CATA_PROMI
ID CATA_PROMI Reviewed; 484 AA.
AC P42321;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
GN Name=katA;
OS Proteus mirabilis.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=584;
RN [1]
RP PROTEIN SEQUENCE, NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-305, OXIDATION AT
RP MET-53, AND MASS SPECTROMETRY.
RC STRAIN=PR;
RX PubMed=7786407; DOI=10.1007/bf01888363;
RA Buzy A., Bracchi V., Sterjiades R., Chroboczek J., Thibault P., Gagnon J.,
RA Jouve H.-M., Hudry-Clergeon G.;
RT "Complete amino acid sequence of Proteus mirabilis PR catalase. Occurrence
RT of a methionine sulfone in the close proximity of the active site.";
RL J. Protein Chem. 14:59-72(1995).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RC STRAIN=PR;
RX PubMed=7791219; DOI=10.1006/jmbi.1995.0350;
RA Gouet P., Jouve H.-M., Dideberg O.;
RT "Crystal structure of Proteus mirabilis PR catalase with and without bound
RT NADPH.";
RL J. Mol. Biol. 249:933-954(1995).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS), AND ABSORPTION SPECTROSCOPY.
RX PubMed=8901874; DOI=10.1038/nsb1196-951;
RA Gouet P., Jouve H.-M., Williams P.A., Andersson I., Andreoletti P.,
RA Nussaume L., Hajdu J.;
RT "Ferryl intermediates of catalase captured by time-resolved Weissenberg
RT crystallography and UV-VIS spectroscopy.";
RL Nat. Struct. Biol. 3:951-956(1996).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND EPR SPECTROSCOPY.
RX PubMed=12486720; DOI=10.1002/prot.10283;
RA Andreoletti P., Sainz G., Jaquinod M., Gagnon J., Jouve H.-M.;
RT "High-resolution structure and biochemical properties of a recombinant
RT Proteus mirabilis catalase depleted in iron.";
RL Proteins 50:261-271(2003).
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 -!- COFACTOR:
CC Name=NADP(+); Xref=ChEBI:CHEBI:58349;
CC -!- SUBUNIT: Homotetramer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- MASS SPECTROMETRY: Mass=55643; Mass_error=5; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:7786407};
CC -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR PIR; A58663; A58663.
DR RefSeq; WP_004248382.1; NZ_WURR01000010.1.
DR PDB; 1E93; X-ray; 2.00 A; A=1-484.
DR PDB; 1H6N; X-ray; 2.11 A; A=1-484.
DR PDB; 1H7K; X-ray; 2.40 A; A=2-484.
DR PDB; 1M85; X-ray; 2.00 A; A=1-484.
DR PDB; 1MQF; X-ray; 2.50 A; A=1-484.
DR PDB; 1NM0; X-ray; 2.30 A; A=1-484.
DR PDB; 2CAG; X-ray; 2.70 A; A=1-484.
DR PDB; 2CAH; X-ray; 2.70 A; A=1-484.
DR PDB; 3HB6; X-ray; 2.30 A; A=1-484.
DR PDBsum; 1E93; -.
DR PDBsum; 1H6N; -.
DR PDBsum; 1H7K; -.
DR PDBsum; 1M85; -.
DR PDBsum; 1MQF; -.
DR PDBsum; 1NM0; -.
DR PDBsum; 2CAG; -.
DR PDBsum; 2CAH; -.
DR PDBsum; 3HB6; -.
DR AlphaFoldDB; P42321; -.
DR SMR; P42321; -.
DR STRING; 584.AOUC001_06445; -.
DR DrugBank; DB01942; Formic acid.
DR DrugBank; DB03790; L-methionine sulfone.
DR GeneID; 6802690; -.
DR OMA; WTCYVQV; -.
DR OrthoDB; 1584770at2; -.
DR BRENDA; 1.11.1.6; 5044.
DR SABIO-RK; P42321; -.
DR EvolutionaryTrace; P42321; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 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; Cytoplasm; Direct protein sequencing; Heme;
KW Hydrogen peroxide; Iron; Metal-binding; NADP; Oxidation; Oxidoreductase;
KW Peroxidase.
