KATG2_BURA4
ID KATG2_BURA4 Reviewed; 741 AA.
AC B1Z5M2;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 73.
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=BamMC406_5625;
OS Burkholderia ambifaria (strain MC40-6).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=398577;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC40-6;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Ramette A.,
RA Konstantinidis K., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 3 of Burkholderia ambifaria MC40-6.";
RL Submitted (APR-2008) 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; CP001027; ACB68068.1; -; Genomic_DNA.
DR RefSeq; WP_012372008.1; NC_010557.1.
DR AlphaFoldDB; B1Z5M2; -.
DR SMR; B1Z5M2; -.
DR EnsemblBacteria; ACB68068; ACB68068; BamMC406_5625.
DR KEGG; bac:BamMC406_5625; -.
DR HOGENOM; CLU_025424_2_0_4; -.
DR OMA; EEIFWGP; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000001680; Chromosome 3.
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 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_5000334004"
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; 80998 MW; 67DA44587234D352 CRC64;
MQKKRIGKSV VAALAIIAMS AGTVAAWADG APRTNDFWWP ERLDLSPLRQ HDVESNPYGK
DFDYAQAFNK LDIEAVKKDI RATLTTSQDW WPADYGNYGP FFIRMAWHGA GTYRTYDGRG
GAGGAQQRFE PLNSWPDNAN LDKARRLLWP IKKKYGQNIS WGDLMVLTGN VALESMGFQT
FGFGGGREDD WQSDLVYWGA GTKFMSDNRD KNGKLEKPLA ATQMGLIYVN PEGPNGNPDP
VAAAKDIREA FGRMAMNDEE TLALIAGGHT FGKAHGAASP DKCVGAAPAG AGVEAQGLGW
ANKCGTGKGA DTITSGLEGA WSVDPVHFTM QYLDNLLEHD WVLTKSPAGA HQWMPKDAQD
IVPDAHDPSK RHPLMMFTTD IALKVDPAYS AIAKRFQAHP EEFKLAFAKA WFKLTHRDLG
PKARYLGKDV PKVDLIWQDP LPVAGYQMIG DADIAELKRR ILASGVPKSE LIKTAWASAA
SFRATDYRGG ANGARIRLAP ENAWAVNDPA SLSKVLKSLE DIQSGFNRNR TDGKQVSLAD
LIVLGGSAAV EDAARKAGYD VKVPFSPGRV DATQAQTDVA SFAVLEPTSD GFRNYYRKSN
ERSPAELMVD RASKLDLSVP EMTVLVGGLR ALDANAGHSR LGVLTNRPGT LSNDFFVNLL
DMSTQWTKSS SADGTYEGRD RKTGALKWTA SPVDLVFGSS SELRAVAEVY ASDDAHEKFV
RDFVHAWTKV MNLDRFDLKR S
