KATG_METI4
ID KATG_METI4 Reviewed; 726 AA.
AC B3E099;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
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=Minf_2274;
OS Methylacidiphilum infernorum (isolate V4) (Methylokorus infernorum (strain
OS V4)).
OC Bacteria; Verrucomicrobia; Methylacidiphilae; Methylacidiphilales;
OC Methylacidiphilaceae; Methylacidiphilum.
OX NCBI_TaxID=481448;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate V4;
RX PubMed=18593465; DOI=10.1186/1745-6150-3-26;
RA Hou S., Makarova K.S., Saw J.H., Senin P., Ly B.V., Zhou Z., Ren Y.,
RA Wang J., Galperin M.Y., Omelchenko M.V., Wolf Y.I., Yutin N., Koonin E.V.,
RA Stott M.B., Mountain B.W., Crowe M.A., Smirnova A.V., Dunfield P.F.,
RA Feng L., Wang L., Alam M.;
RT "Complete genome sequence of the extremely acidophilic methanotroph isolate
RT V4, Methylacidiphilum infernorum, a representative of the bacterial phylum
RT Verrucomicrobia.";
RL Biol. Direct 3:26-26(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; CP000975; ACD84328.1; -; Genomic_DNA.
DR RefSeq; WP_012464608.1; NC_010794.1.
DR AlphaFoldDB; B3E099; -.
DR SMR; B3E099; -.
DR STRING; 481448.Minf_2274; -.
DR EnsemblBacteria; ACD84328; ACD84328; Minf_2274.
DR KEGG; min:Minf_2274; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_0; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000009149; 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.
FT CHAIN 1..726
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354831"
FT REGION 471..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 94
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 257
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 90
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 93..216
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 242)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 216..242
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 93)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 726 AA; 80954 MW; 5DDBE77260C22A3B CRC64;
MTTEGSCPFH HTAAIGGLKT NEEWWPNRLN LKILRQNSPL SNPMGAGFNY AKEFCSLDLS
ALKEDLRRLM TDSQQWWPAD FGHYGPLFIR MAWHSAGTYR VHDGRGGAGS GQQRFAPLNS
WPDNVLLDKA RRLLWPIKQK YGRKISWADL IILAGNVALE SMGLKTFGFG GGRVDSWEPD
ESVYWGVEQK WLEDKRYSGK RDLEQPLAAV QMGLIYVNPE GPNGNPDPVA AAVDIRETFT
RMGMNDAETV ALIAGGHTFG KAHGAGPASF VGPEPEAAGI AEQGLGWRSS YRSGKGADAI
GSGLEVIWTR TPTRWNNDYF QFLFEYEWEP TKSPAGAWQW VAKDAPEIVP DPFDPAKKRK
PTMLTTDLSL RFDPVYEKIA RAYYEQPDLF ADAFARAWFK LTHRDMGPRS RYLGPEVPKE
DLLWQDPIPP VDHPLIETDD MNSLKAKILE SGLTVRELVF TAWSSASTFR GSDKRGGANG
ARIRLSPQKD WPANEPTQLA RVLAVLEQIQ KEFNARSPKK VSMADLIVLG GCAGVEQAAR
NGGRSVVVPF IPGRSDALEE QTDVESFAFL EPWADGFRNF YKKGCSVPQE ALLVDKAQLL
TLTAPEMTVL VGGMRVLDAN VGRSRHGVFT DRPGALTNDF FVNLLDMDTE WKPVDEREEL
FEGRDRKTGT LLWTATRVDL IFGSNSELRA ISEVYGAADA QDKFVKDFIS AWNKVMNLDR
FDLAPA
