KATG_METB6
ID KATG_METB6 Reviewed; 733 AA.
AC A7I6W6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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=Mboo_0959;
OS Methanoregula boonei (strain DSM 21154 / JCM 14090 / 6A8).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanoregulaceae; Methanoregula.
OX NCBI_TaxID=456442;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21154 / JCM 14090 / 6A8;
RX PubMed=25998264; DOI=10.1099/mic.0.000117;
RA Braeuer S., Cadillo-Quiroz H., Kyrpides N., Woyke T., Goodwin L.,
RA Detter C., Podell S., Yavitt J.B., Zinder S.H.;
RT "Genome of Methanoregula boonei 6A8 reveals adaptations to oligotrophic
RT peatland environments.";
RL Microbiology 161:1572-1581(2015).
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; CP000780; ABS55477.1; -; Genomic_DNA.
DR RefSeq; WP_012106502.1; NC_009712.1.
DR AlphaFoldDB; A7I6W6; -.
DR SMR; A7I6W6; -.
DR STRING; 456442.Mboo_0959; -.
DR PeroxiBase; 6985; CMbCP01.
DR EnsemblBacteria; ABS55477; ABS55477; Mboo_0959.
DR GeneID; 5412136; -.
DR KEGG; mbn:Mboo_0959; -.
DR eggNOG; arCOG04487; Archaea.
DR HOGENOM; CLU_025424_2_0_2; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 2839at2157; -.
DR Proteomes; UP000002408; 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; 2.
PE 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome.
FT CHAIN 1..733
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354967"
FT REGION 1..24
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 733 AA; 80523 MW; 907E15C2961F1BAC CRC64;
MTDDSTCPVT GGADKQVTGR GQSYRDWWPN QPNLRVLSQH SPRSNPMGGE FNYAEEFKKL
DFAAVKADLR ALMTSSQEWW PADFGHYGPL FIRMAWHSAG TYRTLDGRGG AGSGQQRFPP
LNSWPDNVNL DKARRLLWPI KKKYGRKISW ADLMILAGNV ALESMGFETF GFAGGRVDTW
EPDEDVYWGS ENTWLGDKRY SGDRKLENPL AAVQMGLIYV NPEGPNGKPD PVAAAKDIRE
TFARMAMNDE ETVALIAGGH SFGKTHGAGP ASHVGPEPEA APIEQQGLGW KSSFGTGKGG
DAIGSGLEVT WTSTPTKWSN NFFRILFSYE WELTKSPAGA YQWQPKDGAG AGTIPDAHDK
NKRRAPTMLT TDLSLRFDPV YEKISRHFYE NPDQLADAFA RAWFKLTHRD MGPRTRYLGP
EVPKEALIWQ DPIPAVNHTL IGPREITFLK RKILASGLSI PELVLTAWAS ASTFRGSDKR
GGANGARIRL APQKDWEVNE PARLRKVLAV LEGIQQEFNK TATGGKKVSL ADLIVLAGCA
GVWKAAKNGG HKVTVPFTPG RMDATQEQTD VNSFAVLEPK ADGFRNYLKG PYAVSAEELL
VDKAQLLTLS APEMTVLIGG LRVIGATYGQ ATHGVFTTLP GALTNDFFTH LLDMGTEWKP
VAGNPDVFEG SDRKTGEPKW TGTRVDLIFG ANAQLRAIAE VYASADGEEK FAQDFVAAWA
KVMNLDRFDL AQK
