ID   CATA_DESVM              Reviewed;         480 AA.
AC   Q9ZN99; B8DLD0;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 2.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=katA; Synonyms=kat; OrderedLocusNames=DvMF_1242;
OS   Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=883;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Kitamura M., Kojima S., Akutsu H., Kumagai I., Nakaya T.;
RT   "Catalase from strictly anaerobic bacteria, Desulfovibrio vulgaris
RT   (Miyazaki F).";
RL   Submitted (NOV-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19637 / Miyazaki F;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C.,
RA   Richardson P.;
RT   "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL   Submitted (OCT-2008) 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   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; AB020341; BAA34670.1; -; Genomic_DNA.
DR   EMBL; CP001197; ACL08192.1; -; Genomic_DNA.
DR   RefSeq; WP_012612380.1; NC_011769.1.
DR   AlphaFoldDB; Q9ZN99; -.
DR   SMR; Q9ZN99; -.
DR   STRING; 883.DvMF_1242; -.
DR   PRIDE; Q9ZN99; -.
DR   EnsemblBacteria; ACL08192; ACL08192; DvMF_1242.
DR   KEGG; dvm:DvMF_1242; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_2_0_7; -.
DR   OMA; WTCYVQV; -.
DR   OrthoDB; 1584770at2; -.
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..480
FT                   /note="Catalase"
FT                   /id="PRO_0000084985"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..16
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        54
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        127
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         337
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        103
FT                   /note="D -> T (in Ref. 1; BAA34670)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        416
FT                   /note="Missing (in Ref. 1; BAA34670)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   480 AA;  54678 MW;  EAE7540616B77AE4 CRC64;
     MTKHKLTTNA GAPVPDNQNA MTAGPRGPML LQDVWFLEKL AHFDREVIPE RRMHAKGSGA
     YGTFTVTHDI TSYTKAALFS KIGKKTDLFV RFSTVAGERG AADAERDIRG FAIKFYTEQG
     NWDLVGNNTP VFFLRDPLKF PDLNHAVKRD PRTNMRSAKN NWDFWTSLPE ALHQVTVVMS
     DRGIPASYRH MHGFGSHTFS FISPDNQRYW VKFHLRTQQG IKNLTDAEAE AIVARDRESH
     QRDLYDSIER GDFPRWTMYV QVMPEKDAEK LPYHPFDLTK VWFHKDCPLI EVGVLELNRN
     PENYFAEVEQ AAFNPANVVP GISFSPDKML QGRLFSYGDA HRYRLGVNHH LIPVNAARCP
     VHSYHRDGAM RVDGNHGSTL AYEPNSYGEW QEQPDFAEPP LAIRGDAAHW NFREDDADYY
     DQPGRLFRLM TPQQQDELFQ NTARAMGDAP EEIKRRHVGN CAKADPAYGA GVARALGLKM