KATG2_BURCJ
ID KATG2_BURCJ Reviewed; 736 AA.
AC Q4F6N6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 98.
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}; Synonyms=katA;
GN OrderedLocusNames=BceJ2315_55450; ORFNames=BCAM2107;
OS Burkholderia cenocepacia (strain ATCC BAA-245 / DSM 16553 / LMG 16656 /
OS NCTC 13227 / J2315 / CF5610) (Burkholderia cepacia (strain J2315)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=216591;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
RX PubMed=17371508; DOI=10.1111/j.1574-695x.2007.00224.x;
RA Charalabous P., Risk J.M., Jenkins R., Birss A.J., Hart C.A., Smalley J.W.;
RT "Characterization of a bifunctional catalase-peroxidase of Burkholderia
RT cenocepacia.";
RL FEMS Immunol. Med. Microbiol. 50:37-44(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-245 / DSM 16553 / LMG 16656 / NCTC 13227 / J2315 / CF5610;
RX PubMed=18931103; DOI=10.1128/jb.01230-08;
RA Holden M.T., Seth-Smith H.M., Crossman L.C., Sebaihia M., Bentley S.D.,
RA Cerdeno-Tarraga A.M., Thomson N.R., Bason N., Quail M.A., Sharp S.,
RA Cherevach I., Churcher C., Goodhead I., Hauser H., Holroyd N., Mungall K.,
RA Scott P., Walker D., White B., Rose H., Iversen P., Mil-Homens D.,
RA Rocha E.P., Fialho A.M., Baldwin A., Dowson C., Barrell B.G., Govan J.R.,
RA Vandamme P., Hart C.A., Mahenthiralingam E., Parkhill J.;
RT "The genome of Burkholderia cenocepacia J2315, an epidemic pathogen of
RT cystic fibrosis patients.";
RL J. Bacteriol. 191:261-277(2009).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. Shows peroxidase specificity towards odianisidine,
CC ABTS and pyrogallol, but methoxyphenol and 2-chloronaphthol are not
CC peroxidized. {ECO:0000255|HAMAP-Rule:MF_01961,
CC ECO:0000269|PubMed:17371508}.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5 for the peroxidase reaction and 6.0 for the
CC catalase reaction. Active from pH 5.5 to 8.5.
CC {ECO:0000269|PubMed:17371508};
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; DQ112341; AAZ14051.1; -; Genomic_DNA.
DR EMBL; AM747721; CAR55964.1; -; Genomic_DNA.
DR RefSeq; WP_006490370.1; NC_011001.1.
DR AlphaFoldDB; Q4F6N6; -.
DR SMR; Q4F6N6; -.
DR STRING; 216591.BCAM2107; -.
DR PeroxiBase; 2309; BcenCP01_J2315.
DR EnsemblBacteria; CAR55964; CAR55964; BCAM2107.
DR KEGG; bcj:BCAM2107; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_4; -.
DR OMA; KWTATRM; -.
DR OrthoDB; 49441at2; -.
DR BioCyc; BCEN216591:G1G1V-6173-MON; -.
DR BRENDA; 1.11.1.6; 8982.
DR Proteomes; UP000001035; 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 1: Evidence at protein level;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT CHAIN 1..736
FT /note="Catalase-peroxidase 2"
FT /id="PRO_0000354740"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 268
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 88
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 91..227
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 253)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 227..253
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 91)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 736 AA; 80487 MW; 48CC314FEA9C30A3 CRC64;
MSNEGQCPFN HANGGGTTNR DWWPNELRLD LLSQHSSKTD PLDPGFNYAE AFNSLDLDAL
RKDLAALMTD SQDWWPADFG HYGPLFVRMA WHSAGTYRMG DGRGGAGRGQ QRFAPLNSWP
DNVSLDKARR LLWPIKQKYG QKISWADLLI LTGDVALTTM GFKTFGYAGG REDTWEPDRD
VYWGSETTWL GGDLRYDKGG ACESQHGGNA GRNLENPLAA VQMGLIYVNP EGPDGNPDPV
AAAYDIREVF GRMAMNDEET VALIAGGHAF GKTHGAGPAD NVGLEPEAAG LEQQGLGWKN
SFGTGKGADT ITSGLEVTWS DTPTQWGMGF FKNLFGYEWE LTKSPAGAHQ WVAKNAEPTI
PHAHDPSKKL LPTMLTTDLS LRFDPVYEKI SRHFMDNPDV FADAFARAWF KLTHRDMGPR
ARYLGPDVPT EELIWQDPIP AVDHVLVDDT DVAPLKETIL ASGLSVAELV STAWASASTF
RGSDKRGGAN GARIRLAPQK DWAVNEPARL AKVLKVLERI QGEFNSTQPG GKKISLADLI
VLAGGAGIEQ AAKRAGHDVV VPFAPGRMDA SQEQTDAHSF AVLEPVADGF RNFVKGKFAV
PAEALLIDKA QLLTLTAPQM TALVGGLRVL NVQTGDEKHG VFTDQPETLT VDFFRNLLDM
ATEWKPIAGE DTYEGRDRRT GELKWTGTRV DLVFGSNAVL RALSEVYASA DGEAKFIRDF
VAAWVKVMNL DRFDLA