FT CHAIN 1..484
FT /note="Catalase"
FT /id="PRO_0000084992"
FT ACT_SITE 54
FT ACT_SITE 127
FT BINDING 337
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:0000269|PubMed:7791219"
FT MOD_RES 53
FT /note="Methionine sulfone"
FT /evidence="ECO:0000269|PubMed:7786407"
FT STRAND 17..19
FT /evidence="ECO:0007829|PDB:1E93"
FT STRAND 22..24
FT /evidence="ECO:0007829|PDB:1E93"
FT HELIX 34..43
FT /evidence="ECO:0007829|PDB:1E93"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1H6N"
FT STRAND 56..66
FT /evidence="ECO:0007829|PDB:1E93"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1E93"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:1E93"
FT STRAND 85..93
FT /evidence="ECO:0007829|PDB:1E93"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1E93"
FT STRAND 103..107
FT /evidence="ECO:0007829|PDB:1E93"
FT STRAND 110..117
FT /evidence="ECO:0007829|PDB:1E93"
FT STRAND 120..130
FT /evidence="ECO:0007829|PDB:1E93"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1E93"
FT HELIX 140..147
FT /evidence="ECO:0007829|PDB:1E93"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:1E93"
FT HELIX 158..166
FT /evidence="ECO:0007829|PDB:1E93"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:1E93"
FT HELIX 172..179
FT /evidence="ECO:0007829|PDB:1E93"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1E93"
FT STRAND 184..186
FT /evidence="ECO:0007829|PDB:1E93"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:1E93"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:1E93"
FT STRAND 208..217
FT /evidence="ECO:0007829|PDB:1E93"
FT HELIX 226..235
FT /evidence="ECO:0007829|PDB:1E93"
FT HELIX 239..249
FT /evidence="ECO:0007829|PDB:1E93"
FT STRAND 255..264
FT /evidence="ECO:0007829|PDB:1E93"
FT HELIX 265..269
FT /evidence="ECO:0007829|PDB:1E93"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:1E93"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:1E93"
FT STRAND 290..299
FT /evidence="ECO:0007829|PDB:1E93"
FT HELIX 304..307
FT /evidence="ECO:0007829|PDB:1E93"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:1E93"
FT HELIX 328..345
FT /evidence="ECO:0007829|PDB:1E93"
FT HELIX 349..351
FT /evidence="ECO:0007829|PDB:1E93"
FT TURN 353..355
FT /evidence="ECO:0007829|PDB:1E93"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:1M85"
FT STRAND 382..384
FT /evidence="ECO:0007829|PDB:1M85"
FT STRAND 386..388
FT /evidence="ECO:0007829|PDB:1E93"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:1E93"
FT HELIX 412..414
FT /evidence="ECO:0007829|PDB:1E93"
FT HELIX 420..428
FT /evidence="ECO:0007829|PDB:1E93"
FT HELIX 431..445
FT /evidence="ECO:0007829|PDB:1E93"
FT HELIX 450..463
FT /evidence="ECO:0007829|PDB:1E93"
FT HELIX 465..478
FT /evidence="ECO:0007829|PDB:1E93"
SQ SEQUENCE 484 AA; 55614 MW; ADC25F3CB41F5C50 CRC64;
MEKKKLTTAA GAPVVDNNNV ITAGPRGPML LQDVWFLEKL AHFDREVIPE RRMHAKGSGA
FGTFTVTHDI TKYTRAKIFS EVGKKTEMFA RFSTVAGERG AADAERDIRG FALKFYTEEG
NWDMVGNNTP VFYLRDPLKF PDLNHIVKRD PRTNMRNMAY KWDFFSHLPE SLHQLTIDMS
DRGLPLSYRF VHGFGSHTYS FINKDNERFW VKFHFRCQQG IKNLMDDEAE ALVGKDRESS
QRDLFEAIER GDYPRWKLQI QIMPEKEAST VPYNPFDLTK VWPHADYPLM DVGYFELNRN
PDNYFSDVEQ AAFSPANIVP GISFSPDKML QGRLFSYGDA HRYRLGVNHH QIPVNAPKCP
FHNYHRDGAM RVDGNSGNGI TYEPNSGGVF QEQPDFKEPP LSIEGAADHW NHREDEDYFS
QPRALYELLS DDEHQRMFAR IAGELSQASK ETQQRQIDLF TKVHPEYGAG VEKAIKVLEG
KDAK
