GenomeNet

Database: UniProt
Entry: Q59296
LinkDB: Q59296
Original site: Q59296 
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-OCT-2014, entry version 88.
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. {ECO:0000305}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs 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; 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   OrthoDB; EOG6P5Z9F; -.
DR   BioCyc; CJEJ192222:GJTS-1358-MONOMER; -.
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   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; SSF56634; 1.
DR   PROSITE; PS00437; CATALASE_1; 1.
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       {ECO:0000250}.
FT   ACT_SITE    124    124       {ECO:0000250}.
FT   METAL       334    334       Iron (heme axial ligand). {ECO:0000250}.
FT   CONFLICT     23     23       T -> A (in Ref. 2; CAL35497).
FT                                {ECO:0000305}.
FT   CONFLICT     82     82       I -> V (in Ref. 2; CAL35497).
FT                                {ECO:0000305}.
FT   CONFLICT    177    177       R -> S (in Ref. 2; CAL35497).
FT                                {ECO:0000305}.
FT   CONFLICT    283    283       L -> F (in Ref. 2; CAL35497).
FT                                {ECO:0000305}.
FT   CONFLICT    440    440       T -> A (in Ref. 2; CAL35497).
FT                                {ECO:0000305}.
FT   CONFLICT    455    455       E -> K (in Ref. 2; CAL35497).
FT                                {ECO:0000305}.
FT   CONFLICT    472    507       FPIVSRIRAWRNHGHRCFLCEIVIRSQFHTTYEPEA -> L
FT                                EK (in Ref. 2; CAL35497). {ECO:0000305}.
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
//
DBGET integrated database retrieval system