KATG_ECOSM
ID KATG_ECOSM Reviewed; 726 AA.
AC B1LNQ3;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 76.
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};
GN OrderedLocusNames=EcSMS35_4390;
OS Escherichia coli (strain SMS-3-5 / SECEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=439855;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SMS-3-5 / SECEC;
RX PubMed=18708504; DOI=10.1128/jb.00661-08;
RA Fricke W.F., Wright M.S., Lindell A.H., Harkins D.M., Baker-Austin C.,
RA Ravel J., Stepanauskas R.;
RT "Insights into the environmental resistance gene pool from the genome
RT sequence of the multidrug-resistant environmental isolate Escherichia coli
RT SMS-3-5.";
RL J. Bacteriol. 190:6779-6794(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; CP000970; ACB18624.1; -; Genomic_DNA.
DR RefSeq; WP_001296626.1; NC_010498.1.
DR AlphaFoldDB; B1LNQ3; -.
DR SMR; B1LNQ3; -.
DR EnsemblBacteria; ACB18624; ACB18624; EcSMS35_4390.
DR KEGG; ecm:EcSMS35_4390; -.
DR HOGENOM; CLU_025424_2_0_6; -.
DR OMA; MILAGNC; -.
DR Proteomes; UP000007011; 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.
FT CHAIN 1..726
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354778"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 106
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 267
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 102
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 105..226
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 252)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 226..252
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 105)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 726 AA; 80026 MW; A2D7A96D86681DC2 CRC64;
MSTSDDIHNT TATGKCPFHQ GGHDQSAGGG TTTRDWWPNQ LRVDLLNQHS NRSNPLGEDF
DYRKEFSKLD YYGLKKDLKA LLTESQPWWP ADWGSYAGLF IRMAWHGAGT YRSIDGRGGA
GRGQQRFAPL NSWPDNVSLD KARRLLWPIK QKYGQKISWA DLFILAGNVA LENSGFRTFG
FGAGREDVWE PDLDVNWGDE KAWLTHRHPE ALAKAPLGAT EMGLIYVNPE GPDHSGEPLS
AAAAIRATFG NMGMNDEETV ALIAGGHTLG KTHGAGPTSN VGPDPEAAPI EEQGLGWAST
YGSGVGADAI TSGLEVVWTQ TPTQWSNYFF ENLFKYEWVQ TRSPAGAIQF EAVDAPEIIP
DPFDPSKKRK PTMLVTDLTL RFDPEFEKIS RRFLNDPQAF NEAFARAWFK LTHRDMGPKS
RYIGPEVPKE DLIWQDPLPQ PIYNPTEQDI IDLKFAIADS GLSVSELVSV AWASASTFRG
GDKRGGANGA RLALMPQRDW DVNAAAVRAL PVLEKIQKES GKASLADIIV LAGVVGVEKA
ASAAGLSIHV PFAPGRVDAR QDQTDIEMFE LLEPIADGFR NYRARLDVST TESLLIDKAQ
QLTLTAPEMT ALVGGMRVLG ANFDGSKNGV FTDRVGVLSN DFFVNLLDMR YEWKATDESK
ELFEGRDRET GEVKYTASRA DLVFGSNSVL RAVAEVYASS DAHEKFVKDF VAAWVKVMNL
DRFDLL
