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 27-MAR-2024, entry version 132. 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; Pseudomonadota; 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 / RC 1C / 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 208964.PA4613; -. DR PaxDb; 208964-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 OrthoDB; 9761719at2; -. DR PhylomeDB; Q59635; -. DR BioCyc; PAER208964:G1FZ6-4707-MONOMER; -. 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 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; 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 //