KATG_PARXL
ID KATG_PARXL Reviewed; 753 AA.
AC Q13US7;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=Bxeno_A3624;
GN ORFNames=Bxe_A0772;
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400;
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000270; ABE32162.1; -; Genomic_DNA.
DR RefSeq; WP_011489662.1; NZ_CP008760.1.
DR AlphaFoldDB; Q13US7; -.
DR SMR; Q13US7; -.
DR STRING; 266265.Bxe_A0772; -.
DR PeroxiBase; 2290; BxCP01.
DR EnsemblBacteria; ABE32162; ABE32162; Bxe_A0772.
DR KEGG; bxb:DR64_2939; -.
DR KEGG; bxe:Bxe_A0772; -.
DR PATRIC; fig|266265.5.peg.3819; -.
DR eggNOG; COG0376; Bacteria.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000001817; Chromosome 1.
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.
FT CHAIN 1..753
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354753"
FT ACT_SITE 92
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 284
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..243
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 269)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 243..269
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 91)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 753 AA; 82467 MW; 22250FE21A9D110F CRC64;
MSSEAKCPFN HAAGGGTTNR DWWPKQLRLD LLSQHSGKSN PLDGGFNYAE AFRSLDLAAV
KKDLAALMTD SQDWWPADFG HYGPLFIRMA WHSAGTYRIG DGRGGAGRGQ QRFAPLNSWP
DNVSLDKARR LLWPIKQKYG QKISWADLLI LTGNVALETM GFKTFGFAGG REDTWEPDLD
VYWGNEKTWL GGDVRYGKGA AGDNDDGGVI VADEEKHGEE VSRDNSGRNL ENPLGAVQMG
LIYVNPEGPD GNPDPLAAAH DIRETFARMA MNDEETVALI AGGHTFGKTH GAGPADNVGP
EPEAADLENQ GLGWKNSFGT GKGADTITSG LEVTWTTTPT KWGNGFFENL FKYEWELTKS
PAGAHQWVAR DAGETIPHAH DPSKKLRPTM LTTDLSLRFD PVYEKISRRF LENPDQLADA
FARAWFKLTH RDMGPRARYL GPEVPAEELN WQDPIPALDH PLVNEQDIAS LKQKILASGL
SVSQLVSTAW ASASTFRGSD KRGGANGARI RLAPQKDWPV NQPEQLAKVL KVLEGIQSEF
NGVQSGGKKI SLADLIVLGG AAAIEQAAKS AGQQVSVPFS PGRMDASQEQ TDVQSVAALE
PLADGFRNYL KGKYRAPAEA LLIDKAQLLT LTAPEMTVLL GGLRALNVHA GQDSHGVFTH
RPQTLSNDFF RNLLDMGTEW KPLSPARDVF EGRDRKTGEL KWTGTRVDLV FGSHAQLRAL
CEVYASEDAQ EKFVRDFVAA WAKVMDLDRF EIA
