CATA_PSEAE
ID CATA_PSEAE Reviewed; 482 AA.
AC O52762;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
GN Name=katA; OrderedLocusNames=PA4236;
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=FRD1;
RX PubMed=10368148; DOI=10.1128/jb.181.12.3730-3742.1999;
RA Ma J.-F., Ochsner U.A., Klotz M.G., Nanayakkara V.K., Howell M.L.,
RA Johnson Z., Posey J.E., Vasil M.L., Monaco J.J., Hassett D.J.;
RT "Bacterioferritin A modulates catalase A (KatA) activity and resistance to
RT hydrogen peroxide in Pseudomonas aeruginosa.";
RL J. Bacteriol. 181:3730-3742(1999).
RN [2]
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).
RN [3]
RP PROTEIN SEQUENCE OF 7-27 AND 218-238.
RC STRAIN=ATCC 33467 / type 1 smooth, and ATCC 33468 / type 2 mucoid;
RA Liddor M.;
RT "Biofouling in water treatment systems: effect of membrane properties on
RT biofilm formation.";
RL Thesis (2005), Ben-Gurion University, Israel.
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 -!- ACTIVITY REGULATION: By peroxide and bfr-bound iron.
CC -!- SUBUNIT: Heteromultimer. Possibly an alpha(2)beta-heterotrimer where
CC the alpha subunit is a 56 kDa protein and the beta subunit a 45 kDa
CC protein.
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR EMBL; AF047025; AAC03118.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07624.1; -; Genomic_DNA.
DR PIR; B83113; B83113.
DR RefSeq; NP_252926.1; NC_002516.2.
DR RefSeq; WP_003103909.1; NZ_QZGE01000028.1.
DR PDB; 4E37; X-ray; 2.53 A; A/B/C/D=3-482.
DR PDBsum; 4E37; -.
DR AlphaFoldDB; O52762; -.
DR SMR; O52762; -.
DR STRING; 287.DR97_3675; -.
DR PaxDb; O52762; -.
DR PRIDE; O52762; -.
DR EnsemblBacteria; AAG07624; AAG07624; PA4236.
DR GeneID; 881831; -.
DR KEGG; pae:PA4236; -.
DR PATRIC; fig|208964.12.peg.4437; -.
DR PseudoCAP; PA4236; -.
DR HOGENOM; CLU_010645_2_0_6; -.
DR InParanoid; O52762; -.
DR OMA; WTCYVQV; -.
DR PhylomeDB; O52762; -.
DR BioCyc; PAER208964:G1FZ6-4309-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004096; F:catalase activity; IDA:PseudoCAP.
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; cd08156; catalase_clade_3; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR040333; Catalase_3.
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 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Heme; Hydrogen peroxide; Iron;
KW Metal-binding; Oxidoreductase; Peroxidase; Reference proteome.
FT CHAIN 1..482
FT /note="Catalase"
FT /id="PRO_0000084994"
FT ACT_SITE 55
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 128
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT BINDING 338
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"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:4E37"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:4E37"
FT STRAND 57..67
FT /evidence="ECO:0007829|PDB:4E37"
FT TURN 72..74
FT /evidence="ECO:0007829|PDB:4E37"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:4E37"
FT STRAND 86..94
FT /evidence="ECO:0007829|PDB:4E37"
FT STRAND 111..118
FT /evidence="ECO:0007829|PDB:4E37"
FT STRAND 121..131
FT /evidence="ECO:0007829|PDB:4E37"
FT HELIX 138..140
FT /evidence="ECO:0007829|PDB:4E37"
FT HELIX 141..148
FT /evidence="ECO:0007829|PDB:4E37"
FT TURN 152..154
FT /evidence="ECO:0007829|PDB:4E37"
FT HELIX 159..166
FT /evidence="ECO:0007829|PDB:4E37"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:4E37"
FT HELIX 173..179
FT /evidence="ECO:0007829|PDB:4E37"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:4E37"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:4E37"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:4E37"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:4E37"
FT STRAND 209..218
FT /evidence="ECO:0007829|PDB:4E37"
FT HELIX 227..236
FT /evidence="ECO:0007829|PDB:4E37"
FT HELIX 240..251
FT /evidence="ECO:0007829|PDB:4E37"
FT STRAND 256..265
FT /evidence="ECO:0007829|PDB:4E37"
FT HELIX 266..271
FT /evidence="ECO:0007829|PDB:4E37"
FT TURN 285..287
FT /evidence="ECO:0007829|PDB:4E37"
FT STRAND 291..300
FT /evidence="ECO:0007829|PDB:4E37"
FT HELIX 305..308
FT /evidence="ECO:0007829|PDB:4E37"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:4E37"
FT HELIX 329..345
FT /evidence="ECO:0007829|PDB:4E37"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:4E37"
FT HELIX 354..356
FT /evidence="ECO:0007829|PDB:4E37"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:4E37"
FT HELIX 396..398
FT /evidence="ECO:0007829|PDB:4E37"
FT STRAND 409..411
FT /evidence="ECO:0007829|PDB:4E37"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:4E37"
FT HELIX 422..430
FT /evidence="ECO:0007829|PDB:4E37"
FT HELIX 433..447
FT /evidence="ECO:0007829|PDB:4E37"
FT HELIX 452..465
FT /evidence="ECO:0007829|PDB:4E37"
FT HELIX 467..477
FT /evidence="ECO:0007829|PDB:4E37"
SQ SEQUENCE 482 AA; 55589 MW; 84E5ABA647CAB414 CRC64;
MEEKTRLTTA AGAPVVDNQN VQTAGPRGPM LLQDVWFLEK LAHFDREVIP ERRMHAKGSA
AYGTFTVTHD ITPYTRAKIF SQVGKKTDMF LRFSTVAGER GAADAERDIR GFSMRFYTEQ
GNWDLVGNNT PVFYLRDPLK FPDLNHVVKR DPRTNLRNAT FKWDFFSHLP ESLHQLTIDF
SDRGLPKSYR HIHGFGSHTF SFINANNERF WVKFHFKTQQ GIENLTNAEA AEVIAQDRES
SQRDLYESIE KGDFPRWKMY VQIMPEKEAA TYRYNPFDLT KVWPHGDYPL IEVGFFELNR
NPDNYFAEVE QAAFTPANVV PGIGFSPDKM LQGRLFSYGD AHRYRLGVNH HQIPVNAARC
PHQVYHRDGG MRVDGNNAHQ RVTYEPNSFN QWQEQPDFSE PPLSLEGAAD HWNHRVDDDY
YSQPAALFHL FTDEQKQRLF ANIAEDIRDV PEQIQRRQIG LFLKVDPAYG KGVADALGLK
LD
