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 27-MAR-2024, entry version 135. DE RecName: Full=Catalase; DE EC=1.11.1.6; GN Name=katA; OS Proteus mirabilis. OC Bacteria; Pseudomonadota; 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}. 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 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; KFRWNVF; -. 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 Gene3D; 2.40.180.10; Catalase core domain; 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; CATALASE; 1. DR PANTHER; PTHR11465:SF61; CATALASE; 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 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 //