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 27-MAR-2024, entry version 107.
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; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Nitratidesulfovibrio.
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 AlphaFoldDB; Q9ZN99; -.
DR SMR; Q9ZN99; -.
DR STRING; 883.DvMF_1242; -.
DR KEGG; dvm:DvMF_1242; -.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_010645_2_0_7; -.
DR OrthoDB; 3169619at2; -.
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 Gene3D; 2.40.180.10; Catalase core domain; 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; CATALASE; 1.
DR PANTHER; PTHR11465:SF61; CATALASE; 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; Heme-dependent catalase-like; 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
//
