KATG_MYCVN
ID KATG_MYCVN Reviewed; 737 AA.
AC Q9R2E9;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=P81;
DE AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961};
OS Mycolicibacterium vanbaalenii (Mycobacterium vanbaalenii).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=110539;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-25, FUNCTION, AND
RP INDUCTION.
RC STRAIN=PYR-1;
RX PubMed=11010873; DOI=10.1128/aem.66.10.4300-4304.2000;
RA Wang R.-F., Wennerstrom D., Cao W.-W., Khan A.A., Cerniglia C.E.;
RT "Cloning, expression, and characterization of the katG gene, encoding
RT catalase-peroxidase, from the polycyclic aromatic hydrocarbon-degrading
RT bacterium Mycobacterium sp. strain PYR-1.";
RL Appl. Environ. Microbiol. 66:4300-4304(2000).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. May play a role in polycyclic aromatic hydrocarbon
CC (PAH) metabolism. {ECO:0000255|HAMAP-Rule:MF_01961,
CC ECO:0000269|PubMed:11010873}.
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 -!- INDUCTION: By the polycyclic aromatic hydrocarbon pyrene.
CC {ECO:0000269|PubMed:11010873}.
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; AF207899; AAF20142.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9R2E9; -.
DR SMR; Q9R2E9; -.
DR PeroxiBase; 2436; MvaCP01_PYR1.
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.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding;
KW Oxidoreductase; Peroxidase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11010873"
FT CHAIN 2..737
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354846"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 108
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 276
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
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 104
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 107..235
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 261)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 235..261
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 107)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 737 AA; 80833 MW; 1CEDDB657B2DEF82 CRC64;
MPEATEHPPI GEAQTEPAQS GCPMVIKPPV EGGSNRDWWP NAVNLKMLQK DPEVIDPIDE
GYDYREAVQT LDVDQLARDF DELCTNSQDW WPADFGHYGP LFIRMSWHAA GTYRVQDGRG
GAGKGMQRFA PLNSWPDNVS LDKARRLLWP LKKKYGKKLS WSDLIVYAGN RAMENMGFKT
AGFAFGRPDY WEPEEDVYWG AEHEWLGSQD RYAGANGDRT KLENPLGASH MGLIYVNPEG
PEGNPDPIAA AIDIRETFGR MAMNDVETAA LIVGGHTFGK THGATDIVNG PEPEAAPLEQ
MGLGWSNPGV GIDTVSSGLE VTWTHTPTKW DNSFLEILYG NEWELFKSPA GANQWRPKDN
GWADSVPMAQ GTGKTHPAML TTDLSMRMDP IYGEITRRWL DHPEELAEEY AKAWFKLLHR
DMGPVQRYLG PLVPTQTWLW QDIVPAGKPL SDADVATLKG AIADSGLTVQ QLVSTAWKAA
SSFRISDMRG GANGGRIRLQ PQLGWESNEP DELAQVISKL EEIQGSSGID VSFADLVVLG
GNVGIETAAK AAGFDIEVPF SSGRGDATQE QTDVEAFSYL EPKADGFRNY VGKGLNLPAE
YQLIDQANLL NLSAPQMTVL IGGLRALGIT HGDSKLGVLT DTPGQLTNDY FVNLTDMGVK
WAPAPADDGT YVGTDRDTGE VKYTASRVDL LFGSNSQLRA LAEVYAEDDS RDKFVKDFVA
AWVNVMDADR YDIGKGA
