ID   CATA_ALIF1              Reviewed;         482 AA.
AC   O68146; Q5E1L7;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
GN   Name=katA; OrderedLocusNames=VF_A0009;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9555890; DOI=10.1128/jb.180.8.2087-2092.1998;
RA   Visick K., Ruby E.G.;
RT   "The periplasmic, group III catalase of Vibrio fischeri is required for
RT   normal symbiotic competence and is induced both by oxidative stress and by
RT   approach to stationary phase.";
RL   J. Bacteriol. 180:2087-2092(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC       protect cells from the toxic effects of hydrogen peroxide. Could
CC       protect cells in nodules which have a high potential to produce
CC       hydrogen peroxide because of the strong reducing conditions required
CC       for nitrogen fixation and the action of several proteins.
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   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- INDUCTION: By hydrogen peroxide.
CC   -!- MISCELLANEOUS: Either KatA or KatC is absolutely required for the
CC       protection of the nitrogen fixation process.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; AF011784; AAC38344.1; -; Genomic_DNA.
DR   EMBL; CP000021; AAW87079.1; -; Genomic_DNA.
DR   RefSeq; WP_011262914.1; NC_006841.2.
DR   RefSeq; YP_205967.1; NC_006841.2.
DR   AlphaFoldDB; O68146; -.
DR   SMR; O68146; -.
DR   STRING; 312309.VF_A0009; -.
DR   EnsemblBacteria; AAW87079; AAW87079; VF_A0009.
DR   KEGG; vfi:VF_A0009; -.
DR   PATRIC; fig|312309.11.peg.2611; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_2_0_6; -.
DR   OMA; WTCYVQV; -.
DR   OrthoDB; 1584770at2; -.
DR   Proteomes; UP000000537; Chromosome II.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
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   2: Evidence at transcript level;
KW   Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Periplasm;
KW   Peroxidase; Reference proteome.
FT   CHAIN           1..482
FT                   /note="Catalase"
FT                   /id="PRO_0000085012"
FT   ACT_SITE        53
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        126
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         336
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   482 AA;  54864 MW;  3808F0DBDE4DCC32 CRC64;
     MSKKLTTAAG CPVAHNQNVQ TAGKRGPQLL QDVWFLEKLA HFDREVIPER RMHAKGSGAY
     GTFTVTHDIT KYTKAKLFSE IGKQTELFAR FTTVAGERGA ADAERDIRGF ALKFYTEEGN
     WDLVGNNTPV FFLRDPLKFP DLNHAVKRDP RTNMRSAKNN WDFWTSLPEA LHQVTIVMSD
     RGIPATYRHM HGFGSHTFSF INSDNERFWV KFHFKSQQGI KNLSDAEAAQ VIGQDRESHQ
     RDLLESIDNQ DFPKWTLKVQ IMPEADAATV PYNPFDLTKV WPHKDYPLIE VGEFELNRNP
     QNFFAEVEQS AFNPANVVPG ISFSPDKMLQ GRLFAYGDAQ RYRLGVNHQH IPVNAPRCPV
     HSYHRDGAMR VDGNFGSTLG YEPNNEGQWA EQPDFAEPAL NLDGAAAHWD HREDEDYFSQ
     PGDLFRLMTA EQQAILFDNT ARNLNGVPKE IQLRHLRHCY KADPAYGEGI GKLLDIDVSE
     FN