KATG3_MYCS2
ID KATG3_MYCS2 Reviewed; 744 AA.
AC A0QYP1; I7FN10;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Catalase-peroxidase 3 {ECO:0000255|HAMAP-Rule:MF_01961};
DE Short=CP 3 {ECO:0000255|HAMAP-Rule:MF_01961};
DE EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE AltName: Full=Peroxidase/catalase 3 {ECO:0000255|HAMAP-Rule:MF_01961};
GN Name=katG3 {ECO:0000255|HAMAP-Rule:MF_01961}; Synonyms=katG;
GN OrderedLocusNames=MSMEG_3729, MSMEI_3640;
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
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=ABK74103.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AFP40103.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; CP000480; ABK74103.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP001663; AFP40103.1; ALT_INIT; Genomic_DNA.
DR RefSeq; YP_888029.1; NC_008596.1.
DR AlphaFoldDB; A0QYP1; -.
DR SMR; A0QYP1; -.
DR STRING; 246196.MSMEI_3640; -.
DR PRIDE; A0QYP1; -.
DR EnsemblBacteria; ABK74103; ABK74103; MSMEG_3729.
DR EnsemblBacteria; AFP40103; AFP40103; MSMEI_3640.
DR KEGG; msg:MSMEI_3640; -.
DR KEGG; msm:MSMEG_3729; -.
DR PATRIC; fig|246196.19.peg.3673; -.
DR eggNOG; COG0376; Bacteria.
DR Proteomes; UP000000757; Chromosome.
DR Proteomes; UP000006158; 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..744
FT /note="Catalase-peroxidase 3"
FT /id="PRO_0000354840"
FT ACT_SITE 107
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 269
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 103
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 106..228
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 254)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 228..254
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 106)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 744 AA; 82295 MW; A980D38FD8FCBF8E CRC64;
MPESPDAYVN RTYDQTVAVR RSLKRRNSPA ASEDGLGWPR RLNLRILAQP CRTSSPLGED
FDYAKEFLSL DLDELARDID EVLTTSQDWW PADFGHYGPL VLRMAWHFAG TYRIGDGRGG
AGAGMLRFAP LNSFPDNRNL DKARRLLWPV KKKYGRKISW SDLMIFAGNR ALESMGCRTF
GFAGGREDAW EADETYWGPE STWLADERHS GVRDLDQPLA ASEMGLIYVD PQGPATLPDP
LASARDIRET FRRMGMNDEE TVALIAGGHT FGKSHGPTDP SRCLGPEPEG APLEALGLGW
VNSFGTGNGA DTVTSGLDGI WTATPTKWDM SFLTTLFAYE WDVALSPAGM WQWVPRNGAG
AGTVPDPYDP SRTHAPTMLT TDLALQEDPR YRVIALRFLE NPDEFADTFA RAWFKLTHID
MGPIQRYLGP LVPTERMIWQ DPVPHVDHEL ADADDVAALK REILGSGLSV SQLVTTAWAS
ASTFRNSDKR GGANGARIRL EPQRSWAVNE PEKLAIVLDR LERIRRRFND SHRGGKQISA
ADLIMLGGCA AVEHAAAEAG HPIEVPCRLG RTDAPQEWTD IEWFSALEPT ADAFRNYVGE
GNRPPPEHLL VDRASQLTLT APQMTVLLGG LRVLGANHGG SPLGVFTASP GALSNDFFVN
LLDVNIEWTP RADTADWTAA YEGRDRRTGE VTWIASRVDL SFASDPVLRA ISEVYASADA
EEKFVRDFVS AWDKVMNLDL FDRT
