KATG_SYNY3
ID KATG_SYNY3 Reviewed; 754 AA.
AC P73911; P97083; Q79EX5;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 139.
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=sll1987;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Ushimaru T., Hayashi H., Murata N.;
RT "Nucleotide sequence of katG of Synechocystis sp. PCC 6803.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
RN [3]
RP BIOPHYSICOCHEMICAL PROPERTIES, HEME-BINDING, SUBUNIT, AND MASS
RP SPECTROMETRY.
RX PubMed=10543446; DOI=10.1515/bc.1999.135;
RA Jakopitsch C., Ruker F., Regelsberger G., Dockal M., Peschek G.A.,
RA Obinger C.;
RT "Catalase-peroxidase from the cyanobacterium Synechocystis PCC 6803:
RT cloning, overexpression in Escherichia coli, and kinetic
RT characterization.";
RL Biol. Chem. 380:1087-1096(1999).
RN [4]
RP BIOPHYSICOCHEMICAL PROPERTIES, HEME-BINDING, AND SUBUNIT.
RX PubMed=9919646; DOI=10.1111/j.1574-6968.1999.tb13348.x;
RA Regelsberger G., Obinger C., Zoder R., Altmann F., Peschek G.A.;
RT "Purification and characterization of a hydroperoxidase from the
RT cyanobacterium Synechocystis PCC 6803: identification of its gene by
RT peptide mass mapping using matrix assisted laser desorption ionization
RT time-of-flight mass spectrometry.";
RL FEMS Microbiol. Lett. 170:1-12(1999).
RN [5]
RP COVALENT BOND.
RX PubMed=14527675; DOI=10.1016/s0014-5793(03)00901-3;
RA Jakopitsch C., Kolarich D., Petutschnig G., Furtmueller P.G., Obinger C.;
RT "Distal side tryptophan, tyrosine and methionine in catalase-peroxidases
RT are covalently linked in solution.";
RL FEBS Lett. 552:135-140(2003).
RN [6]
RP RADICAL INTERMEDIATE.
RX PubMed=14611246; DOI=10.1021/ja035582+;
RA Ivancich A., Jakopitsch C., Auer M., Un S., Obinger C.;
RT "Protein-based radicals in the catalase-peroxidase of synechocystis
RT PCC6803: a multifrequency EPR investigation of wild-type and variants on
RT the environment of the heme active site.";
RL J. Am. Chem. Soc. 125:14093-14102(2003).
RN [7]
RP RADICAL INTERMEDIATE.
RX PubMed=16574230; DOI=10.1016/j.jinorgbio.2006.02.009;
RA Jakopitsch C., Obinger C., Un S., Ivancich A.;
RT "Identification of Trp106 as the tryptophanyl radical intermediate in
RT Synechocystis PCC6803 catalase-peroxidase by multifrequency electron
RT paramagnetic resonance spectroscopy.";
RL J. Inorg. Biochem. 100:1091-1099(2006).
RN [8]
RP CATALYTIC MECHANISM.
RX PubMed=17260948; DOI=10.1021/bi062266+;
RA Jakopitsch C., Vlasits J., Wiseman B., Loewen P.C., Obinger C.;
RT "Redox intermediates in the catalase cycle of catalase-peroxidases from
RT Synechocystis PCC 6803, Burkholderia pseudomallei, and Mycobacterium
RT tuberculosis.";
RL Biochemistry 46:1183-1193(2007).
RN [9]
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=18178143; DOI=10.1016/j.abb.2007.12.008;
RA Singh R., Wiseman B., Deemagarn T., Jha V., Switala J., Loewen P.C.;
RT "Comparative study of catalase-peroxidases (KatGs).";
RL Arch. Biochem. Biophys. 471:207-214(2008).
CC -!- FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum
CC peroxidase activity. Also displays NADH oxidase, isoniazid hydrazine
CC lyase and isonicotinoyl-NAD synthase activities.
