KATG1_HALMA
ID KATG1_HALMA Reviewed; 730 AA.
AC Q5V0S5;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Catalase-peroxidase 1 {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP 1 {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase 1 {ECO:0000255|HAMAP-Rule:MF_01961};
GN Name=katG1 {ECO:0000255|HAMAP-Rule:MF_01961}; OrderedLocusNames=rrnAC2018;
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809;
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
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; AY596297; AAV46878.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5V0S5; -.
DR SMR; Q5V0S5; -.
DR STRING; 272569.rrnAC2018; -.
DR PeroxiBase; 3064; HmaCP02.
DR EnsemblBacteria; AAV46878; AAV46878; rrnAC2018.
DR KEGG; hma:rrnAC2018; -.
DR PATRIC; fig|272569.17.peg.2672; -.
DR eggNOG; arCOG04487; Archaea.
DR HOGENOM; CLU_025424_2_0_2; -.
DR OMA; EEIFWGP; -.
DR Proteomes; UP000001169; Chromosome I.
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..730
FT /note="Catalase-peroxidase 1"
FT /id="PRO_0000354965"
FT ACT_SITE 93
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 258
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 89
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 92..217
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 243)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 217..243
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 92)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 730 AA; 81147 MW; 490649C67F89CCA4 CRC64;
MLKTVLMPSP SKCSLMAKRD QDWSPNQLRL DILDQNARDA DPRGTGFDYA EEFQELDLDA
VKADLEELMT SSQDWWPADY GHYGPLFIRM AWHSAGTYRT TDGRGGASGG RQRFAPLNSW
PDNANLDKAR RLLWPIKKKY GRKLSWADLI VLAGNHAIES MGLKTFGWAG GREDAFEPDE
AVDWGPEDEM EAHQSERRTD DGELKEPLGA AVMGLIYVDP EGPNGNPDPL ASAENIRESF
GRMAMNDEET AALIAGGHTF GKVHGADDPE ENLGDVPEDA PIEQMGLGWE NDYGSGKAGD
TITSGIEGPW TQAPIEWDNG YIDNLLDYEW EPEKGPGGAW QWTPTDEALA NTVPDAHDPS
EKQTPMMLTT DIALKRDPDY REVMERFQEN PMEFGINFAR AWYKLIHRDM GPPERFLGPD
APDEEMIWQD PVPDVDHDLI GDEEVAELKT DILETDLTVS QLVKTAWASA STYRDSDKRG
GANGARIRLE PQKNWEVNEP AQLETVLATL EEIQAEFNSA RTDDTRVSLA DLIVLGGNAA
VEQAAADAGY DVTVPFEPGR TDATPEQTDV DSFEALKPRA DGFRNYARDD VDVPAEELLV
DRADLLDLTP EEMTVLVGGL RSLGATYQDS DLGVFTDEPG TLTNDFFEVV LGMDTEWEPV
SESKDVFEGY DRETGEQTWA ASRVDLIFGS HSRLRAIAEV YGADGAEAEL VDDFVDAWHK
VMRLDRFDLE
