CATB_PSESY
ID CATB_PSESY Reviewed; 510 AA.
AC P46206; P95545;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
DE Flags: Precursor;
GN Name=katB; Synonyms=catF;
OS Pseudomonas syringae pv. syringae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Pss61;
RX PubMed=7546603; DOI=10.1007/bf00164770;
RA Klotz M.G., Kim Y.C., Katsuwon J., Anderson A.J.;
RT "Cloning, characterization and phenotypic expression in Escherichia coli of
RT catF, which encodes the catalytic subunit of catalase isozyme CatF of
RT Pseudomonas syringae.";
RL Appl. Microbiol. Biotechnol. 43:656-666(1995).
RN [2]
RP SEQUENCE REVISION TO C-TERMINUS.
RA Klotz M.G.;
RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AF001355; AAC61659.1; -; Genomic_DNA.
DR PDB; 1M7S; X-ray; 1.80 A; A/B/C/D=27-510.
DR PDBsum; 1M7S; -.
DR AlphaFoldDB; P46206; -.
DR SMR; P46206; -.
DR PRIDE; P46206; -.
DR SABIO-RK; P46206; -.
DR EvolutionaryTrace; P46206; -.
DR GO; GO:0042597; C:periplasmic space; 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 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; 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; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW Periplasm; Peroxidase; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000255"
FT CHAIN 27..510
FT /note="Catalase"
FT /id="PRO_0000004694"
FT REGION 386..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 386..403
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 78
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT ACT_SITE 150
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT BINDING 358
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 41..43
FT /evidence="ECO:0007829|PDB:1M7S"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1M7S"
FT HELIX 58..67
FT /evidence="ECO:0007829|PDB:1M7S"
FT STRAND 80..90
FT /evidence="ECO:0007829|PDB:1M7S"
FT TURN 95..97
FT /evidence="ECO:0007829|PDB:1M7S"
FT HELIX 101..103
FT /evidence="ECO:0007829|PDB:1M7S"
FT STRAND 108..116
FT /evidence="ECO:0007829|PDB:1M7S"
FT STRAND 118..120
FT /evidence="ECO:0007829|PDB:1M7S"
FT STRAND 133..140
FT /evidence="ECO:0007829|PDB:1M7S"
FT STRAND 143..154
FT /evidence="ECO:0007829|PDB:1M7S"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:1M7S"
FT HELIX 163..170
FT /evidence="ECO:0007829|PDB:1M7S"
FT TURN 174..176
FT /evidence="ECO:0007829|PDB:1M7S"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:1M7S"
FT HELIX 192..194
FT /evidence="ECO:0007829|PDB:1M7S"
FT HELIX 195..202
FT /evidence="ECO:0007829|PDB:1M7S"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:1M7S"
FT STRAND 207..209
FT /evidence="ECO:0007829|PDB:1M7S"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:1M7S"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:1M7S"
FT STRAND 231..240
FT /evidence="ECO:0007829|PDB:1M7S"
FT HELIX 249..258
FT /evidence="ECO:0007829|PDB:1M7S"
FT HELIX 262..272
FT /evidence="ECO:0007829|PDB:1M7S"
FT STRAND 278..286
FT /evidence="ECO:0007829|PDB:1M7S"
FT HELIX 288..293
FT /evidence="ECO:0007829|PDB:1M7S"
FT STRAND 294..296
FT /evidence="ECO:0007829|PDB:1M7S"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:1M7S"
FT STRAND 310..321
FT /evidence="ECO:0007829|PDB:1M7S"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:1M7S"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:1M7S"
FT STRAND 343..345
FT /evidence="ECO:0007829|PDB:1M7S"
FT HELIX 349..365
FT /evidence="ECO:0007829|PDB:1M7S"
FT HELIX 370..372
FT /evidence="ECO:0007829|PDB:1M7S"
FT HELIX 374..376
FT /evidence="ECO:0007829|PDB:1M7S"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:1M7S"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:1M7S"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:1M7S"
FT STRAND 425..428
FT /evidence="ECO:0007829|PDB:1M7S"
FT HELIX 439..447
FT /evidence="ECO:0007829|PDB:1M7S"
FT HELIX 450..464
FT /evidence="ECO:0007829|PDB:1M7S"
FT HELIX 469..482
FT /evidence="ECO:0007829|PDB:1M7S"
FT HELIX 484..493
FT /evidence="ECO:0007829|PDB:1M7S"
FT HELIX 498..506
FT /evidence="ECO:0007829|PDB:1M7S"
SQ SEQUENCE 510 AA; 56865 MW; A64C96552BCB1DD3 CRC64;
MPLLNWSRHM VCLTAAGLIT VPTVYATDTL TRDNGAVVGD NQNSQTAGAQ GPVLLQDVQL
LQKLQRFDRE RIPERVVHAR GTGVKGEFTA SADISDLSKA TVFKSGEKTP VFVRFSSVVH
GNHSPETLRD PHGFATKFYT ADGNWDLVGN NFPTFFIRDA IKFPDMVHAF KPDPRTNLDN
DSRRFDFFSH VPEATRTLTL LYSNEGTPAG YRFMDGNGVH AYKLVNAKGE VHYVKFHWKS
LQGIKNLDPK EVAQVQSKDY SHLTNDLVGA IKKGDFPKWD LYVQVLKPEE LAKFDFDPLD
ATKIWPDVPE KKIGQMVLNK NVDNFFQETE QVAMAPANLV PGIEPSEDRL LQGRVFSYAD
TQMYRLGAIG LSLPVNQPKV AVNNGNQDGA LNTGHTTSGV NYEPSRLEPR PADDKARYSE
LPLSGTTQQA KITREQNFKQ AGDLFRSYSA KEKTDLVQRF GESLADTHTE SKNIMLSVLY
KEDRHYGTRV AEVAKGDLSK VKSLAASLKD
