CATA_VIBPA
ID CATA_VIBPA Reviewed; 504 AA.
AC Q87JE8;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Catalase;
DE EC=1.11.1.6;
DE Flags: Precursor;
GN OrderedLocusNames=VPA0305;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC61648.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000032; BAC61648.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_799815.1; NC_004605.1.
DR RefSeq; WP_021450939.1; NC_004605.1.
DR AlphaFoldDB; Q87JE8; -.
DR SMR; Q87JE8; -.
DR STRING; 223926.28808471; -.
DR EnsemblBacteria; BAC61648; BAC61648; BAC61648.
DR GeneID; 1190993; -.
DR KEGG; vpa:VPA0305; -.
DR PATRIC; fig|223926.6.peg.3257; -.
DR eggNOG; COG0753; Bacteria.
DR HOGENOM; CLU_010645_2_0_6; -.
DR OMA; HVWPQKQ; -.
DR Proteomes; UP000002493; 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; Reference proteome; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..504
FT /note="Catalase"
FT /id="PRO_0000004690"
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 504 AA; 56585 MW; A62EA2603CC9AD3C CRC64;
MQMSKSFLLI TVGLASTSLQ AQTLTRDNGA PVGDNQNSIT AGENGSVLLQ DVHLIQKLQR
FARERIPERV VHARGTGAHG EFVASGDFSD LTVSAPFTEK GKVTPVFVRF STVIHSKGSP
ETLRDPRGFA TKFYTEQGNW DLVGNNLPVF FIRDSIKFPD MVHSLKPSPV TNVQDPNRFF
DFFSHEPSAT HMLTWVYSNL GTPASYRTMD GFGVHAYKWI NQQGDVNYVK FQWKSQQGIK
SLRPNKVTEM QGKDFNHLTN DLYAAIGRGN YPKWDLYVKV LSPEALSKLD YNGLDATKVW
LNVPDRKVGT MTLNRLPENF FLETEQSAFA PSNLIPGIEP SEDRLLQGRL FAYADTQLYR
LGANLFQLPV NRPLTSVNNH NQNGLSNNAQ LSNGDVNYEP SRKLNLAEDN QFKAVETKLV
GTVQQKAISK PRDFYQAGVL YRSMNEQDRS DLIANLAGDL NKVIDKDIKA TMVSYFYRAD
KEYGSRLAEA TDTNLSQVKN KAMM