KATG1_MYCFO
ID KATG1_MYCFO Reviewed; 752 AA.
AC O08404;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 97.
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}; Synonyms=katGI;
OS Mycolicibacterium fortuitum (Mycobacterium fortuitum).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1766;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 6841 / DSM 46621 / CIP 104534 / JCM 6387 / KCTC 9510 / NBRC
RC 13159 / NCTC 10394;
RX PubMed=9371430; DOI=10.1128/jb.179.22.6880-6886.1997;
RA Menendez M.C., Ainsa J.A., Martin C., Garcia M.J.;
RT "katGI and katGII encode two different catalases-peroxidases in
RT Mycobacterium fortuitum.";
RL J. Bacteriol. 179:6880-6886(1997).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. May play a role in the intracellular survival of
CC mycobacteria (By similarity). {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 Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.;
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; Y07865; CAA69192.1; -; Genomic_DNA.
DR AlphaFoldDB; O08404; -.
DR SMR; O08404; -.
DR STRING; 1766.XA26_32250; -.
DR PeroxiBase; 2396; MfoCP01.
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.
FT CHAIN 1..752
FT /note="Catalase-peroxidase 1"
FT /id="PRO_0000055572"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..32
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 117
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 285
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 113
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 116..244
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 270)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 244..270
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 116)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 752 AA; 83101 MW; B66BAD53DD26E70D CRC64;
MPPNTPDASD ARPPQADTET HSHSESENPV IESPKPKAHA PLTNQDWWPD QVDVSRLHKQ
PIEGNPLGAG FNYAEEFQKL DVEALRADML ELMTSSQDWW PRDYGTYAGL FIRMSWHAAG
TYRIFDGRGG AGQGAQRFAP INSWPDNVSL DKARRLLWPI KQKYGNKISW ADLIIFAGNV
ALESAGFKTF GFAFGRQDIW EPEEILWGQE DTWLGTDKRY GGTNDSTNRE LANPYGATTM
GLIYVNPEGP EGKPDPLAAA HDIRETFGRM AMNDEETAAL IVGGHTLGKT HGPGPGDLVG
PEPEAAPIEQ QGLGWKCAFG SGKGSDTITS GLEVVWTTTP TKWSNSYLEI LYGYEWELTK
SPGDAWQFEA KDAEAIIPDP FGGPPRKPTM LVTDISMRVD PIYGPITRRW LEHPEELNEA
FAKAWYKLLH RDMGPISRYL GPWIPEPQLW QDPVPDVDHP LVDEQDIAAL KEKLLDSGLS
VQQLVKTAWS AAASFRGTDK RGGANGGRLR LQPQRNWEVN EPSELDKALP VLERIAQDFN
ASASDGKKIS LADLIVLGGS AAIEKAARDG GYEVKVHFVA GRTDASQENT DVDSFAVLEP
RADGFRNFVR PGDKAPLEQL LVDKAYFLNL TAPEMTVLVG GLRALNTNHG GSKHGVFTAN
PGALSNDFFV NLLDMSTEWK PSETAENVYE GRDRRTGQTR WTATANDLVF GSNSVLRAVA
EVYAQEDNKA KMIEDFVAAW VKVMNNDRFD LD
