KATG2_VIBPA
ID KATG2_VIBPA Reviewed; 724 AA.
AC Q87I38;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Catalase-peroxidase 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase 2 {ECO:0000255|HAMAP-Rule:MF_01961};
GN Name=katG2 {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=VPA0768;
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: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275,
CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01961};
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=1.11.1.21;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC -!- COFACTOR:
CC Name=heme b; Xref=ChEBI:CHEBI:60344;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01961};
CC Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.
CC {ECO:0000255|HAMAP-Rule:MF_01961};
CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP-Rule:MF_01961}.
CC -!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is important
CC for the catalase, but not the peroxidase activity of the enzyme.
CC {ECO:0000255|HAMAP-Rule:MF_01961}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
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DR EMBL; BA000032; BAC62111.1; -; Genomic_DNA.
DR RefSeq; NP_800278.1; NC_004605.1.
DR RefSeq; WP_005481286.1; NC_004605.1.
DR AlphaFoldDB; Q87I38; -.
DR SMR; Q87I38; -.
DR STRING; 223926.28809003; -.
DR PeroxiBase; 2656; VpCP02_RIMD2210633.
DR EnsemblBacteria; BAC62111; BAC62111; BAC62111.
DR GeneID; 1191457; -.
DR KEGG; vpa:VPA0768; -.
DR PATRIC; fig|223926.6.peg.3701; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; MILAGNC; -.
DR Proteomes; UP000002493; Chromosome 2.
DR GO; GO:0004096; F:catalase activity; IEA:UniProtKB-UniRule.
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 HAMAP; MF_01961; Catal_peroxid; 1.
DR InterPro; IPR000763; Catalase_peroxidase.
DR InterPro; IPR002016; Haem_peroxidase.
DR InterPro; IPR010255; Haem_peroxidase_sf.
DR InterPro; IPR019794; Peroxidases_AS.
DR PANTHER; PTHR30555; PTHR30555; 1.
DR Pfam; PF00141; peroxidase; 2.
DR PRINTS; PR00460; BPEROXIDASE.
DR PRINTS; PR00458; PEROXIDASE.
DR SUPFAM; SSF48113; SSF48113; 2.
DR TIGRFAMs; TIGR00198; cat_per_HPI; 1.
DR PROSITE; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome.
FT CHAIN 1..724
FT /note="Catalase-peroxidase 2"
FT /id="PRO_0000354951"
FT ACT_SITE 99
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 267
FT /ligand="heme b"
FT /ligand_id="ChEBI:CHEBI:60344"
FT /ligand_part="Fe"
FT /ligand_part_id="ChEBI:CHEBI:18248"
FT /note="axial binding residue"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT SITE 95
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 98..226
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 252)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 226..252
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 98)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 724 AA; 80704 MW; 6F552DAA3ECD9EA9 CRC64;
MSNTNGGSVG KCPVMHGGQT STDKSVMDWW PNALNLDILH QHDSKTNPFG PDFNYKEELK
KLDVDALKQD LKDLMTNSQV WWPADWGHYG GLMIRMAWHA AGSYRIADGR GGAATGNQRF
APLNSWPDNA NLDKARRLLW PIKRKYGNKL SWADLIILAG NMAYESMGFK TFGFGFGRED
IWHPEKDTYW GSEQEWLAPS GAKNSRYSGE RDLENPLAAV MMGLIYVNPE GVDGNPDPLK
TAQDMRVTFA RMAMNDEETV ALTAGGHTVG KCHGNGDAAN LGPDPEGADV HEQGLGWMNH
KTRGIGRDTV TSGLEGAWTT HPTQWDNGYF YLLFKYDWEL KKSPAGAWQW EPIDIEEQDK
PVDVEDGSKR YNPIMTDADM ALKMDPEYRK ISERFQQDPA YFEDMFARAW FKLTHRDMGP
KSCYLGPDVP SEDLIWQDPT PAGKTDYNVD LVKGKIEASG LSIADLVATA WDSARTYRGS
DRRGGANGAR IRLAPQKDWQ GNEPERLSRV LAVLESIAAE EGCSVADAIV LAGNVGIELA
ARAAGHDVSV PFAPGRGDAS QDMTDVESFE VLEPVADGFR NWLKKDYVVK PEELLLDRAQ
LMGLTAPEMT VLIGGLRVLG SNYGGSKDGV FTDRVGTLSN DFFVNLTDMA YTWKPAGENQ
YEIRDRKTDQ VKWTATRVDL VFGSNSILRS YAEVYAQDDN QEKFIHDFVA AWTKVMNADR
FDLQ
