ID   KATG_SYNP6              Reviewed;         720 AA.
AC   Q5MZ99; Q9R6S9;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 102.
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}; OrderedLocusNames=syc2431_d;
OS   Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS   nidulans).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=269084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBUNIT, HEME-BINDING, AND
RP   ACTIVITY REGULATION.
RX   PubMed=10863004; DOI=10.1016/s0300-9084(00)00204-2;
RA   Engleder M., Regelsberger G., Jakopitsch C., Furtmueller P.G., Rueker F.,
RA   Peschek G.A., Obinger C.;
RT   "Nucleotide sequence analysis, overexpression in Escherichia coli and
RT   kinetic characterization of Anacystis nidulans catalase-peroxidase.";
RL   Biochimie 82:211-219(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX   PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA   Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA   Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT   "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT   Synechococcus elongatus PCC 6301 chromosome: gene content and
RT   organization.";
RL   Photosyn. Res. 93:55-67(2007).
RN   [3]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND SUBCELLULAR LOCATION.
RX   PubMed=9207193; DOI=10.1006/bbrc.1997.6847;
RA   Obinger C., Regelsberger G., Strasser G., Burner U., Peschek G.A.;
RT   "Purification and characterization of a homodimeric catalase-peroxidase
RT   from the cyanobacterium Anacystis nidulans.";
RL   Biochem. Biophys. Res. Commun. 235:545-552(1997).
CC   -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC       peroxidase activity. {ECO:0000255|HAMAP-Rule:MF_01961,
CC       ECO:0000269|PubMed:10863004, ECO:0000269|PubMed:9207193}.
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       Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.;
CC   -!- ACTIVITY REGULATION: Inhibited by cyanide.
CC       {ECO:0000269|PubMed:10863004}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=4.3 mM for H(2)O(2) for the catalase reaction
CC         {ECO:0000269|PubMed:9207193};
CC       pH dependence:
CC         Optimum pH is 6.5-7.5 for both the catalase and the peroxidase
CC         reaction. {ECO:0000269|PubMed:9207193};
CC   -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10863004,
CC       ECO:0000269|PubMed:9207193}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:9207193}.
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; AF197161; AAF05841.1; -; Genomic_DNA.
DR   EMBL; AP008231; BAD80621.1; -; Genomic_DNA.
DR   RefSeq; WP_011244741.1; NC_006576.1.
DR   AlphaFoldDB; Q5MZ99; -.
DR   SMR; Q5MZ99; -.
DR   STRING; 269084.syc2431_d; -.
DR   PeroxiBase; 3578; SeCP01_PCC6301.
DR   EnsemblBacteria; BAD80621; BAD80621; syc2431_d.
DR   KEGG; syc:syc2431_d; -.
DR   eggNOG; COG0376; Bacteria.
DR   OMA; MILAGNC; -.
DR   Proteomes; UP000001175; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
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   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; PS00436; PEROXIDASE_2; 1.
DR   PROSITE; PS50873; PEROXIDASE_4; 2.
PE   1: Evidence at protein level;
KW   Cytoplasm; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
KW   Peroxidase.
FT   CHAIN           1..720
FT                   /note="Catalase-peroxidase"
FT                   /id="PRO_0000354941"
FT   ACT_SITE        95
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   BINDING         263
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            91
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        94..222
FT                   /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT                   248)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CROSSLNK        222..248
FT                   /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT                   94)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT   CONFLICT        5
FT                   /note="Q -> R (in Ref. 1; AAF05841)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        358
FT                   /note="V -> I (in Ref. 1; AAF05841)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   720 AA;  80078 MW;  93A4C2E9990F1A2F CRC64;
     MTATQGKCPV MHGGATTVNI STAEWWPKAL NLDILSQHDR KTNPMGPDFN YQEEVKKLDV
     AALKQDLQAL MTDSQDWWPA DWGHYGGLMI RLTWHAAGTY RIADGRGGAG TGNQRFAPLN
     SWPDNTNLDK ARRLLWPIKQ KYGNKLSWAD LIAYAGTIAY ESMGLKTFGF AFGREDIWHP
     EKDIYWGPEK EWVPPSTNPN SRYTGDRELE NPLAAVTMGL IYVNPEGVDG NPDPLKTAHD
     VRVTFARMAM NDEETVALTA GGHTVGKCHG NGNAALLGPE PEGADVEDQG LGWINKTQSG
     IGRNAVTSGL EGAWTPHPTQ WDNGYFRMLL NYDWELKKSP AGAWQWEPIN PREEDLPVDV
     EDPSIRRNLV MTDADMAMKM DPEYRKISER FYQDPAYFAD VFARAWFKLT HRDMGPKARY
     IGPDVPQEDL IWQDPIPAGN RNYDVQAVKD RIAASGLSIS ELVSTAWDSA RTYRNSDKRG
     GANGARIRLA PQKDWEGNEP DRLAKVLAVL EGIAAATGAS VADVIVLAGN VGVEQAARAA
     GVEIVLPFAP GRGDATAEQT DTESFAVLEP IHDGYRNWLK QDYAATPEEL LLDRTQLLGL
     TAPEMTVLIG GLRVLGTNHG GTKHGVFTDR EGVLTNDFFV NLTDMNYLWK PAGKNLYEIC
     DRKTNQVKWT ATRVDLVFGS NSILRAYSEL YAQDDNKEKF VRDFVAAWTK VMNADRFDLD