CATB_PSEAE
ID CATB_PSEAE Reviewed; 513 AA.
AC Q59635;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
DE AltName: Full=Paraquat-inducible catalase isozyme B;
DE Flags: Precursor;
GN Name=katB; OrderedLocusNames=PA4613;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FRD2;
RX PubMed=7592431; DOI=10.1128/jb.177.22.6536-6544.1995;
RA Brown S.M., Howell M.L., Vasil M.L., Anderson A.J., Hassett D.J.;
RT "Cloning and characterization of the katB gene of Pseudomonas aeruginosa
RT encoding a hydrogen peroxide-inducible catalase: purification of KatB,
RT cellular localization, and demonstration that it is essential for optimal
RT resistance to hydrogen peroxide.";
RL J. Bacteriol. 177:6536-6544(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=FRD1;
RA Howell M.L., Heur M., Klotz M.G., Hassett D.J.;
RT "Pseudomonas aeruginosa oxidative stress operon.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
CC -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC protect cells from the toxic effects of hydrogen peroxide.
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:0000255|PROSITE-ProRule:PRU10013};
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; U34896; AAA79046.1; -; Genomic_DNA.
DR EMBL; U89384; AAB49463.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG08001.1; -; Genomic_DNA.
DR PIR; E83069; E83069.
DR RefSeq; NP_253303.1; NC_002516.2.
DR RefSeq; WP_003094881.1; NZ_QZGE01000004.1.
DR AlphaFoldDB; Q59635; -.
DR SMR; Q59635; -.
DR STRING; 287.DR97_1919; -.
DR PaxDb; Q59635; -.
DR PRIDE; Q59635; -.
DR EnsemblBacteria; AAG08001; AAG08001; PA4613.
DR GeneID; 881120; -.
DR KEGG; pae:PA4613; -.
DR PATRIC; fig|208964.12.peg.4828; -.
DR PseudoCAP; PA4613; -.
DR HOGENOM; CLU_010645_2_0_6; -.
DR InParanoid; Q59635; -.
DR OMA; HVWPQKQ; -.
DR PhylomeDB; Q59635; -.
DR BioCyc; PAER208964:G1FZ6-4707-MON; -.
DR SABIO-RK; Q59635; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004096; F:catalase activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
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; PTHR11465; 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; SSF56634; 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; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Periplasm;
KW Peroxidase; Reference proteome; Signal.
FT SIGNAL 1..30
FT /evidence="ECO:0000255"
FT CHAIN 31..513
FT /note="Catalase"
FT /id="PRO_0000004693"
FT REGION 391..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 391..407
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 81
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 153
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
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:0000250"
SQ SEQUENCE 513 AA; 57131 MW; C9A09B88629A11CB CRC64;
MNPSLNAFRP GRLLVAASLT ASLLSLSVQA ATLTRDNGAP VGDNQNSQTA GPNGSVLLQD
VQLLQKLQRF DRERIPERVV HARGTGAHGE FVASADISDL SMAKVFRKGE KTPVFVRFSA
VVHGNHSPET LRDPRGFATK FYTADGNWDL VGNNFPTFFI RDAIKFPDMV HAFKPDPRSN
LDDDSRRFDF FSHVPEATRT LTLLYSNEGT PASYREMDGN SVHAYKLVNA RGEVHYVKFH
WKSLQGQKNL DPKQVAEVQG RDYSHMTNDL VSAIRKGDFP KWDLYIQVLK PEDLAKFDFD
PLDATKIWPG IPERKIGQMV LNRNVDNFFQ ETEQVAMAPS NLVPGIEPSE DRLLQGRLFA
YADTQMYRVG ANGLGLPVNR PRSEVNTVNQ DGALNAGHST SGVNYQPSRL DPREEQASAR
YVRTPLSGTT QQAKIQREQN FKQTGELFRS YGKKDQADLI ASLGGALAIT DDESKYIMLS
YFYKADSDYG TGLAKVAGAD LQRVRQLAAK LQD
