ID   CATA_NEIGO              Reviewed;         500 AA.
AC   Q59602;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=katA;
OS   Neisseria gonorrhoeae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=485;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8698488; DOI=10.1128/iai.64.7.2627-2634.1996;
RA   Johnson S.R., Steiner B.M., Perkins G.H.;
RT   "Cloning and characterization of the catalase gene of Neisseria
RT   gonorrhoeae: use of the gonococcus as a host organism for recombinant
RT   DNA.";
RL   Infect. Immun. 64:2627-2634(1996).
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   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; U35457; AAB18144.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59602; -.
DR   SMR; Q59602; -.
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; 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   3: Inferred from homology;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT   CHAIN           1..500
FT                   /note="Catalase"
FT                   /id="PRO_0000084991"
FT   ACT_SITE        59
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        131
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         339
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"
SQ   SEQUENCE   500 AA;  56671 MW;  CBF76FD8951B0D5F CRC64;
     MTTSKCPVTH LTMNNGAPVA DNQNSLTAGT RGPLLTQDLW LNEKLADFVR EVIPERRMHA
     KGSGAFGTFT VTRDITKYTR AKIFSEVGKK TEMFGRLATV AGERGADAYT RVRGFALKFY
     TEEGNWDVVG NNTPVFYPDL RKFPDLNKAV KRSAHQYSSA TNNWDFWALL PEALHQVTIV
     MSDRGIPASY RHMHGFGSHT YSLWNEAGER FWVKFHFRSQ QGIKNLTNEE AAKIIADDRE
     SHQRDLYEAI ERGEFPKWTM YIQVMPEADA AKVPYHPFDL TKVWPKKDYP LIEVAEFELN
     RNPENFFADV EQSAFAPSNL VPGIGASPDK MLQARLFNYA DAQRYRLGVN FRQIPVNRPR
     CPVHSNQRDG QGRATELRQP AHYEPNSFGQ WSQQPDFAEP PLKINGDAAH WDYRQDDDDY
     FSQPRALFNL MNDAQKQALF DNTAAAMGDA PDFIKYRHIR NCYRCDPAYG EGGSKALGLT
     VEEPQAARAT DPALGQGGLL