KATG_MYCIT
ID KATG_MYCIT Reviewed; 746 AA.
AC Q04657;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 95.
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};
DE AltName: Full=Protein Mi85;
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961}; Synonyms=Mi85;
OS Mycobacterium intracellulare.
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=1767;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1336034; DOI=10.1099/00221287-138-11-2363;
RA Morris S.L., Nair J., Rouse D.A.;
RT "The catalase-peroxidase of Mycobacterium intracellulare: nucleotide
RT sequence analysis and expression in Escherichia coli.";
RL J. Gen. Microbiol. 138:2363-2370(1992).
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 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; M86741; AAA25360.1; -; Genomic_DNA.
DR PIR; A47685; A47685.
DR RefSeq; WP_038536301.1; NZ_LZJT01000119.1.
DR AlphaFoldDB; Q04657; -.
DR SMR; Q04657; -.
DR PeroxiBase; 2433; MinCP01.
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..746
FT /note="Catalase-peroxidase"
FT /id="PRO_0000055570"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
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 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"
SQ SEQUENCE 746 AA; 81418 MW; 15F35F7F5028F2B2 CRC64;
MSSDTSSSRP PQPDSGTASK SESENPAIPS PKPKAHAPLT NRDWWPDQVD VSSLHPHSPL
SNPLGDDFDY AAEFAKLDVE ALKADMISLM TTSQDWWPAD YGHYGGLFIR MSWHAAGTYR
IHDGRGGAGQ GMQRFAPLNS WPDNASLDKA RRLLWPIKKK YGNKISWADL ITYAGNVALE
SMGFKTFGFG FGREDVWEPE EILWGEEEEW LGTDKRYSGE RELAQPYGAT TMGLIYVNPE
GPEGKPDPIA AAIDIRETFG RMAMNDEETA ALIVGGHSFG KTHGAGDADL VGPEPEAAPI
EQQGLGWKSS YGTGSGKDAI TSGLEVVWTP TPTKWDNSFL ETLYGYEWEL TKSPAGAWQF
TAKDGAGAGT IPDPFGGAGR APTMLVTDIS LRESPIYADI TRRWLDHPEE LADAFAKAWY
KLLHRDMGPI SRYLGPWVAE PQLWQDPVPA VDHELVDDND VAALKKKVLD SGLSIPQLVK
TAWSAAASYR NTDKRGGANG GRLRLQPQRS WEVNEPSELD KVLPVLEKIQ QDFNASASGG
KKISLADLIV LAGSAAVEKA AKDAGYEISV HFAPGRTDAS QESTDVESFA VLEPRADGFR
NYIRPGEKAP LEQLLIERAY LLGVTGPEMT VLVGGLRALG ANHGSSKHGV FTDRPGALTN
DFFVNLLDMG TEWKASETAE NVYEGRDRAS GALKWTATAN DLVFGSNSVL RGLVEVYAQD
DAHGKFVEDF VAAWVKVMNS DRFDLK
