ID CATA_CAMJE Reviewed; 507 AA.
AC Q59296; Q0P8M4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 01-MAY-2013, entry version 83.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
GN Name=katA; OrderedLocusNames=Cj1385;
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 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;
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=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.,
RA Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M.,
RA Whitehead S., 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;
CC serves to protect cells from the toxic effects of hydrogen
CC peroxide.
CC -!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
CC -!- COFACTOR: Heme group.
CC -!- SIMILARITY: Belongs to the catalase family.
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DR EMBL; X85130; CAA59444.1; -; Genomic_DNA.
DR EMBL; AL111168; CAL35497.1; -; Genomic_DNA.
DR PIR; F81283; F81283.
DR PIR; I40767; I40767.
DR RefSeq; YP_002344773.1; NC_002163.1.
DR ProteinModelPortal; Q59296; -.
DR SMR; Q59296; 2-474.
DR IntAct; Q59296; 37.
DR STRING; 192222.Cj1385; -.
DR PeroxiBase; 5383; CjejKat01.
DR EnsemblBacteria; CAL35497; CAL35497; Cj1385.
DR GeneID; 905678; -.
DR KEGG; cje:Cj1385; -.
DR PATRIC; 20059735; VBICamJej33762_1366.
DR eggNOG; COG0753; -.
DR HOGENOM; HOG000087852; -.
DR KO; K03781; -.
DR ProtClustDB; CLSK879231; -.
DR BioCyc; CJEJ192222:GJTS-1358-MONOMER; -.
DR GO; GO:0004096; F:catalase activity; IEA: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 Gene3D; 2.40.180.10; -; 1.
DR InterPro; IPR018028; Catalase.
DR InterPro; IPR020835; Catalase-like_dom.
DR InterPro; IPR024711; Catalase_clade1/3.
DR InterPro; IPR011614; Catalase_core.
DR InterPro; IPR002226; Catalase_haem_BS.
DR InterPro; IPR010582; Catalase_immune_responsive.
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; Catalase_N; 1.
DR PROSITE; PS00437; CATALASE_1; 1.
DR PROSITE; PS00438; CATALASE_2; FALSE_NEG.
DR PROSITE; PS51402; CATALASE_3; 1.
PE 3: Inferred from homology;
KW Complete proteome; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW Oxidoreductase; Peroxidase; Reference proteome.
FT CHAIN 1 507 Catalase.
FT /FTId=PRO_0000084983.
FT ACT_SITE 52 52 By similarity.
FT ACT_SITE 124 124 By similarity.
FT METAL 334 334 Iron (heme axial ligand) (By similarity).
FT CONFLICT 23 23 T -> A (in Ref. 2; CAL35497).
FT CONFLICT 82 82 I -> V (in Ref. 2; CAL35497).
FT CONFLICT 177 177 R -> S (in Ref. 2; CAL35497).
FT CONFLICT 283 283 L -> F (in Ref. 2; CAL35497).
FT CONFLICT 440 440 T -> A (in Ref. 2; CAL35497).
FT CONFLICT 455 455 E -> K (in Ref. 2; CAL35497).
FT CONFLICT 472 507 FPIVSRIRAWRNHGHRCFLCEIVIRSQFHTTYEPEA -> L
FT EK (in Ref. 2; CAL35497).
SQ SEQUENCE 507 AA; 58416 MW; B1320894668E867E CRC64;
MKKLTNDFGN IIADNQNSLS AGTKGPLLMQ DYLLLEKLAH QNRERIPERT VHAKGSGAYG
EIKITADLSA YTKAKIFQKG EITPLFLRFS TVAGEAGAAD AERDVRGFAI KFYTKEGNWD
LVGNNTPTFF IRDAYKFPDF IHTQKRDPRT HLRSNNAAWD FWSLCPESLH QVTILMRDRG
IPASYRHMHG FGSHTYSFIN DKNERFWVKF HFKTQQGIKN LTNQEAAELI AKDRESHQRD
LYNAIENKDF PKWKVQVQIL AEKDIEKLGF NPFDLTKIWP HSLVPLMDIG EMILNKNPQN
YFNEVEQAAF SPSNIVPGIG FSPDKMLQAR IFSYPDAQRY RIGTNYHLLP VNRAKSEVNT
YNVAGAMNFD SYKNDAAYYE PNSYDNSPKE DKSYLEPDLV LEGVAQRYAP LDNDFYTQPR
ALFNLMNDDQ KTQLFHNIAT SMEGVDEKII TRALEHFEKI SPDYAKGIKK AFPIVSRIRA
WRNHGHRCFL CEIVIRSQFH TTYEPEA
//
