ID A0A3P4B2D4_9BURK Unreviewed; 797 AA.
AC A0A3P4B2D4;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
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:VCU70443.1};
GN ORFNames=PIGHUM_02515 {ECO:0000313|EMBL:VCU70443.1};
OS Pigmentiphaga humi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pigmentiphaga.
OX NCBI_TaxID=2478468 {ECO:0000313|EMBL:VCU70443.1, ECO:0000313|Proteomes:UP000277294};
RN [1] {ECO:0000313|EMBL:VCU70443.1, ECO:0000313|Proteomes:UP000277294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DnA1 {ECO:0000313|EMBL:VCU70443.1};
RA Criscuolo A.;
RL Submitted (OCT-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 -!- 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.
CC {ECO:0000256|PIRNR:PIRNR038927}.
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DR EMBL; UWPJ01000018; VCU70443.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P4B2D4; -.
DR OrthoDB; 9761719at2; -.
DR Proteomes; UP000277294; 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; 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; 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; 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:UP000277294}.
FT DOMAIN 126..514
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 173
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT ACT_SITE 246
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-1"
FT BINDING 170
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 210
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 259
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 456
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
FT BINDING 460
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 467
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000256|PIRSR:PIRSR038927-3"
SQ SEQUENCE 797 AA; 85590 MW; AD9FBE879448DB77 CRC64;
MPTRKRPPTD PAPQPAVDTA YLNTDSGPAT PPSEAAAHPA VKQARAVGKM VEGMPANPNK
PAEYGLAAAR PPAGATAEPA EESALASTLS EKNRSGKTGA RAASGVNAAG GELPRVRADG
SGQAITTNQG VPVSDNQSSL KAGLRGPALL KDFILREKIT HFDHERIPER IVHARGSAAH
GYFECYEALA DLTCASLFAE AGKRTPVFVR FSTVAGERGS KDTARDVRGF AVKFYTDQGN
WDLVGNNMPV FFIQDAMKFP DLVHAVKPEP HHGMPQAASA HDTFWDFISL MPESTHMIMW
LMSDRAIPRS YRMMQGFGVH TFRFVNAEGQ AKLVKFHWNP KLGTHSHVWD EAVKISGADP
DYHRRDLWEA IEAGEYPEWE LGVQVFDEAQ AEQFSFDILD STKIVPEELV PIRPIGRMVL
NRNPDNFFAE TEQVAFCTAH IVPGLDFTND PLLAGRIHSY VDTQISRLGG PNFHELPINA
PLAPVHNNQR DGMHRQAIHR GRVAYEPNSL AGGCPFQAGS AGFVSFPEPV AADELRGKAE
KFAEHYNQAT LFYESQSGHE QQHIIDAFSF ELSKVTVPGI RQRIVATLRN VSETLAQAVA
ANLGMPGLPD PLARADGSAP EPEVGHSAAL SLLARPGDGG IRTRKIAVLV ADGVDGQAAM
QTAQALIGKG AVVRLVGQHV GLLEAAAGQS LDADASFQNS PSVLFDAAVV PDGAAAIEAL
CADGFALEFI RDLFRHGKSL LAIGAGRQLL EQAGVPLADP DPGLVLADSA GKPALASFIQ
AVARHRHPER ETDPPKV
//
