KATG_STRCO
ID KATG_STRCO Reviewed; 740 AA.
AC Q9RJH9; Q9KK92;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 131.
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}; Synonyms=catC, cpeB;
GN OrderedLocusNames=SCO0560; ORFNames=SCF73.07c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, AND SUBUNIT.
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=10850993; DOI=10.1128/jb.182.13.3767-3774.2000;
RA Hahn J.-S., Oh S.-Y., Roe J.-H.;
RT "Regulation of the furA and catC operon, encoding a ferric uptake regulator
RT homologue and catalase-peroxidase, respectively, in Streptomyces coelicolor
RT A3(2).";
RL J. Bacteriol. 182:3767-3774(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961,
CC ECO:0000269|PubMed:10850993}.
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. {ECO:0000269|PubMed:10850993}.
CC -!- INDUCTION: Induced in late exponential growth phase (at protein level).
CC {ECO:0000269|PubMed:10850993}.
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; AF126956; AAF78102.1; -; Genomic_DNA.
DR EMBL; AL939106; CAB57412.1; -; Genomic_DNA.
DR RefSeq; NP_624873.1; NC_003888.3.
DR RefSeq; WP_011027206.1; NZ_VNID01000015.1.
DR AlphaFoldDB; Q9RJH9; -.
DR SMR; Q9RJH9; -.
DR STRING; 100226.SCO0560; -.
DR PeroxiBase; 2351; ScoCP01_A3.
DR GeneID; 1095983; -.
DR KEGG; sco:SCO0560; -.
DR PATRIC; fig|100226.15.peg.541; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_11; -.
DR InParanoid; Q9RJH9; -.
DR OMA; MILAGNC; -.
DR PhylomeDB; Q9RJH9; -.
DR Proteomes; UP000001973; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004096; F:catalase activity; IBA:GO_Central.
DR GO; GO:0020037; F:heme binding; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IBA:GO_Central.
DR GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome.
FT CHAIN 1..740
FT /note="Catalase-peroxidase"
FT /id="PRO_0000055576"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
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 215
FT /note="D -> A (in Ref. 1; AAF78102)"
FT /evidence="ECO:0000305"
FT CONFLICT 258
FT /note="A -> G (in Ref. 1; AAF78102)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="H -> Y (in Ref. 1; AAF78102)"
FT /evidence="ECO:0000305"
FT CONFLICT 585
FT /note="A -> L (in Ref. 1; AAF78102)"
FT /evidence="ECO:0000305"
FT CONFLICT 722..723
FT /note="HD -> QH (in Ref. 1; AAF78102)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 740 AA; 80816 MW; 767C0A9BC9BD7798 CRC64;
MSENHDAIVT DAKTEETDGC PVAHGRAPHP TQGGGNRQWW PERLNLKILA KNPAVANPLG
EEFDYAEAFE ALDLAAVKRD IAEVLTTSQD WWPADFGNYG PLMIRMAWHS AGTYRISDGR
GGAGAGQQRF APLNSWPDNG NLDKARRLLW PVKKKYGQNL SWADLLVLTG NVALETMGFE
TFGFAGGRAD VWEAEEDVYW GPETTWLDDR RYTGDRELEN PLGAVQMGLI YVNPEGPNGN
PDPIAAARDI RETFRRMAMN DEETVALIAG GHTFGKTHGA GPADAVGDDP EAAAMEQQGL
GWKSTHGTGK GGDAITSGLE VTWTSTPTQW GNGFFKNLFE FEYELEQSPA GANQWVAKDA
PEIIPDAHDP AKKHRPRMLT TDLSLRLDPI YGPISRRFYE NPEEFADAFA RAWFKLTHRD
MGPKSLYLGP EVPEETLIWQ DPLPEPEGEV IDAEDVATLK TKLLESGLSV SQLVTTAWAS
ASTFRGSDKR GGANGARIRL EPQRGWEVNE PDELAQVLRV LEGVQREFNS GSGAKKVSLA
DLIVLGGSAA VEKAAKEAGF PVEVPFAAGR VDATEEHTDA ESFEALEPTA DGFRNYLGKG
NRLPAEFLLL DRANLLTLSA PEMTVLVGGL RVLGAGHQQS QLGVFTRTPG SLTNDFFVNL
LDLGTTWKST SEDRTTFEGR DAATGEVKWA GSRADLVFGS NAELRALAEV YASDDAGEKF
VHDFVAAWVK VMNLDRFDLA
