ID A0A2A2DM44_9PSED Unreviewed; 513 AA.
AC A0A2A2DM44;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN ORFNames=BZL43_19545 {ECO:0000313|EMBL:PAU54758.1};
OS Pseudomonas sp. PICF141.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1949067 {ECO:0000313|EMBL:PAU54758.1, ECO:0000313|Proteomes:UP000217819};
RN [1] {ECO:0000313|EMBL:PAU54758.1, ECO:0000313|Proteomes:UP000217819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PICF141 {ECO:0000313|EMBL:PAU54758.1,
RC ECO:0000313|Proteomes:UP000217819};
RA Gomez-Lama C., Legarda-Cristobal G., Trivino J.C., Mercado-Blanco J.;
RT "Genome sequences of Pseudomonas strains PIC25, PIC105 and PICF141
RT indigenous of the olive (Olea europaea L.) cv. Picual rhizosphere and
RT effective biological control agents against Verticillium dahliae.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:PAU54758.1}.
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DR EMBL; MUNM01000069; PAU54758.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A2DM44; -.
DR OrthoDB; 9761719at2; -.
DR Proteomes; UP000217819; Unassembled WGS sequence.
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..30
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 31..513
FT /note="Catalase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012109845"
FT DOMAIN 34..414
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
FT REGION 397..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..433
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 81
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT ACT_SITE 153
FT /evidence="ECO:0000256|PIRSR:PIRSR038928-1"
FT BINDING 361
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 513 AA; 56410 MW; 602A37E4749C69F4 CRC64;
MTTPLGLGAF PLRRTLGVLT ASLLSFSVNA ATLTRDNGAA VGDNQNSQTA GATGPVLLQD
IQLIQKLQRF DRERIPERVV HARGTGAHGT FTVTDDLSDL TKAKVFAGGQ STPVFVRFSA
VVHGNHSPET LRDPRGFATK FYTADGNWDL VGNNFPTFFI RDAIKFPDMV HAFKPDPRTN
LDDDSRRFDF FSHVPEATRT LTELYSNSGT PASYREMDGN GVHAYKLVNA KGDVHYVKFH
WKSLQGLKNL DPKEVTSVQG QDYSHMTNDL VANINKGNFP KWDLYIQVLS PQDLSKFDFD
PLDATKIWPG VPERKVGQMV LNRNPANVFQ ETEQVAMAPA NLVPGIEPSE DRLLQGRVFS
YADTQLYRLG ANALQLPINA PKVAVNNGNQ DGAMNIGASS TGVNYQPSRL LSRDEPPTAR
YSQSALSGST QQTKIQREQN FKQAGDLYRS FNQKERQDLI GSFGGSLATT DDESKHIILS
FLYKADPEYG TGVAKVAKGD LARVKALAAK LVD
//
