ID A0A3N4PU23_9BACT Unreviewed; 716 AA.
AC A0A3N4PU23;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 ORFNames=EGT74_00925 {ECO:0000313|EMBL:RPE12152.1};
OS Chitinophaga lutea.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=2488634 {ECO:0000313|EMBL:RPE12152.1, ECO:0000313|Proteomes:UP000278351};
RN [1] {ECO:0000313|EMBL:RPE12152.1, ECO:0000313|Proteomes:UP000278351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZY74 {ECO:0000313|EMBL:RPE12152.1,
RC ECO:0000313|Proteomes:UP000278351};
RA Zong Y.;
RT "Chitinophaga lutea sp.nov., isolate from arsenic contaminated soil.";
RL Submitted (NOV-2018) 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}.
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:RPE12152.1}.
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DR EMBL; RPDH01000001; RPE12152.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4PU23; -.
DR OrthoDB; 9760293at2; -.
DR Proteomes; UP000278351; Unassembled WGS sequence.
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; cd08155; catalase_clade_2; 1.
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:UP000278351}.
FT DOMAIN 31..420
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT ACT_SITE 78
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 152
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 75
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 116
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 165
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 362
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 366
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 373
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ SEQUENCE 716 AA; 78904 MW; CD9A5AF279191642 CRC64;
MAKKTPGNEN PNPKTEQLAA HTEESTGEML TTNQGLLVND DQNSLKAGNR GPSLLEDFIL
REKITHFDHE RIPERIVHAR GSGAHGVFRV YDDSMARYTR AAFLTDPSVE TPVFVRFSTV
AGSRGSTDLA RDVRGFAVKF YTPEGNFDLV GNNIPVFFIQ DAVKFPDLIH AAKPEQDHEM
PQAATAHDTF WDFISLMPES AHMIMWAMSD RAIPRSYRMM EGFGVHTFRF VNGKGKGCFV
KFHWKPLLGV HSVAWDEAQK ISGKDPDFHR RDLWEAIEAG HYPEYEFGVQ IVAEEDEHKF
EFDLLDPTKI IPEELVPVRR IGKLTLNRNP DNFFAETEQV AMHPGHIVPG IDFSNDPLLQ
GRLFSYTDTQ LIRLGGPNFH EIPINRSIEP VHNHQRDGFM RQQINKGKAN YNPNSLGGGC
PFQAKMADGG FVSYPEKIDA KKVRERSRSF FDHFSQATLF YNSQSEPEKQ HIADALSFEL
GKVVTVAIRQ RMLGILTRID EGLAAKVAGA LGMPVPTGPD QPVNHSIPAD GNPKDFQPVK
VTASVTKSAA LSMANTVKNT IKSRKIAILA ADGVNGASLN AMKKALAAGG ALGVVIAPHL
GNIQPAKGEA IPVDQSFLTA ASVLFDAVYV PGGENSVAAL TINADAVHFL NEAYRHCKAI
AADADAEEVL NSTYFGKAPG PGVITGADNA ELAQRFTEAI AQHRFWEREQ ERRVPA
//
