KATG1_MYCVP
ID KATG1_MYCVP Reviewed; 747 AA.
AC A1TA09;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 84.
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}; OrderedLocusNames=Mvan_3208;
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000511; ABM14009.1; -; Genomic_DNA.
DR RefSeq; WP_011780414.1; NC_008726.1.
DR AlphaFoldDB; A1TA09; -.
DR SMR; A1TA09; -.
DR STRING; 350058.Mvan_3208; -.
DR PeroxiBase; 3576; MvaCP02_PYR1.
DR EnsemblBacteria; ABM14009; ABM14009; Mvan_3208.
DR KEGG; mva:Mvan_3208; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_11; -.
DR OMA; EEIFWGP; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000009159; 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; 2.
PE 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome.
FT CHAIN 1..747
FT /note="Catalase-peroxidase 1"
FT /id="PRO_0000354847"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 113
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 281
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 109
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 112..240
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 266)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 240..266
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 112)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 747 AA; 82208 MW; F081DB8AE9B70E83 CRC64;
MTDTSDARPP HSDDKTRSHS ESENPAIDSP EPKVHAPLTN KDWWPEQVDV SVLHKQNEKG
NPLGEDFDYA TEFAKLDVEA FKRDVIDLIN TSQDWWPADY GSYAGLFIRM SWHAAGTYRI
FDGRGGAGQG SQRFAPLNSW PDNANLDKAR RLLWPIKRKY GNKISWADLI AYAGNAALES
AGFQTFGFAF GREDIWEPEE MLWGQEDTWL GTDKRYGGTN DSDTRELAEP FGATTMGLIY
VNPEGPEGKP DPLAAAHDIR ETFGRMAMND EETAALIVGG HTLGKTHGAA DVNVGPEPEG
APIEQQGLGW KCPFGTGNAG DTVTSGLEVV WTTTPTKWSN AYLELLYGYE WELTKSPGGA
WQFEAKDAEA IIPDPFGGPP RKPTMLVTDV SMRVDPIYGP ITRRWLDHPE EMNEAFAKAW
YKLMHRDMGP VSRYLGPWVA EPQLWQDPVP AVDHELIDES DIAALKAAVL QSGLSVPQLV
KTAWASASSF RGTDKRGGAN GARLRLEPQR SWEANEPSEL DKVLPVLERI QQDFNASATG
GKKVSLADLI VLAGSAAVEK AAKDGGYEIS VHFAPGRTDA SQEQTDVDSF AVLEPRADGF
RNFARPGEKT PLEQLLVDKA YFLDLTAPEM TALIGGLRTL NANHGGSKHG VFTERPGVLS
NDFFVNLLDM GTEWKPSELT ENVYDGKDRA TGQPKWTATA ADLVFGSNSV LRAVVEVYAQ
DDNQGKFVED FVAAWVKVMN NDRFDLG
