CATA_CAMJE
ID CATA_CAMJE Reviewed; 474 AA.
AC Q59296; Q0P8M4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 17-JUN-2020, sequence version 2.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
GN Name=katA; OrderedLocusNames=Cj1385;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33560 / CIP 702 / DSM 4688 / NCTC 11351;
RX PubMed=7670638; DOI=10.1099/13500872-141-6-1369;
RA Grant K.A., Park S.F.;
RT "Molecular characterization of katA from Campylobacter jejuni and
RT generation of a catalase-deficient mutant of Campylobacter coli by
RT interspecific allelic exchange.";
RL Microbiology 141:1369-1376(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
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 -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
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 EMBL; X85130; CAA59444.1; -; Genomic_DNA.
DR EMBL; AL111168; CAL35497.1; -; Genomic_DNA.
DR PIR; F81283; F81283.
DR PIR; I40767; I40767.
DR RefSeq; WP_002856117.1; NC_002163.1.
DR RefSeq; YP_002344773.1; NC_002163.1.
DR AlphaFoldDB; Q59296; -.
DR SMR; Q59296; -.
DR IntAct; Q59296; 37.
DR STRING; 192222.Cj1385; -.
DR PeroxiBase; 5383; CjejKat01.
DR PaxDb; Q59296; -.
DR PRIDE; Q59296; -.
DR EnsemblBacteria; CAL35497; CAL35497; Cj1385.
DR GeneID; 905678; -.
DR KEGG; cje:Cj1385; -.
DR PATRIC; fig|192222.6.peg.1366; -.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_010645_2_0_7; -.
DR OMA; WTCYVQV; -.
DR Proteomes; UP000000799; Chromosome.
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; 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; PS51402; CATALASE_3; 1.
PE 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome.
FT CHAIN 1..474
FT /note="Catalase"
FT /id="PRO_0000084983"
FT ACT_SITE 52
FT /evidence="ECO:0000250"
FT ACT_SITE 124
FT /evidence="ECO:0000250"
FT BINDING 334
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 CONFLICT 23
FT /note="A -> T (in Ref. 1; CAA59444)"
FT /evidence="ECO:0000305"
FT CONFLICT 82
FT /note="V -> I (in Ref. 1; CAA59444)"
FT /evidence="ECO:0000305"
FT CONFLICT 177
FT /note="S -> R (in Ref. 1; CAA59444)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="F -> L (in Ref. 1; CAA59444)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="A -> T (in Ref. 1; CAA59444)"
FT /evidence="ECO:0000305"
FT CONFLICT 455
FT /note="K -> E (in Ref. 1; CAA59444)"
FT /evidence="ECO:0000305"
FT CONFLICT 472..474
FT /note="LEK -> FPIVSRIRAWRNHGHRCFLCEIVIRSQFHTTYEPEA (in Ref.
FT 1; CAA59444)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 54323 MW; A694600028CA7D5C CRC64;
MKKLTNDFGN IIADNQNSLS AGAKGPLLMQ DYLLLEKLAH QNRERIPERT VHAKGSGAYG
EIKITADLSA YTKAKIFQKG EVTPLFLRFS TVAGEAGAAD AERDVRGFAI KFYTKEGNWD
LVGNNTPTFF IRDAYKFPDF IHTQKRDPRT HLRSNNAAWD FWSLCPESLH QVTILMSDRG
IPASYRHMHG FGSHTYSFIN DKNERFWVKF HFKTQQGIKN LTNQEAAELI AKDRESHQRD
LYNAIENKDF PKWKVQVQIL AEKDIEKLGF NPFDLTKIWP HSFVPLMDIG EMILNKNPQN
YFNEVEQAAF SPSNIVPGIG FSPDKMLQAR IFSYPDAQRY RIGTNYHLLP VNRAKSEVNT
YNVAGAMNFD SYKNDAAYYE PNSYDNSPKE DKSYLEPDLV LEGVAQRYAP LDNDFYTQPR
ALFNLMNDDQ KTQLFHNIAA SMEGVDEKII TRALKHFEKI SPDYAKGIKK ALEK
