ID A0A126P9L8_9BACT Unreviewed; 729 AA.
AC A0A126P9L8;
DT 11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT 11-MAY-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
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:AMJ65709.1};
GN ORFNames=AXW84_09920 {ECO:0000313|EMBL:AMJ65709.1};
OS Hymenobacter sp. PAMC 26628.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1484118 {ECO:0000313|EMBL:AMJ65709.1, ECO:0000313|Proteomes:UP000059956};
RN [1] {ECO:0000313|EMBL:AMJ65709.1, ECO:0000313|Proteomes:UP000059956}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC26628 {ECO:0000313|EMBL:AMJ65709.1,
RC ECO:0000313|Proteomes:UP000059956};
RA Wen L., He K., Yang H.;
RL Submitted (FEB-2016) 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 -!- 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; CP014304; AMJ65709.1; -; Genomic_DNA.
DR RefSeq; WP_068232160.1; NZ_CP014304.1.
DR AlphaFoldDB; A0A126P9L8; -.
DR STRING; 1484118.AXW84_09920; -.
DR KEGG; hyz:AXW84_09920; -.
DR OrthoDB; 9760293at2; -.
DR Proteomes; UP000059956; 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; 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; 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:UP000059956}.
FT DOMAIN 36..423
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 83
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 155
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 80
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 119
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 168
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 365
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 369
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 376
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ SEQUENCE 729 AA; 80469 MW; 230538C7BDF375DF CRC64;
MSDKPLAKQT HEDVVGNPKT DELAKNREDG YGEFLTTNQG LRINDDQNSL KAGERGPTLL
EDFILREKIT HFDHERIPER VVHARGVAAH GYFQAYDDNA NLSRAAFLQP GAVTPVFTRF
STVAGSRGSS DMARDVRGFA VKFYTEEGIF DLVGNNIPVF FIQDATKFPD FIHAVKPEPH
NEIPQAASAH DTFYDFISTN PETSHMLLWV MSDRGLPRSL RMMEGFGIHA FRLVNAEGKA
RFVKFHWKPT LGTHSVAWEE AQQISGKDPD FHRRDLWNSI EGGAYPEWEL GVQVVEEEDE
RKFDFDILDS TKLIPEELVP VIKLGKMVLN RNVDNYFAET EQVAFCLSHI VPGIDFSNDP
LLQGRLFSYL DTQLKRLGGP NFHEIPINRS LAPIHNGQRD GHMRQTINKG NVAYGVNLLN
DNYPRQAKQS QGGFTSTYER VEGHKIRLRS KSFVDHYSQA KLFWNSQTAA EKMHIVKALR
FELSHVQKVE VQARTLVQLA QIDHDLVSRV AEGLGMAVPS AEGVQLNLAV PADGDAAYYQ
SAPAKQDDAN SAALSISVNS PINAGKTSIK TRHIAILATD GADVGAIGEL MTTLMAEGAQ
TAIVATHLGK LKGTDGQEVL INWTFQATSS VLFDAVYVAG GASSVQKLTQ DADAVRFVNE
AFRHCKPIAA SAEGVDLLKA ASYPGATDIL GADGVITSAD NKVAGLAQEF IKAIGYHRFW
SRELKSMPA
//
