ID   KATG2_MYCS2             Reviewed;         748 AA.
AC   A0QXX7; I7FMA5; Q93JZ3; Q9R4J9;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Catalase-peroxidase 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE            Short=CP 2 {ECO:0000255|HAMAP-Rule:MF_01961};
DE            EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
DE   AltName: Full=Peroxidase/catalase 2 {ECO:0000255|HAMAP-Rule:MF_01961};
GN   Name=katG2 {ECO:0000255|HAMAP-Rule:MF_01961}; Synonyms=katH;
GN   OrderedLocusNames=MSMEG_3461, MSMEI_3380;
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 [GENOMIC DNA].
RA   Honore N.;
RT   "The catalase-peroxidase of Mycobacterium smegmatis.";
RL   Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR METHIONINE.
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).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-20, BIOPHYSICOCHEMICAL PROPERTIES, HEME-BINDING,
RP   SUBUNIT, MASS SPECTROMETRY, AND DISRUPTION PHENOTYPE.
RX   PubMed=7673210; DOI=10.1074/jbc.270.38.22290;
RA   Marcinkeviciene J.A., Magliozzo R.S., Blanchard J.S.;
RT   "Purification and characterization of the Mycobacterium smegmatis catalase-
RT   peroxidase involved in isoniazid activation.";
RL   J. Biol. Chem. 270:22290-22295(1995).
CC   -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC       peroxidase activity. May play a role in the intracellular survival of
CC       mycobacteria.
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 2 heme B (iron-protoporphyrin IX) groups per tetramer.;
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1.4 mM for H(2)O(2) for the catalase reaction
CC         {ECO:0000269|PubMed:7673210};
CC         KM=0.19 mM for o-dianisidine for the peroxidase reaction
CC         {ECO:0000269|PubMed:7673210};
CC         KM=0.17 mM for NADPH for the peroxidase reaction
CC         {ECO:0000269|PubMed:7673210};
CC         KM=0.23 mM for NADH for the peroxidase reaction
CC         {ECO:0000269|PubMed:7673210};
CC         KM=0.31 mM for pyrogallol for the peroxidase reaction
CC         {ECO:0000269|PubMed:7673210};
CC         KM=0.11 mM for 2,2'-azino-bis-(3-ethylbenzthiazoline-6-sulfonic acid)
CC         for the peroxidase reaction {ECO:0000269|PubMed:7673210};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:7673210}.
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   -!- MASS SPECTROMETRY: Mass=81889; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:7673210};
CC   -!- DISRUPTION PHENOTYPE: Defects cause isoniazid (INH) resistance.
CC       {ECO:0000269|PubMed:7673210}.
CC   -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
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DR   EMBL; AJ311851; CAC44462.1; -; Genomic_DNA.
DR   EMBL; CP000480; ABK73887.1; -; Genomic_DNA.
DR   EMBL; CP001663; AFP39843.1; -; Genomic_DNA.
DR   RefSeq; WP_011729086.1; NZ_SIJM01000039.1.
DR   RefSeq; YP_887765.1; NC_008596.1.
DR   AlphaFoldDB; A0QXX7; -.
DR   SMR; A0QXX7; -.
DR   STRING; 246196.MSMEI_3380; -.
DR   PeroxiBase; 3570; MsmCP02_mc2155.
DR   PRIDE; A0QXX7; -.
DR   EnsemblBacteria; ABK73887; ABK73887; MSMEG_3461.
DR   EnsemblBacteria; AFP39843; AFP39843; MSMEI_3380.
DR   GeneID; 66734854; -.
DR   KEGG; msg:MSMEI_3380; -.
DR   KEGG; msm:MSMEG_3461; -.
DR   PATRIC; fig|246196.19.peg.3418; -.
DR   eggNOG; COG0376; Bacteria.
DR   OMA; EEIFWGP; -.
DR   OrthoDB; 49441at2; -.
DR   SABIO-RK; A0QXX7; -.
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   1: Evidence at protein level;
KW   Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW   Oxidoreductase; Peroxidase; Reference proteome.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:18955433,
FT                   ECO:0000269|PubMed:7673210"
FT   CHAIN           2..748
FT                   /note="Catalase-peroxidase 2"
FT                   /id="PRO_0000345094"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..28
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        114
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   BINDING         279
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            110
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        113..238
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   264)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        238..264
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   113)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ   SEQUENCE   748 AA;  81998 MW;  73E44205C96B2FD3 CRC64;
     MSSDTSDSRP PNPDTKTAST SESENPAIPS PKPKSGAPLR NQDWWPNQID VSRLHPHPPQ
     GNPLGEDFDY AEEFAKLDVN ALKADLTALM TQSQDWWPAD YGHYGGLFIR MSWHSAGTYR
     IHDGRGGGGQ GAQRFAPINS WPDNVSLDKA RRLLWPIKQK YGNKISWADL LVFTGNVALE
     SMGFKTFGFG FGREDIWEPE EILFGEEDEW LGTDKRYGGG EQRQLAEPYG ATTMGLIYVN
     PEGPEGQPDP LAAAHDIRET FGRMAMNDEE TAALIVGGHT FGKTHGAGDA SLVGPEPEAA
     PIEQQGLGWK SSYGTGKGPD TITSGLEVVW TNTPTKWDNS FLEILYGYEW ELTKSPAGAW
     QFTAKDGAGA GTIPDPFGGP GRNPTMLVTD ISMRVDPIYG KITRRWLDHP EELSEAFAKA
     WYKLLHRDMG PISRYLGPWV AEPQLWQDPV PAVDHPLVDD QDIAALKSTV LDSGLSTGQL
     IKTAWASAAS YRNTDKRGGA NGARVRLEPQ KNWDVNEPAE LATVLPVLER IQQDFNASAS
     GGKKVSLADL IVLAGSAAIE KAAKDGGYNV TVPFAPGRTD ASQENTDVES FAVLEPRADG
     FRNYVRPGEK VQLEKMLLER AYFLGVTAPQ LTALVGGLRA LDVNHGGTKH GVFTDRPGAL
     TNDFFVNLLD MGTEWKTSET TENVYEGVDR KTGQLKWTAT ANDLVFGSHS VLRAVAEVYA
     QSDNGERFVN DFVKAWVKVM NNDRFDLK