KATG2_BURVG
ID KATG2_BURVG Reviewed; 741 AA.
AC A4JPG0;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
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};
DE Flags: Precursor;
GN Name=katG2 {ECO:0000255|HAMAP-Rule:MF_01961};
GN OrderedLocusNames=Bcep1808_5214;
OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS (strain R1808)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=269482;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G4 / LMG 22486;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 2 of Burkholderia vietnamiensis G4.";
RL Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000615; ABO58163.1; -; Genomic_DNA.
DR AlphaFoldDB; A4JPG0; -.
DR SMR; A4JPG0; -.
DR STRING; 269482.Bcep1808_5214; -.
DR PeroxiBase; 2701; BviCP02.
DR EnsemblBacteria; ABO58163; ABO58163; Bcep1808_5214.
DR KEGG; bvi:Bcep1808_5214; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_4; -.
DR OMA; EEIFWGP; -.
DR Proteomes; UP000002287; 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 InterPro; IPR019793; Peroxidases_heam-ligand_BS.
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; PS00435; PEROXIDASE_1; 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; Signal.
FT SIGNAL 1..28
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CHAIN 29..741
FT /note="Catalase-peroxidase 2"
FT /id="PRO_5000232530"
FT ACT_SITE 108
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 269
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 104
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 107..228
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 254)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 228..254
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 107)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 741 AA; 80509 MW; D9D4B4A38E9E7964 CRC64;
MQRNRIAKSV LAALAVIAMS AGSISARADG APRANGFWWP ETLDLSPLRQ HDVESNPYGK
DFDYAQAFQK LDIEAVKKDI RTTLTTSQDW WPADYGNYGP FFIRMAWHGA GTYRTYDGRG
GAGGAQQRFE PLNSWPDNAN LDKARRLLWP IKKKYGQNIS WGDLMVLTGN VALESMGFQT
FGFGGGREDD WQSDLVYWGA GPKFMSNNRD KNGKLEKPLA ATQMGLIYVN PEGPNGNPDP
VAAAQDIREA FGRMAMNDEE TLALIAGGHT FGKAHGAASP DKCVGVAPAG AGVEAQGLGW
ANKCGTGKGV DTITSGLEGA WSVDPVHFTM QYLDNLLGHD WVLTKSPAGA HQWMPKDAQS
IVPDAHDPSK LHPLMMFTTD IALKVDPAYS KIAKRFEEHP DEFKLAFAKA WFKLTHRDLG
PKARYLGKDV PKVDLIWQDP LPVAGYQTIG AADIADLKSR ILASGLPKSE LIKTAWASAA
SFRGTDYRGG ANGARIRLAP ENGWAVNDPA SVAKVLKSLE AIQSGFNKGR TDGKQVSLAD
LIVLGGSAAV EDAARKAGYD ITVPFAPGRV DATQAQTDVA SFAVLEPTAD GFRNYYQKGN
ERSPAELLVD RASKLDLTVP EMTVLVGGLR ALDANTGHSK LGVLTNHPGT LSNEFFVNLL
DMSTEWKKSP SADGTYEGRD RKTGALRWTA SPVDLVFGSS SELRAVAEVY ASDDAHEKFV
RDFVAAWTKV MNLDRFDLKR I
