ID   CATA_VIBVY              Reviewed;         508 AA.
AC   Q7MFM6;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
DE   Flags: Precursor;
GN   OrderedLocusNames=VVA0294;
OS   Vibrio vulnificus (strain YJ016).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=196600;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YJ016;
RX   PubMed=14656965; DOI=10.1101/gr.1295503;
RA   Chen C.-Y., Wu K.-M., Chang Y.-C., Chang C.-H., Tsai H.-C., Liao T.-L.,
RA   Liu Y.-M., Chen H.-J., Shen A.B.-T., Li J.-C., Su T.-L., Shao C.-P.,
RA   Lee C.-T., Hor L.-I., Tsai S.-F.;
RT   "Comparative genome analysis of Vibrio vulnificus, a marine pathogen.";
RL   Genome Res. 13:2577-2587(2003).
CC   -!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to
CC       protect cells from the toxic effects of hydrogen peroxide.
CC       {ECO:0000250}.
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; Evidence={ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the catalase family. {ECO:0000305}.
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DR   EMBL; BA000038; BAC96320.1; -; Genomic_DNA.
DR   RefSeq; WP_011151700.1; NC_005140.1.
DR   AlphaFoldDB; Q7MFM6; -.
DR   SMR; Q7MFM6; -.
DR   STRING; 672.VV93_v1c32820; -.
DR   EnsemblBacteria; BAC96320; BAC96320; BAC96320.
DR   KEGG; vvy:VVA0294; -.
DR   PATRIC; fig|196600.6.peg.3501; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_4_0_6; -.
DR   OMA; WTCYVQV; -.
DR   OrthoDB; 1584770at2; -.
DR   Proteomes; UP000002675; 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   InterPro; IPR018028; Catalase.
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; Periplasm;
KW   Peroxidase; Reference proteome; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..508
FT                   /note="Catalase"
FT                   /id="PRO_0000004692"
FT   REGION          373..396
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        72
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   ACT_SITE        145
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10013"
FT   BINDING         353
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   508 AA;  56608 MW;  51A2E1BDC101B523 CRC64;
     MHMSKSFLLI SMGLASISVH AQTLTRDNGA PVGDNQNSIT AGENGSVLLQ DVHLIQKLQR
     FARERIPERV VHARGTGAHG EFVASGDFSD LTLSSPFAQS GKVTPVFVRF STVIHSKGSP
     ETLRDPRGFA TKFYTDQGNW DLVGNNLPVF FIRDSIKFPD MVHSLKPSPV TNLQDPNRFF
     DFFSSQPSAT NMLTWVYTNL GTPASYRTMD GFGVHAYKWI NQKGEVNYVK FHWKSQQGVK
     SLRPAEVTKV QGEDFNHLTN DLYTQINAGN FPKWDLYVKV LSPKALSKLD YNGLDATKVW
     LDVPEKKVGT MTLNRVPDNF FLETEQSAFA PSNIIPGIEP SEDRLLQGRL FAYADTQLYR
     LGANLFQLPV NSPKSPVANH NQDGPSNNST GLGNVDSLDV NYEPSRLVNL TVDKQARAVE
     TPLSGHVQQQ AIRNPRDFFQ AGVLYRSLSE QDKADLIHNL SGDLNKVNDA EVKAIMVSYF
     YRADKEYGTR LAKATDVNLK QVTKLASM