KATG_SYNPW
ID KATG_SYNPW Reviewed; 731 AA.
AC A5GJV3;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, 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=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
GN Name=katG {ECO:0000255|HAMAP-Rule:MF_01961};
GN OrderedLocusNames=SynWH7803_0792;
OS Synechococcus sp. (strain WH7803).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32051;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WH7803;
RG Genoscope;
RL Submitted (MAY-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; CT971583; CAK23218.1; -; Genomic_DNA.
DR RefSeq; WP_011932700.1; NC_009481.1.
DR AlphaFoldDB; A5GJV3; -.
DR SMR; A5GJV3; -.
DR STRING; 32051.SynWH7803_0792; -.
DR PeroxiBase; 6246; SspCP01_WH7803.
DR EnsemblBacteria; CAK23218; CAK23218; SynWH7803_0792.
DR KEGG; syx:SynWH7803_0792; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_3; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR Proteomes; UP000001566; 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; 1.
PE 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome.
FT CHAIN 1..731
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354945"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 96
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 259
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 92
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 95..218
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 244)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 218..244
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 95)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 731 AA; 79962 MW; 7F170F1D7523A733 CRC64;
MSDLKCPFSG HTGAVTPAGN TNNGDWWPNQ INLGILHQHH PASNPLGDAF DYPTAFASLD
YSALKADLQT LMTDSQDWWP ADWGHYGALF IRLAWHSAGT YRTGDGRGGA GHGNQRFAPL
NSWPDNTNLD KARRLLWPIK RKYGNAISWA DLIILSGNVA LESMGFRTFG FAGGREDIWQ
PEEDVFWGKE TGWLKDERRN DKGELNQPLA AVEMGLIYVN PEGPHGEPDP VASGRDVRET
FARMGMTVEE TVALVAGGHT FGKCHGAAPD SHLEAEPEGA ALHEQGLGWR NTYESGKGEH
TITSGIEGAW KPNPTRWDQG YFQMMFTYEW ELTKSPAGAW QWTAKDVKPE HMIPDAHVAG
KSSAPIMTTA DLSLRHDAIM EPVARRFHLD QEAFADAFAR AWFKLTHRDL GPRALYLGPD
VPEEVQIWQD PVPPVTHPLI DEAEISTLKQ QILASGQSVS ALVAAAWGSA STFRGSDRRG
GANGGRIRLL PQRTWEVNDP EQLNGVLTAL ETIQSQFNSS SSNGKSVSIA DLIVLGGCAA
VEKAAADGGH TVVVPFRPGR SDAGPEQTDT ASFNVLKPLA DGFRNWQRSG LPLRAEELLV
DRAQLLTLSA PEMTVLLAGL RVMGANTAGN RQGVFTQNVG VLSNDFCVNL LDMTTRWTPT
SEAQDAYIGR DSATGAERWS ASRADLVFGS NSQLRAIVEV YAQNDGGSRF VADFVKAWVK
VMELDRFDLR S
