KATG1_MYCS2
ID KATG1_MYCS2 Reviewed; 739 AA.
AC A0R609; I7GAP8; O05763; Q59557;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
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};
GN OrderedLocusNames=MSMEG_6384, MSMEI_6216;
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], AND DISRUPTION PHENOTYPE.
RX PubMed=8870251; DOI=10.1111/j.1574-6968.1996.tb08507.x;
RA Billman-Jacobe H., Sloan J., Coppel R.L.;
RT "Analysis of isoniazid-resistant transposon mutants of Mycobacterium
RT smegmatis.";
RL FEMS Microbiol. Lett. 144:47-52(1996).
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].
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. 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 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 -!- DISRUPTION PHENOTYPE: Defects cause isoniazid (INH) resistance.
CC {ECO:0000269|PubMed:8870251}.
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
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DR EMBL; X98718; CAA67268.1; -; Genomic_DNA.
DR EMBL; CP000480; ABK73944.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP42642.1; -; Genomic_DNA.
DR RefSeq; WP_011731250.1; NZ_CP009494.1.
DR RefSeq; YP_890597.1; NC_008596.1.
DR AlphaFoldDB; A0R609; -.
DR SMR; A0R609; -.
DR STRING; 246196.MSMEI_6216; -.
DR PeroxiBase; 3550; MsmCP01_mc2155.
DR EnsemblBacteria; ABK73944; ABK73944; MSMEG_6384.
DR EnsemblBacteria; AFP42642; AFP42642; MSMEI_6216.
DR GeneID; 66737662; -.
DR KEGG; msg:MSMEI_6216; -.
DR KEGG; msm:MSMEG_6384; -.
DR PATRIC; fig|246196.19.peg.6211; -.
DR eggNOG; COG0376; Bacteria.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
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..739
FT /note="Catalase-peroxidase 1"
FT /id="PRO_0000293596"
FT REGION 1..33
FT /note="Disordered"
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 277
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..236
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 262)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 236..262
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 113)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CONFLICT 374..378
FT /note="AHEDG -> PTRTA (in Ref. 1; CAA67268)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 739 AA; 81115 MW; 5E87F6B884D832ED CRC64;
MPEDRPIEDS PPIGEAQTDA PAGGCPAGFG RIKPPVAGGS NRDWWPNQLN LKILQKNPDV
INPLDEDFDY RSAVQNLDVD ALRADIVEVM HTSQDWWPAD FGHYGPLFIR MAWHAAGTYR
VSDGRGGAGA GMQRFAPLNS WPDNASLDKA RRLLWPVKKK YGKNLSWADL IVYAGNVALE
DMGFRTAGFA FGREDRWEPE EDVYWGPEQE WLDDKRYTGE RDLENPLAAV QMGLIYVNPE
GPNGNPDPQA SAIDIRETFG RMAMNDVETA ALIVGGHTFG KTHGNGDASL VGPEPEAAPL
EEVGLGWRNP QGTGVGKDAI TSGLEVTWTH TPTKWDNSFL EILYGNEWEL TKSPAGANQW
KPKDNGWANS VPLAHEDGKT HPSMLTSDLA LRVDPIYEQI TRRWLDHPEE LAEEFAKAWF
KLLHRDMGPV TRYLGPEVPK DTWLWQDNIP AGNDLSDDEV AKLKELIADS GLTVSQLVST
AWKAASTFRS SDLRGGANGG RIRLQPQLGW EANEPDELAQ VVRKYEEIQK ASGINVSFAD
LVVLGGNVGV EKAAKAAGFD VTVPFTPGRG DATQEETDVD SFAYLEPKAD GFRNYLGKGS
DLPAEFKLID RANLLGLSAP EMTTLVGGLR VLDVNHGGTK HGVLTDKPGA LTTDFFVNLL
DMSTAWKPSP ADDGTYIGTD RATGSPKWTG TRVDLVFASN SQLRALAEVY AEDDSKEKFV
KDFVAAWTKV MDADRFDVA
