KATG_STRAM
ID KATG_STRAM Reviewed; 738 AA.
AC A0ACX8;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 56.
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}; ORFNames=SAMR0623;
OS Streptomyces ambofaciens.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1889;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23877 / 3486 / DSM 40053 / JCM 4204 / NBRC 12836 / NRRL B-2516;
RX PubMed=16956972; DOI=10.1093/molbev/msl108;
RA Choulet F., Aigle B., Gallois A., Mangenot S., Gerbaud C., Truong C.,
RA Francou F.-X., Fourrier C., Guerineau M., Decaris B., Barbe V.,
RA Pernodet J.-L., Leblond P.;
RT "Evolution of the terminal regions of the Streptomyces linear chromosome.";
RL Mol. Biol. Evol. 23:2361-2369(2006).
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; AM238664; CAJ88333.1; -; Genomic_DNA.
DR RefSeq; WP_053141208.1; NZ_CP012949.1.
DR AlphaFoldDB; A0ACX8; -.
DR SMR; A0ACX8; -.
DR PATRIC; fig|1889.10.peg.6676; -.
DR OMA; MILAGNC; -.
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_0000354938"
FT REGION 1..37
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"
SQ SEQUENCE 738 AA; 80883 MW; F81E8BE56B76287A CRC64;
MSENHDAIVT DAKTEEAGGC PVAHGRAPHP TQGGGNRQWW PERLNLKILA KNPAVANPLG
DGFDYAEAFG SLDLPAVKRD IAEVLTTSQD WWPADFGHYG PLMIRMAWHS AGTYRISDGR
GGAGAGQQRF APLNSWPDNG NLDKARRLLW PVKKKYGQSL SWADLLILTG NVALEQMGFE
TFGFAGGRAD VWEAEEDVYW GPETTWLDDR RYSGDRELEN PLGAVQMGLI YVNPEGPNGN
PDPIAAARDI RETFGRMAMN DEETVALIAG GHTFGKTHGA GPADHVGDDP EAASMEEQGL
GWRNSFGTGK GGDAITSGLE VTWTSTPTRW SNGFFKNLFE FEYELEQSPA GANQWVAKDA
PEIVPDAHDP SKKHRPKMLT TDLSLRYDPI YEPISRRFYE NPEEFADAFA RAWYKLTHRD
MGPKSLYLGP EVPEETLLWQ DPLPEADGEP VDAEDVATLK TKLLESGLSV SQLVSTAWAS
ASTFRGSDKR GGANGARIRL EPQRGWEVNE PDELAQVLRV LEGIQQEFNS GTKKVSLADL
IVLGGTAAVE KAAKEAGFQV QVPFTAGRVD ATEEHTDAES FEALEPVADG FRNYLGKGNR
LPAEYLLLDR ANLLTLSAPE MTVLVGGLRV LGANYQKSPL GAFTRTPGSL TNDFFVNLLD
LGVTWKSTSE DQTTFEGRDA ATGEVKWAGS RADLVFGSNS ELRALAEVYA SDDAKEKFVH
DFVDAWVKVM NLDRFDLV
