CATE_PSEAE
ID CATE_PSEAE Reviewed; 709 AA.
AC Q9I1W8;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Catalase HPII;
DE EC=1.11.1.6;
GN Name=katE; OrderedLocusNames=PA2147;
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 [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 {ECO:0000250}.
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; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the catalase family. HPII subfamily.
CC {ECO:0000305}.
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DR EMBL; AE004091; AAG05535.1; -; Genomic_DNA.
DR PIR; B83376; B83376.
DR RefSeq; NP_250837.1; NC_002516.2.
DR RefSeq; WP_003113643.1; NZ_QZGE01000014.1.
DR AlphaFoldDB; Q9I1W8; -.
DR SMR; Q9I1W8; -.
DR STRING; 287.DR97_6280; -.
DR PeroxiBase; 4089; PaerKat03_PAO1.
DR PaxDb; Q9I1W8; -.
DR PRIDE; Q9I1W8; -.
DR EnsemblBacteria; AAG05535; AAG05535; PA2147.
DR GeneID; 881554; -.
DR KEGG; pae:PA2147; -.
DR PATRIC; fig|208964.12.peg.2245; -.
DR PseudoCAP; PA2147; -.
DR HOGENOM; CLU_010645_3_0_6; -.
DR InParanoid; Q9I1W8; -.
DR OMA; VMWQMSD; -.
DR PhylomeDB; Q9I1W8; -.
DR BioCyc; PAER208964:G1FZ6-2187-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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:0006979; P:response to oxidative stress; IBA:GO_Central.
DR CDD; cd03132; GATase1_catalase; 1.
DR Gene3D; 1.20.1370.20; -; 1.
DR Gene3D; 3.40.50.880; -; 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; IPR002226; Catalase_haem_BS.
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; PTHR42821; 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; SSF52317; 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 Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW Peroxidase; Reference proteome.
FT CHAIN 1..709
FT /note="Catalase HPII"
FT /id="PRO_0000287752"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 419..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 90
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 163
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT BINDING 377
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 709 AA; 77963 MW; EF3977DA832D6E1E CRC64;
MSEQNNEQRS QAAGTDTVDR GNSNAKLEQL EAYREDATGE ALSTNTGTRI ADNQNTLKAG
ERGPSLLEDF IMREKITHFD HERIPERVVH ARGSAAHGYF EAYEDLSDLT KAGFLAEAGK
RTPVFVRFST VQGPRGSADT VRDVRGFAVK FYTDEGNFDL VGNNMPVFFI QDAIKFPDFV
HAVKPEPHNE IPTGASAHDT FWDFVSLTPE SAHMVMWLMS DRAIPIAYRN MQGFGVHTFR
LVNAAGESVL VKFHWRPKSG TCSLVWDEAQ KLAGKDPDFN RRTLWEDIEK GDYPEWELGL
QVIPENQQDS FDFDLLDPTK LVPEELVPVR VVGRMVLNRN PDNFFAETEQ VAFHVGHVVP
GIDFTNDPLL QGRLFSYTDT QLLRLSGPNF NEIPINRPLC PFHNNQRDAP HRQTINRGRA
SYEPNSIDGG WPKETPPAAR NGGFSTYHEP VSGSKLRKRA DSFADHFSQA ALFWHSMSEA
EQAHIVAAYS FELSKVERQS IREREVNQIL LNIDPQLAAR VAANVGVQLA APANPTPQPK
PSPALSQMNL LSGDIRSRKV AILIADGVAE SDVSDLRDAL RQEGADAKLI APSASPVQAE
NGAELSPEGT WDGLPSVAFD AVFVPGGAAS SQAIGADGRG LHYLLEAYKH LKPVAFAGDA
QALASQLSLP GDPGVVLGAT ATDVFPGLRQ ALMQHRIWQR EAATKAIPA
