KATG_GLOVI
ID KATG_GLOVI Reviewed; 735 AA.
AC Q7NGW6;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=gll2771;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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; BA000045; BAC90712.1; -; Genomic_DNA.
DR RefSeq; NP_925717.1; NC_005125.1.
DR RefSeq; WP_011142765.1; NC_005125.1.
DR AlphaFoldDB; Q7NGW6; -.
DR SMR; Q7NGW6; -.
DR STRING; 251221.35213340; -.
DR PeroxiBase; 2378; GviCP01_PCC7421.
DR EnsemblBacteria; BAC90712; BAC90712; BAC90712.
DR KEGG; gvi:gll2771; -.
DR PATRIC; fig|251221.4.peg.2799; -.
DR eggNOG; COG0376; Bacteria.
DR HOGENOM; CLU_025424_2_0_3; -.
DR InParanoid; Q7NGW6; -.
DR OMA; MILAGNC; -.
DR OrthoDB; 49441at2; -.
DR PhylomeDB; Q7NGW6; -.
DR Proteomes; UP000000557; 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 3: Inferred from homology;
KW Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase;
KW Reference proteome.
FT CHAIN 1..735
FT /note="Catalase-peroxidase"
FT /id="PRO_0000354803"
FT REGION 342..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 98
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 261
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 94
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 97..220
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 246)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 220..246
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 97)"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
SQ SEQUENCE 735 AA; 80389 MW; 18F3B16163E81E7F CRC64;
MDVEAKCPMG GGKVEGRAVL FEMTNRLWWP NHLDLSVLHQ NPPAGNPMGE GFNYAAEFES
LDLAAVKQDI FALMTESQDW WPADYGHYGP LFIRMAWHAA GTYRIGDGRG GAGAGTQRFA
PLNSWPDNAN LDKARLLLWP IKEKYGRKLS WGDLLILAGN CALESMGFKT AGFAGGRVDI
WEPENDIFWG PEREWLGDER YSSDRDLAHP LAAVQMGLIY VNPEGPNGKP DPMAAAHDIR
ETFGRMAMND EETVALIAGG HTFGKCHGAA EPSQYVGAEP EGAGIERQGL GWDNSFGSGR
GVHTITSGLE GAWTKNPIQW DNGYFENLFE YEWELTKSPA GAHQWTPKNP EAASTVPDAH
DPHKRHAPMM ATTDLAMRAD PAYEKISRRF YDNPDQLAHA FAEAWYKLTH RDMGPYARLL
GPEVPSEPRI WQDPVPASDH PLIDDADIAE LKAQILAAGL SIARLVTTAW ASASTFRGTD
KRGGANGARI RLVPQKDWAV NEPTELATAL AKLEAIQQDF NAGQTGGKQV SLADLIVLGG
CAAVEQAAKK AGHDITVPFT PGRTDASPDQ TDVESFAPLE PKIDGFRNYV GEKSVYSAEE
MLVDRAHLLT LSAPEMTVLV GGLRVLGANY GGSKLGVFTE RPETLTNDFF VNLLKTSTSM
KWEASPDADV FEASDRATGE KKWAGTRVDL IFGSNSQLRA LSEAYATADA QQTFVDAFVA
AWTKVMNLDR FDLPR