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 -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20 mM for H(2)O(2) for the catalase reaction (at pH 5.5-6.0)
CC {ECO:0000269|PubMed:10543446, ECO:0000269|PubMed:18178143,
CC ECO:0000269|PubMed:9919646};
CC KM=3.1 mM for H(2)O(2) for the catalase reaction (at pH 7.0)
CC {ECO:0000269|PubMed:10543446, ECO:0000269|PubMed:18178143,
CC ECO:0000269|PubMed:9919646};
CC KM=1000 uM for H(2)O(2) for the peroxidase reaction
CC {ECO:0000269|PubMed:10543446, ECO:0000269|PubMed:18178143,
CC ECO:0000269|PubMed:9919646};
CC KM=7 uM for ABTS for the peroxidase reaction
CC {ECO:0000269|PubMed:10543446, ECO:0000269|PubMed:18178143,
CC ECO:0000269|PubMed:9919646};
CC Vmax=6000 umol/min/mg enzyme for H(2)O(2) for the catalase reaction
CC (at pH 5.5-6.0) {ECO:0000269|PubMed:10543446,
CC ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:9919646};
CC Vmax=5400 umol/min/mg enzyme for H(2)O(2) for the catalase reaction
CC (at pH 7.0) {ECO:0000269|PubMed:10543446,
CC ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:9919646};
CC Vmax=9.3 umol/min/mg enzyme for ABTS for the peroxidase reaction
CC {ECO:0000269|PubMed:10543446, ECO:0000269|PubMed:18178143,
CC ECO:0000269|PubMed:9919646};
CC pH dependence:
CC Optimum pH is 4.25 for the peroxidase reaction and 6.5 for the
CC catalase reaction. {ECO:0000269|PubMed:10543446,
CC ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:9919646};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10543446,
CC ECO:0000269|PubMed:9919646}.
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 -!- MASS SPECTROMETRY: Mass=85122; Method=MALDI; Note=Reported mass
CC includes mass of a C-terminal His6 tag, expressed in E.coli.;
CC Evidence={ECO:0000269|PubMed:10543446};
CC -!- MISCELLANEOUS: In contrast to the M.tuberculosis enzyme, no Trp radical
CC is formed on the proximal Trp residue (Trp-341).
CC -!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
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DR EMBL; D83990; BAA20459.1; -; Genomic_DNA.
DR EMBL; BA000022; BAA17975.1; -; Genomic_DNA.
DR PIR; S75113; S75113.
DR AlphaFoldDB; P73911; -.
DR SMR; P73911; -.
DR IntAct; P73911; 8.
DR STRING; 1148.1653058; -.
DR PeroxiBase; 2479; SYspCP01_PCC6803.
DR PaxDb; P73911; -.
DR EnsemblBacteria; BAA17975; BAA17975; BAA17975.
DR KEGG; syn:sll1987; -.
DR eggNOG; COG0376; Bacteria.
DR InParanoid; P73911; -.
DR OMA; MILAGNC; -.
DR PhylomeDB; P73911; -.
DR BRENDA; 1.11.1.21; 382.
DR SABIO-RK; P73911; -.
DR Proteomes; UP000001425; 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 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 Heme; Hydrogen peroxide; Iron; Metal-binding; Organic radical;
KW Oxidoreductase; Peroxidase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..754
FT /note="Catalase-peroxidase"
FT /id="PRO_0000345096"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 106
FT /note="Tryptophan radical intermediate"
FT /evidence="ECO:0000269|PubMed:16574230,
FT ECO:0000269|PubMed:17260948"
FT ACT_SITE 123
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT BINDING 290
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 119
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01961"
FT CROSSLNK 122..249
FT /note="Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-
FT 275)"
FT CROSSLNK 249..275
FT /note="Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-
FT 122)"
SQ SEQUENCE 754 AA; 84446 MW; AC5709DB6468D4F7 CRC64;
MGTQPARKLR NRVFPHPHNH RKEKPMANDQ VPASKCPVMH GANTTGQNGN LNWWPNALNL
DILHQHDRKT NPMDDGFNYA EAFQQLDLAA VKQDLHHLMT DSQSWWPADW GHYGGLMIRM
AWHAAGTYRI ADGRGGAATG NQRFAPLNSW PDNVNLDKAR RLLWPIKKKY GNKLSWGDLI
ILAGTMAYES MGLKVYGFAG GREDIWHPEK DIYWGAEKEW LASSDHRYGS EDRESLENPL
AAVQMGLIYV NPEGVDGHPD PLCTAQDVRT TFARMAMNDE ETVALTAGGH TVGKCHGNSK
AELIGPEPEG ADVVEQGLGW HNQNGKGVGR ETMSSGIEGA WTTHPTQWDN GYFYMLFNHE
WELKKSPAGA WQWEPVNIKE EDKPVDVEDP NIRHNPIMTD ADMAMIKDPI YRQISERFYR
EPDYFAEVFA KAWFKLTHRD LGPKSRYLGP DVPQEDLIWQ DPIPPVDYTL SEGEIKELEQ
QILASGLTVS ELVCTAWDSA RTFRSSDYRG GANGARIRLE PQKNWPGNEP TRLAKVLAVL
ENIQANFAKP VSLADLIVLG GGAAIAKAAL DGGIEVNVPF LPGRGDATQA MTDAESFTPL
EPIHDGYRNW LKQDYAVSPE ELLLERTQLM GLTAPEMTVL IGGMRVLGTN HGGTKHGVFT
DRVGVLSNDF FVNLTDMAYQ WRPAGNNLYE IGDRQTGEVK WTATKVDLVF GSNSILRSYA
EVYAQDDNRE KFVRDFVAAW TKVMNADRFD LPRG
