KATG_MYCA9
ID KATG_MYCA9 Reviewed; 738 AA.
AC B1MBD0; A0F0B8;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 89.
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=MAB_2470c;
OS Mycobacteroides abscessus (strain ATCC 19977 / DSM 44196 / CIP 104536 / JCM
OS 13569 / NCTC 13031 / TMC 1543) (Mycobacterium abscessus).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacteroides; Mycobacteroides abscessus.
OX NCBI_TaxID=561007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Park Y., Lee S., Ryu S., Bai G., Cho S.;
RL Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19977 / DSM 44196 / CIP 104536 / JCM 13569 / NCTC 13031 / TMC
RC 1543;
RX PubMed=19543527; DOI=10.1371/journal.pone.0005660;
RA Ripoll F., Pasek S., Schenowitz C., Dossat C., Barbe V., Rottman M.,
RA Macheras E., Heym B., Herrmann J.L., Daffe M., Brosch R., Risler J.L.,
RA Gaillard J.L.;
RT "Non mycobacterial virulence genes in the genome of the emerging pathogen
RT Mycobacterium abscessus.";
RL PLoS ONE 4:E5660-E5660(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}.
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DR EMBL; DQ872161; ABJ97682.1; -; Genomic_DNA.
DR EMBL; CU458896; CAM62551.1; -; Genomic_DNA.
DR RefSeq; WP_005111000.1; NZ_MLCG01000006.1.
DR AlphaFoldDB; B1MBD0; -.
DR SMR; B1MBD0; -.
DR EnsemblBacteria; CAM62551; CAM62551; MAB_2470c.
DR GeneID; 66972844; -.
DR KEGG; mab:MAB_2470c; -.
DR OMA; MILAGNC; -.
DR Proteomes; UP000007137; 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.
FT CHAIN 1..738
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354834"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 109
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 272
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 105
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 108..231
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 257)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 231..257
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 108)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CONFLICT 719
FT /note="A -> V (in Ref. 1; ABJ97682)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 738 AA; 80406 MW; 64FD248A6E87F843 CRC64;
MSEEHPPIAE ANSQPSNGCP VAGGRLNYPV EGGNANREWW PTQLNLQILK KNPPAANPLG
EDFDYAKAVQ TIDVDQLKAD VAKVLTDSQD WWPADFGNYG PMFIRMAWHA AGTYRVGDGR
GGAGAGMQRF APLNSWPDNV LLDRARRLLW PVKKKYGNKL SWADLIVFAG NHAMDTMGFK
TFGFAFGRED RWEPEQDVYW GPEHTWLGDE RYTGDRDLEN PLAAVQMGLI YVNPEGPNGN
PDPLAAAIDI RETFGRMAMN DEETAALIVG GHTFGKTHGA GDAGLVGPDP EAAPLEQMGI
GWKSAFGSGK GNDAIGSGLE VIWTHTPTKW DNSFLEILYG NEWELTKSPA GAHQWKPKDG
GWANSVPMAQ GTGKTHPSML TTDLSMRFDP IYGQITKRWL DHPEELADAY AKAWYKLIHR
DLGPLSRYLG PLVPKETLPW QDVIPVSETN VGADDVAELK KQVLASGLTV PQLVSTAWKA
AASYRNSDKR GGANGGRIRL QPQAGWESNE PDELAQVIRI LEGVQESFNA GDKKISFADL
VVLGGAAAVE KAARDAGFDI TVPFTPGRGD ATQEQTDVES FSYLEPTADG FRNYLGKGAQ
IPAEYKLIDR ANLLALSPPE LAVLVGGLRV LGANYQGSEL GVLTDRPGTL TNDFFVNLVD
MGTEWTPSPA DDGTYVGTDR ATGASKWTAS RVDLVFGANS ELRALAEVYA QDDAQEKFAK
DFVAAWVKVS DADRFDVR
