CATA_VIBVU
ID CATA_VIBVU Reviewed; 508 AA.
AC Q8D452;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
DE Flags: Precursor;
GN OrderedLocusNames=VV2_1473;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) 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 {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; AE016796; AAO08343.2; -; Genomic_DNA.
DR RefSeq; WP_011082332.1; NC_004460.2.
DR AlphaFoldDB; Q8D452; -.
DR SMR; Q8D452; -.
DR EnsemblBacteria; AAO08343; AAO08343; VV2_1473.
DR KEGG; vvu:VV2_1473; -.
DR HOGENOM; CLU_010645_4_0_6; -.
DR OMA; WTCYVQV; -.
DR Proteomes; UP000002275; Chromosome 2.
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; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..508
FT /note="Catalase"
FT /id="PRO_0000004691"
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; 56664 MW; 2E594ECD51B261E6 CRC64;
MHMSKSFLLI SMGLASISVH AQTLTRDNGA PVGDNQNSIT AGENGSVLLQ DVHLIQKLQR
FARERIPERV VHARGTGAHG EFVVSGDFSD LTLSSPFAQS GKVTPVFVRF STVIHSKGSP
ETLRDPRGFA TKFYTDQGNW DLVGNNLPVF FIRDSIKFPD MVHSLKPSPV TNLQDPNRFF
DFFSSQPSAT NMLTWVYTNL GTPASYRTMD GFGVHAYKWI NRKGEVNYVK 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