KATG2_BURCM
ID KATG2_BURCM Reviewed; 741 AA.
AC Q0B385;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 88.
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}; OrderedLocusNames=Bamb_5842;
OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS (strain AMMD)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=339670;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-244 / AMMD;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA Ramette A., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 3 of Burkholderia cepacia AMMD.";
RL Submitted (AUG-2006) 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; CP000442; ABI91388.1; -; Genomic_DNA.
DR RefSeq; WP_011660735.1; NC_008392.1.
DR AlphaFoldDB; Q0B385; -.
DR SMR; Q0B385; -.
DR STRING; 339670.Bamb_5842; -.
DR PeroxiBase; 2702; BamCP02.
DR PRIDE; Q0B385; -.
DR EnsemblBacteria; ABI91388; ABI91388; Bamb_5842.
DR GeneID; 44696389; -.
DR KEGG; bam:Bamb_5842; -.
DR PATRIC; fig|339670.21.peg.6795; -.
DR eggNOG; COG0376; Bacteria.
DR OMA; EEIFWGP; -.
DR Proteomes; UP000000662; 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_5000128247"
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; 80910 MW; 7BDB180568080277 CRC64;
MQKKRVGKSV VAALAIIAMS AGTVAAWADG APRTNDFWWP ERLDLSPLRQ HDVESNPYGK
DFDYAQAFNK LDIEAVKKDI RATLTTSQDW WPADYGNYGP FFIRMAWHGA GTYRTYDGRG
GAGGAQQRFE PLNSWPDNAN LDKARRLLWP IKKKYGENIS WGDLMVLTGN VALESMGFQT
FGFGGGREDD WQSDLVYWGA GTKFMSNNRD KNGKLEKPLA ATQMGLIYVN PEGPNGNPDP
VAAAKDIRDA FGRMAMNDEE TLALIAGGHT FGKAHGAASP DKCVGAAPAG AGVEAQGLGW
ANKCGTGKGA DTITSGLEGA WSVDPVHFTM QYLDNLLEHD WVLTKSPAGA HQWMPKDAQD
IVPDAHDPSK RHPLMMFTTD IALKVDPAYS AIAKRFHAHP EEFKLAFAKA WFKLTHRDLG
PKARYLGKDV PKVDLIWQDP LPVAGYQMIG DADIAELKRR ILASGVPKAE LIKTAWASAA
SFRATDYRGG ANGARIRLAP ENDWAVNDPA SLSKVLKSLE GIQSGFNRNR TDGKQVSLAD
LIVLGGSAAV EDAARKAGYD VKVPFSPGRV DATQAQTDVA SFAVLEPTAD GFRNYYQKSN
ERSPAELMVD RASKLDLTVP EMTVLVGGLR ALDANAGHSR LGVLTNRPGT LSNDFFVNLL
DMSTQWTKSS SADGTYEGRD RKTGALKWTA SPVDLVFGSS SELRAVAEVY ASDDAHEKFV
RDFVQAWTKV MNLDRFDLKR S
