KATG_SYNP2
ID KATG_SYNP2 Reviewed; 725 AA.
AC B1XK45;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=SYNPCC7002_A2422;
OS Synechococcus sp. (strain ATCC 27264 / PCC 7002 / PR-6) (Agmenellum
OS quadruplicatum).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=32049;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27264 / PCC 7002 / PR-6;
RA Li T., Zhao J., Zhao C., Liu Z., Zhao F., Marquardt J., Nomura C.T.,
RA Persson S., Detter J.C., Richardson P.M., Lanz C., Schuster S.C., Wang J.,
RA Li S., Huang X., Cai T., Yu Z., Luo J., Zhao J., Bryant D.A.;
RT "Complete sequence of Synechococcus sp. PCC 7002.";
RL Submitted (FEB-2008) 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; CP000951; ACB00400.1; -; Genomic_DNA.
DR AlphaFoldDB; B1XK45; -.
DR SMR; B1XK45; -.
DR STRING; 32049.SYNPCC7002_A2422; -.
DR PeroxiBase; 6257; SspCP01_PCC7002.
DR EnsemblBacteria; ACB00400; ACB00400; SYNPCC7002_A2422.
DR KEGG; syp:SYNPCC7002_A2422; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_3; -.
DR OMA; MILAGNC; -.
DR Proteomes; UP000001688; 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 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; 1.
PE 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome.
FT CHAIN 1..725
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354942"
FT ACT_SITE 100
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 268
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 96
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 99..227
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 253)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 227..253
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 99)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 725 AA; 80606 MW; 37FA7650DB77FF50 CRC64;
MHDHITNTGG KCPVMHGALT TSSMATNMEW WPKALNLDIL HQHDHKTNPM GANFNYQDAV
KTLDVDALKR DLHALMTDSQ DWWPADWGHY GGLMIRMTWH AAGTYRIADG RGGAGTGNQR
FAPINSWPDN TNLDKARRLL WPLKKKYGNK LSWADLIAYA GTIAYESMGL KTFGFAFGRE
DIWHPEKDIY WGSEKEWLAP SDNPHSRYSG ERDLENPLAA VMMGLIYVNP EGVDGNPDPL
KTAHDIRITF SRMAMNDEET VALTAGGHTV GKCHGNGDAT LLGPEPEAAD LDDQGLGWLN
KTQRGIGRNT VTSGIEGAWT TYPTQWDNGY FRLLLNYDWE LKKSPAGAWQ WEPINIKEED
KPVDVEDPSI RLSPIMTDAD MAMKMDPDYR QISERFYQDP AYFAETFARA WFKLTHRDMG
PKSRYIGPDV PQEDLLWQDP IPAGKTDYDP QAVKDKIAAS GLSVSEMVCT AWDSARTFRG
SDKRGGANGA RIRLAPQKDW AGNEPARLAK VLPVLEAIAT ESGASVADVI VLAGNVGIEQ
AAQAAGVEIT VPFAPGRGDA TAEMTDVEGF AVLEPLHDGY RNWLQKDYVV SPEELMLDRT
QLMGLTAPEM TVLVGGMRVL GTNYGGTKHG VLTDREGALT NDFFVNLTDM KYTWKPAGKN
LYEIGDRHTG EVKWTATRVD LVFGCNSILR AYAEVYAQDD SNEKFIQDFV AAWTKVMNAD
RFDLA
