR024708; Catalase_AS.
DR InterPro; IPR024712; Catalase_clade2.
DR InterPro; IPR043156; Catalase_clade2_helical.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
DR InterPro; IPR041399; Catalase_large_C.
DR InterPro; IPR020835; Catalase_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR PANTHER; PTHR42821; CATALASE; 1.
DR PANTHER; PTHR42821:SF1; CATALASE-B; 1.
DR Pfam; PF00199; Catalase; 1.
DR Pfam; PF06628; Catalase-rel; 1.
DR Pfam; PF18011; Catalase_C; 1.
DR PIRSF; PIRSF038927; Catalase_clade2; 1.
DR PRINTS; PR00067; CATALASE.
DR SMART; SM01060; Catalase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 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|PIRNR:PIRNR038927};
KW Hydrogen peroxide {ECO:0000256|ARBA:ARBA00023324,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRNR:PIRNR038927};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|PIRNR:PIRNR038927};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559, ECO:0000256|PIRNR:PIRNR038927};
KW Reference proteome {ECO:0000313|Proteomes:UP000244527}.
FT DOMAIN 30..418
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..43
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 77
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 150
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 74
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 114
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 163
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 360
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 364
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:PIRSR038927-2"
FT BINDING 371
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ SEQUENCE 712 AA; 80065 MW; 96855B9581735D94 CRC64;
MATNKKENLG SAKTEALKAS EKDSTGKVMT TNQGLKVNDT NNSLKSGERG STLLEDFLLR
EKITSFDHER IPERIVHARG SAAHGVFELY ESIEQYSKAG IFTDVKRTTP VFVRFSTVAG
SKGSPDLARD VRGFAVKFYT QEGTWDLVGN NMPIFFIQDA IKFPDLIHSV KPEPNKEIPQ
AASAHDTFYD FVSHTTETLH NHIWVMSDRA IPRSFRMMEG FGIHTFRLIN DKNESHFVRF
HWKPKLGVHS LTWDEAVKIN GADADFHRRD LWDAIDAGQF PEWELGVQII PQEDEFKFEF
DLLDPTKLIP EEMVPVKIIG KMTLNKNPEN FFAETEQVAF LPGHIVPGID FTNDPLLQGR
LFSYRDTQLS RLGGPNFNQI PINRPVVESH NNQRDGMMQT EINKGQTAYF PNSLSGGCPH
LAKMAEGGFH SYEERIDAKK IRTRSASFND HFSQPALFYR SLAKWEQQHV ADAYTFELGK
CNHDHIKERM LWLIAEIDED LAKKVAKGLG LEIPSDIERP INQAIGADAN IEEQQPPKKK
NYLDSAPTLS QANTKFDSIV SRKIAVLVAN GFSMKNYKAM ADALEKEGAV LNLVAPHGGM
VTCDAGMKHK VDAAIMTTES VLFDAVYIPG GKESVNELMG EAKFLKFINE ALKHCKAIAV
DGKDNALIDK TYLAKFKDDA AVLIDEKPDA FINAIKQHRN WDRSEKVKEI PA
//
