KATG_GRABC
ID KATG_GRABC Reviewed; 760 AA.
AC Q0BRH7;
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 {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};
DE Flags: Precursor;
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961};
GN OrderedLocusNames=GbCGDNIH1_1677;
OS Granulibacter bethesdensis (strain ATCC BAA-1260 / CGDNIH1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Granulibacter.
OX NCBI_TaxID=391165;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1260 / CGDNIH1;
RX PubMed=17827295; DOI=10.1128/jb.00793-07;
RA Greenberg D.E., Porcella S.F., Zelazny A.M., Virtaneva K., Sturdevant D.E.,
RA Kupko J.J. III, Barbian K.D., Babar A., Dorward D.W., Holland S.M.;
RT "Genome sequence analysis of the emerging human pathogenic acetic acid
RT bacterium Granulibacter bethesdensis.";
RL J. Bacteriol. 189:8727-8736(2007).
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; CP000394; ABI62575.1; -; Genomic_DNA.
DR AlphaFoldDB; Q0BRH7; -.
DR SMR; Q0BRH7; -.
DR STRING; 391165.GbCGDNIH1_1677; -.
DR PeroxiBase; 7329; GbeCP01.
DR EnsemblBacteria; ABI62575; ABI62575; GbCGDNIH1_1677.
DR KEGG; gbe:GbCGDNIH1_1677; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_5; -.
DR OMA; EEIFWGP; -.
DR Proteomes; UP000001963; Chromosome.
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..45
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CHAIN 46..760
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354805"
FT ACT_SITE 125
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 286
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 121
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 124..245
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 271)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 245..271
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 124)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 760 AA; 83184 MW; 368607ECC3D2B891 CRC64;
MKGTPFRSPH LYQEGSSCMH RTIRSVAAVL TVVLSATIPM VPAWSDGEPR SIQFWWPDHL
DLSPLRQHAA ESDPLGANFN YIKAFQTLDL GAVKKDIAVL LKTPQDWWPA DYGNYGPFFI
RMAWHGAGTY RTYDGRGGAS GAQQRFEPLN SWPDNANLDK ARRLLWPIKK KYGEKLSWGD
LMVLTGNVAL ETMGFKTYGF AGGRTDDWEP DLIYWGSGAK FMSNNRDKNG KLEKPLAATQ
MGLIYVNPEG PNGVPDPVAA ARDIREAFGG MAMDDEETVA LIAGGHTFGK AHGAASPSKC
VGPAPAAAGI EEQGLGWKNK CGTGKGPDAI TSGLEGAWSA DPVNFTSQYL DNLFGFDWVL
TKSPGGAVQW KPKDASADQL VPDAFDASKR HPPMMFTTDI ALKTDPSYRK IALSFQKDPE
KFKAAFARAW FKLVHRDMGP RSRYFGPEVP KEDLLWQDPL PAITYKAVDE ADITDLKQKI
LASGLTVPEL VRTAWGSAAS FRGTDKRGGA NGARIRLAPE KDWPVNDPQE LKKVLDKLES
IQTAFNDGNH DGKKISLADL IVLGGNVGVE EAAKKAGYPV TVPFAPGRVD AVQAQTDVKS
FAVLEPTADG FRNYYASSNQ LSPAEMLVTR ASMLNLTVPE MTVLVGGMRV LDANEGHSQL
GVLTDHPGVL SNDFFVNLLD MSTKWSKAAD TAGVYEGHDR KTDALRWKGS TVDLIFGSNS
ELRAVAEVYA SDDAKEKFVR DFVAAWNKVM TLDRFDLQRQ
