KATG_AERS4
ID KATG_AERS4 Reviewed; 699 AA.
AC A4SS04;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=ASA_3715;
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449;
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(2008).
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; CP000644; ABO91676.1; -; Genomic_DNA.
DR RefSeq; WP_005316054.1; NC_009348.1.
DR AlphaFoldDB; A4SS04; -.
DR SMR; A4SS04; -.
DR STRING; 382245.ASA_3715; -.
DR EnsemblBacteria; ABO91676; ABO91676; ASA_3715.
DR KEGG; asa:ASA_3715; -.
DR PATRIC; fig|382245.13.peg.3690; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000000225; 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 PANTHER; PTHR30555; PTHR30555; 2.
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; PS00436; PEROXIDASE_2; 1.
DR PROSITE; PS50873; PEROXIDASE_4; 1.
PE 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.
FT CHAIN 1..699
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354714"
FT ACT_SITE 73
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 241
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 69
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 72..200
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 226)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 200..226
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 72)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 699 AA; 77263 MW; 5B05B9F09887CBAE CRC64;
MSNNSERSQG KCPVMHGGTT SGEQANMAWW PKSLNLDMAA LKQDVTALMT DSQDWWPADW
GHYGALMIRM AWHSAGTYRI ADGRGGGSTG NQRFAPLNSW PDNANLDKAR RLLWPIKKKY
GNKISWADLI ILAGTVAYES MGLKTFGFAF GREDIWHPEK DIYWGAEKEW LAPSSKPGGR
YSGERDLDNP LAAVMMGLIY VNPEGVDGNP DPLKTAKDMR VTFARMAMDD EETVALTAGG
HTVGKCHGNG DARLLGPEPE GAAVEDQGLG WLNKTQRGIG RNAVTSGIEG AWTTHPTRWD
NGYFYLLFNY EWELKKSPAG AWQWEPVNIR EEDKPVDVED PAIRHNPIMT DADMALKFDP
EYRKIAERFR ADPAAFSDAF ARAWFKLTHR DLGPKTRYVG PYVPAEDLIW QDPVPAGRTD
YDVAAVKASI AASGLSISDM VSTAWDSART FRGSDLRGGA NGARIRLAPQ NEWEGNEPAR
LARVLKVLEP IAAASQISVA DVIVLAGNLG VELAARAAGV EVTVPFSPGR GDASQARTDV
ASFDVLEPLA DGYRNWLKKD YAVTAEELML DRTQLMGLTA HEMTVLVGGM RVLGTNHGGT
RHGVFTEREG ALTNDYFVNL TDMANTWHPS GDRLYEVRDR KSGKVKWTAT RIDLVFGSNS
VLRAYAEVYA QDDNKEKFVC DFISAWNKVM NADRFDLMS
