KATG_HALS3
ID KATG_HALS3 Reviewed; 720 AA.
AC B0R9V8;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=OE_5186R;
OS Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1).
OG Plasmid PHS3.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=478009;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29341 / DSM 671 / R1;
RX PubMed=18313895; DOI=10.1016/j.ygeno.2008.01.001;
RA Pfeiffer F., Schuster S.C., Broicher A., Falb M., Palm P., Rodewald K.,
RA Ruepp A., Soppa J., Tittor J., Oesterhelt D.;
RT "Evolution in the laboratory: the genome of Halobacterium salinarum strain
RT R1 compared to that of strain NRC-1.";
RL Genomics 91:335-346(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; AM774418; CAP15539.1; -; Genomic_DNA.
DR RefSeq; WP_010904144.1; NC_010368.1.
DR AlphaFoldDB; B0R9V8; -.
DR SMR; B0R9V8; -.
DR EnsemblBacteria; CAP15539; CAP15539; OE_5186R.
DR GeneID; 5954764; -.
DR GeneID; 62888199; -.
DR KEGG; hsl:OE_5186R; -.
DR HOGENOM; CLU_025424_2_0_2; -.
DR OMA; MILAGNC; -.
DR PhylomeDB; B0R9V8; -.
DR Proteomes; UP000001321; Plasmid PHS3.
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 Plasmid.
FT CHAIN 1..720
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354966"
FT ACT_SITE 83
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 248
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 79
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 82..207
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 233)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 207..233
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 82)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 720 AA; 80477 MW; FB88823BCD3CB2F9 CRC64;
MENEDHNFGT SDWWPNQLDL EILDQNSQQV DPYGEDFDYA EAFEDLDLAA VKDDLEEMMT
DSKDWWPADY GHYGPLFIRM AWHSAGTYRT FDGRGGAAGG RQRLPPVDSW PDNVNLDKAR
RLLWPIKQKY GRKLSWGDLI ILAGNVALES MGFETYGFAG GRKDDYTPDE AVDWGPEDEW
ETTSGDRFDA DGSLKWPLGN TVMGLIYVNP EGPNGEPDLE GSAKNIRESF GKMAMNDKET
VALIAGGHTF GKVHGADDPE ENVGAEPAAA PIEKQGLGWE NEFGEGKGPD TITSGIEGPW
NTTPTQWDMS YVDNLLEYEW EPEKGPGGAW QWTTKSGELN ESAPGVQDPT DTEDVMMLTT
DVALKDDPDY REVLETFQEN PREFQQSFSK AWYKLIHRDM GPSERFLGPE VPEETMIWQD
PLPDADYDLV DDEAVAALKS ELLESELSIP QLVKTAWASA STYRDSDKRG GANGARIRLE
PQRSWEVNEP EQLEAALSTY EDIQAEFNDA RSDDMRVSLA DLIVLGGNAA IEQAAADAGY
DVDVPFEPGR TDATPEQTDV ESFEALKPKA DGFRNYLGDD AEREPEELLV DKAELLNLTA
DDMTVLVGGL RALGVTHGDS ELGIFTDQPG TLTNDFFTTL LDMDYEWEAA SEDREVFELR
DRETGDVEWT GSRVDLLFGS NTRLRAIAEV YGSDADEELF VQDFVDTWSE VMKLDRFDLE
