ID Q4K5Q7_PSEF5 Unreviewed; 513 AA.
AC Q4K5Q7;
DT 02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 2.
DT 24-JAN-2024, entry version 108.
DE RecName: Full=Catalase {ECO:0000256|ARBA:ARBA00014132, ECO:0000256|RuleBase:RU000498};
DE EC=1.11.1.6 {ECO:0000256|RuleBase:RU000498};
GN Name=katB {ECO:0000313|EMBL:AAY94568.2};
GN OrderedLocusNames=PFL_5358 {ECO:0000313|EMBL:AAY94568.2};
OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=220664 {ECO:0000313|EMBL:AAY94568.2, ECO:0000313|Proteomes:UP000008540};
RN [1] {ECO:0000313|EMBL:AAY94568.2, ECO:0000313|Proteomes:UP000008540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5
RC {ECO:0000313|Proteomes:UP000008540};
RX PubMed=15980861; DOI=10.1038/nbt1110;
RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.,
RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S.III.,
RA Thomashow L.S., Loper J.E.;
RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT Pf-5.";
RL Nat. Biotechnol. 23:873-878(2005).
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}.
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DR EMBL; CP000076; AAY94568.2; -; Genomic_DNA.
DR RefSeq; WP_011063582.1; NC_004129.6.
DR AlphaFoldDB; Q4K5Q7; -.
DR STRING; 220664.PFL_5358; -.
DR PeroxiBase; 4079; PfKat02_Pf5.
DR KEGG; pfl:PFL_5358; -.
DR PATRIC; fig|220664.5.peg.5471; -.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_010645_2_0_6; -.
DR OMA; HVWPQKQ; -.
DR Proteomes; UP000008540; Chromosome.
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_5005695459"
FT DOMAIN 34..414
FT /note="Catalase core"
FT /evidence="ECO:0000259|SMART:SM01060"
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; 56860 MW; A8C859AA3AC5922D CRC64;
MTASLGLGSL SQRRVLGVLA ASMLSLSVQA ATLTRDNGAA VGDNQNSQTA GATGPVLLQD
VQLIQKLQRF DRERIPERVV HARGTGAHGT FTVTDNLTDL TRAKVFAAGE VTPVFVRFSA
VVHGNHSPET LRDPRGFATK FYTEDGNWDL VGNNFPTFFI RDAIKFPDMV HAFKPDPRTN
LDDDSRRFDF FSHVPEATRT LTELYSNSGT PASYREMDGN GVHAYKLINA KGEVHYVKFH
WKSLQGLKNL DPKQVVEVQG RDYSHMTNDL VTHINKGDFP KWDLYVQVLK PEDLAKFDFD
PLDATKIWPG VPERKVGQMV LNRNPANVFQ ETEQVAMAPA NLVPGIEPSE DRLLQGRVFS
YADTQMYRIG ANALQLPINA PKNPVNNGNQ DGAMNLGHSS TGVNYQPSRL MPREEPQTAR
YSQMALAGST QQAKIQREQN FKQAGDLYRS FSKKERQDLI DSFGGSLATT DDESKHIMLS
FLYKADPEYG TGVTKVAKGD LARVKALAAK LSD
//