ID   CATA_VIBCH              Reviewed;         503 AA.
AC   Q9KRQ1;
DT   15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 106.
DE   RecName: Full=Catalase;
DE            EC=1.11.1.6;
DE   Flags: Precursor;
GN   OrderedLocusNames=VC_1585;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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=AAF94739.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE003852; AAF94739.2; ALT_INIT; Genomic_DNA.
DR   PIR; C82183; C82183.
DR   RefSeq; NP_231225.2; NC_002505.1.
DR   RefSeq; WP_000551119.1; NC_002505.1.
DR   STRING; 243277.VC_1585; -.
DR   PRIDE; Q9KRQ1; -.
DR   DNASU; 2613839; -.
DR   EnsemblBacteria; AAF94739; AAF94739; VC_1585.
DR   KEGG; vch:VC_1585; -.
DR   PATRIC; fig|243277.26.peg.1512; -.
DR   eggNOG; COG0753; Bacteria.
DR   HOGENOM; CLU_010645_4_0_6; -.
DR   OMA; WTCYVQV; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004096; F:catalase activity; IBA:GO_Central.
DR   GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
DR   GO; GO:0042542; P:response to hydrogen peroxide; IBA:GO_Central.
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..503
FT                   /note="Catalase"
FT                   /id="PRO_0000004689"
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   503 AA;  56552 MW;  9C4CAECDB109118D CRC64;
     MHMSKSFLII SMGFVAVSVQ AQTLTRDNGA PVGDNQNSIT AGEHGSVLLQ DVHLIQKLQR
     FARERIPERV VHARGTGAHG EFVASGDFSD LTLSAPFTSK GKITPVFVRF STVIHSKGSP
     ETLRDPRGFA TKFYTEQGNW DLVGNNLPVF FIRDSIKFPD MVHSLKPSPV TNLQDPNRFF
     DFFSHEPGST HMLTWVYTNL GTPASYRTMD GFGVHAYKWI NQKGDVNYVK FHWKSLQGIE
     SLRPDEVVKV QGQDFNHLTN DLYTQINAGN HPKWDLYVQV LTPEQLSKLD YNGLDATKVW
     LDVPEKKVGT MTLNKVPDNF FLETEQSAFA PSNLIPGIEP SEDRLLQGRL FAYADTQLYR
     LGANLFQLPI NRPLVEVNSH NQEGASNSAQ TASDINYQPS RKLELKEDPQ FKAVQTQLVG
     SVQQKAISNP RNFYQAGVLY RSLNEQDKQD LITNLXGBLN KVTDKEIKAT MVSHFYRADK
     DYGTRLARAT NTDLKQVAKL AAM