KATG_METHJ
ID KATG_METHJ Reviewed; 732 AA.
AC Q2FSF4;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 80.
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=Mhun_2433;
OS Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS JF-1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX NCBI_TaxID=323259;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL Stand. Genomic Sci. 11:2-2(2016).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABD42134.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000254; ABD42134.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_048067526.1; NC_007796.1.
DR AlphaFoldDB; Q2FSF4; -.
DR SMR; Q2FSF4; -.
DR STRING; 323259.Mhun_2433; -.
DR PeroxiBase; 2516; MhCP01.
DR EnsemblBacteria; ABD42134; ABD42134; Mhun_2433.
DR GeneID; 3922420; -.
DR KEGG; mhu:Mhun_2433; -.
DR eggNOG; arCOG04487; Archaea.
DR HOGENOM; CLU_025424_2_0_2; -.
DR OrthoDB; 2839at2157; -.
DR Proteomes; UP000001941; 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..732
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354969"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 97
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 260
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 93
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 96..219
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 245)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 219..245
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 96)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 732 AA; 81574 MW; 38D461A2F30AC8CE CRC64;
MADNKKSPET GGITMQIPGK GRTNRDWWPD QLNLKILSQN SPLSNPLGQK FNYRVEFSKL
DLAAVKQDLR DLMTSSQDWW PADFGHYGPL FIRMAWHSAG TYRTFDGRGG ASGGEQRFPP
LNSWPDNVNL DKARRLLWPI KQKYGQKISW ADLMILAGNV ALESMGFKTF GFGGGREDVW
EPQEDTYWGS EDTWLGDKRY SGDRELEKPL AAVQMGLIYV NPEGPDGNPD PVAAARDIRE
VFARMAMNDE ETVALIAGGH AFGKTHGAGP ASHLGPEPEA AGIEEQGLGW KNSFGTGKGN
DTITSGIEIT WTPTPTKWSN NFFRVLFSYE WELTKSPAGA YQWKPKGEAG AGTVPDPHDP
KKRHAPGMLT TDLALRFDPI YEKISRRFYE NPELFADAFA RAWFKLTHRD MGPKTRYLGP
EVPDEDLIWQ DPIPAINHPL IDDQDIALLK SRILASGLSI SRLVYTAWAA ASTFRGSDKR
GGANGARIRL DPQKNWEVNE PEELANVLKI LEGIQHEFNQ NAPGGKRVSL ADLIVLGGCA
GIEQAAKNAG YSVTVPFTPG RMDAVQEQTD AASFAVLEPM ADGFRNYAKR HLPMKPEAML
IDKAQLLMLT APEMTVLIGG MRVLNTNFGQ TKHGVFTDKP ETLTNDYFVH LLDMGTEWTP
VSETEDLYEG RDRRTGEIRW TGTRVDLIFG SNSQLRALAE VYACSDGKDK FIQDFVAAWA
KVMNLDRFDR IQ
