KATG_NATPD
ID KATG_NATPD Reviewed; 713 AA.
AC Q3IQZ9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 08-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=NP_2708A;
OS Natronomonas pharaonis (strain ATCC 35678 / DSM 2160 / CIP 103997 / JCM
OS 8858 / NBRC 14720 / NCIMB 2260 / Gabara) (Halobacterium pharaonis).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Natronomonas.
OX NCBI_TaxID=348780;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35678 / DSM 2160 / CIP 103997 / JCM 8858 / NBRC 14720 / NCIMB
RC 2260 / Gabara;
RX PubMed=16169924; DOI=10.1101/gr.3952905;
RA Falb M., Pfeiffer F., Palm P., Rodewald K., Hickmann V., Tittor J.,
RA Oesterhelt D.;
RT "Living with two extremes: conclusions from the genome sequence of
RT Natronomonas pharaonis.";
RL Genome Res. 15:1336-1343(2005).
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; CR936257; CAI49445.1; -; Genomic_DNA.
DR RefSeq; WP_011323070.1; NC_007426.1.
DR AlphaFoldDB; Q3IQZ9; -.
DR SMR; Q3IQZ9; -.
DR STRING; 348780.NP_2708A; -.
DR PeroxiBase; 2515; NpCP01.
DR EnsemblBacteria; CAI49445; CAI49445; NP_2708A.
DR GeneID; 3703016; -.
DR KEGG; nph:NP_2708A; -.
DR eggNOG; arCOG04487; Archaea.
DR HOGENOM; CLU_025424_2_0_2; -.
DR OrthoDB; 2839at2157; -.
DR Proteomes; UP000002698; 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.
FT CHAIN 1..713
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354970"
FT ACT_SITE 78
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 74
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 77..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 77)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 713 AA; 79455 MW; 90FA3F659414A865 CRC64;
MSIDYKKLWP EALDFESLDQ NAQHVDPKDE DFDYAEAFQE LDLEEVKQDI ESVMTDSQEW
WPADYGHYGP LFIRMAWHSA GTYRTTDGRG GASGGYQRLP PVDSWPDNAN LDKARRVLWP
VKQKYGQNLS WADLIVLAGN VALESMGFET FGFAGGREDD FAPDESVDWG PEEEMEASDR
YDEAGELPEP LGATVMGLIY VNPEGPDGEP DLEGSAANIR ESFGRMAMND EETVALIAGG
HTFGKVHGAD DPDEHVGGPP ADAPIDLQGL GWENDFGEGK GPDTITSGIE GPWNTTPTQW
DMSYIDNLLD YEWWPEKGPG GAWQWTTESG ELDAAAPSVD GSSEKEDVMM LTTDVALKRD
PDYREVLERF QENPDEFQEA FAKAWYKLIH RDMGPPERFL GPEVPEETLI WQDPLPDADY
DSIGDEEVAE LKEALLDSEL SVAQLVKTAW ASASTYRDSD KRGGANGARI RLEPQRSWEV
NEPAALADAL ETYEAIQEEF NSARSDAVRV SLADLIVLGG NAAVEQAAAD AGYDVTVPFE
PGRTDATPEQ TDVESFEALK PKADGFRNYL SDEAERKPEE LLVDKADLLN LTPPEMTVLV
GGMRALGATY QDTDRGVFTD EPGTLTNDFF VNILDMDYEW EPVSEDREVF ELRDRETGEV
EWEGTRFDLI FGSDSRLRAI SEVYGADDGE AEFVEDFVDT WSKVMKLDRF DLE
