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Catalase-peroxidase (CP) (EC 1.11.1.21) (Peroxidase/catalase)

 KATG_SYNY3              Reviewed;         754 AA.
P73911; P97083; Q79EX5;
22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
23-MAY-2018, entry version 122.
RecName: Full=Catalase-peroxidase {ECO:0000255|HAMAP-Rule:MF_01961};
Short=CP {ECO:0000255|HAMAP-Rule:MF_01961};
EC=1.11.1.21 {ECO:0000255|HAMAP-Rule:MF_01961};
AltName: Full=Peroxidase/catalase {ECO:0000255|HAMAP-Rule:MF_01961};
Name=katG {ECO:0000255|HAMAP-Rule:MF_01961};
OrderedLocusNames=sll1987;
Synechocystis sp. (strain PCC 6803 / Kazusa).
Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae;
Synechocystis.
NCBI_TaxID=1111708;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Ushimaru T., Hayashi H., Murata N.;
"Nucleotide sequence of katG of Synechocystis sp. PCC 6803.";
Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=PCC 6803 / Kazusa;
PubMed=8905231; DOI=10.1093/dnares/3.3.109;
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T.,
Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S.,
Shimpo S., Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M.,
Tabata S.;
"Sequence analysis of the genome of the unicellular cyanobacterium
Synechocystis sp. strain PCC6803. II. Sequence determination of the
entire genome and assignment of potential protein-coding regions.";
DNA Res. 3:109-136(1996).
[3]
BIOPHYSICOCHEMICAL PROPERTIES, HEME-BINDING, SUBUNIT, AND MASS
SPECTROMETRY.
PubMed=10543446; DOI=10.1515/BC.1999.135;
Jakopitsch C., Ruker F., Regelsberger G., Dockal M., Peschek G.A.,
Obinger C.;
"Catalase-peroxidase from the cyanobacterium Synechocystis PCC 6803:
cloning, overexpression in Escherichia coli, and kinetic
characterization.";
Biol. Chem. 380:1087-1096(1999).
[4]
BIOPHYSICOCHEMICAL PROPERTIES, HEME-BINDING, AND SUBUNIT.
PubMed=9919646; DOI=10.1111/j.1574-6968.1999.tb13348.x;
Regelsberger G., Obinger C., Zoder R., Altmann F., Peschek G.A.;
"Purification and characterization of a hydroperoxidase from the
cyanobacterium Synechocystis PCC 6803: identification of its gene by
peptide mass mapping using matrix assisted laser desorption ionization
time-of-flight mass spectrometry.";
FEMS Microbiol. Lett. 170:1-12(1999).
[5]
COVALENT BOND.
PubMed=14527675; DOI=10.1016/S0014-5793(03)00901-3;
Jakopitsch C., Kolarich D., Petutschnig G., Furtmueller P.G.,
Obinger C.;
"Distal side tryptophan, tyrosine and methionine in catalase-
peroxidases are covalently linked in solution.";
FEBS Lett. 552:135-140(2003).
[6]
RADICAL INTERMEDIATE.
PubMed=14611246; DOI=10.1021/ja035582+;
Ivancich A., Jakopitsch C., Auer M., Un S., Obinger C.;
"Protein-based radicals in the catalase-peroxidase of synechocystis
PCC6803: a multifrequency EPR investigation of wild-type and variants
on the environment of the heme active site.";
J. Am. Chem. Soc. 125:14093-14102(2003).
[7]
RADICAL INTERMEDIATE.
PubMed=16574230; DOI=10.1016/j.jinorgbio.2006.02.009;
Jakopitsch C., Obinger C., Un S., Ivancich A.;
"Identification of Trp106 as the tryptophanyl radical intermediate in
Synechocystis PCC6803 catalase-peroxidase by multifrequency electron
paramagnetic resonance spectroscopy.";
J. Inorg. Biochem. 100:1091-1099(2006).
[8]
CATALYTIC MECHANISM.
PubMed=17260948; DOI=10.1021/bi062266+;
Jakopitsch C., Vlasits J., Wiseman B., Loewen P.C., Obinger C.;
"Redox intermediates in the catalase cycle of catalase-peroxidases
from Synechocystis PCC 6803, Burkholderia pseudomallei, and
Mycobacterium tuberculosis.";
Biochemistry 46:1183-1193(2007).
[9]
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=18178143; DOI=10.1016/j.abb.2007.12.008;
Singh R., Wiseman B., Deemagarn T., Jha V., Switala J., Loewen P.C.;
"Comparative study of catalase-peroxidases (KatGs).";
Arch. Biochem. Biophys. 471:207-214(2008).
-!- FUNCTION: Bifunctional enzyme with both catalase and broad-
spectrum peroxidase activity. Displays also NADH oxidase,
isoniazid hydrazine lyase and isonicotinoyl-NAD synthase activity.
-!- CATALYTIC ACTIVITY: Donor + H(2)O(2) = oxidized donor + 2 H(2)O.
{ECO:0000255|HAMAP-Rule:MF_01961}.
-!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
{ECO:0000255|HAMAP-Rule:MF_01961}.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.;
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=20 mM for H(2)O(2) for the catalase reaction (at pH 5.5-6.0)
{ECO:0000269|PubMed:10543446, ECO:0000269|PubMed:18178143,
ECO:0000269|PubMed:9919646};
KM=3.1 mM for H(2)O(2) for the catalase reaction (at pH 7.0)
{ECO:0000269|PubMed:10543446, ECO:0000269|PubMed:18178143,
ECO:0000269|PubMed:9919646};
KM=1000 uM for H(2)O(2) for the peroxidase reaction
{ECO:0000269|PubMed:10543446, ECO:0000269|PubMed:18178143,
ECO:0000269|PubMed:9919646};
KM=7 uM for ABTS for the peroxidase reaction
{ECO:0000269|PubMed:10543446, ECO:0000269|PubMed:18178143,
ECO:0000269|PubMed:9919646};
Vmax=6000 umol/min/mg enzyme for H(2)O(2) for the catalase
reaction (at pH 5.5-6.0) {ECO:0000269|PubMed:10543446,
ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:9919646};
Vmax=5400 umol/min/mg enzyme for H(2)O(2) for the catalase
reaction (at pH 7.0) {ECO:0000269|PubMed:10543446,
ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:9919646};
Vmax=9.3 umol/min/mg enzyme for ABTS for the peroxidase reaction
{ECO:0000269|PubMed:10543446, ECO:0000269|PubMed:18178143,
ECO:0000269|PubMed:9919646};
pH dependence:
Optimum pH is 4.25 for the peroxidase reaction and 6.5 for the
catalase reaction. {ECO:0000269|PubMed:10543446,
ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:9919646};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10543446,
ECO:0000269|PubMed:9919646}.
-!- PTM: Formation of the three residue Trp-Tyr-Met cross-link is
important for the catalase, but not the peroxidase activity of the
enzyme. {ECO:0000255|HAMAP-Rule:MF_01961}.
-!- MASS SPECTROMETRY: Mass=85122; Method=MALDI; Range=2-754;
Note=Reported mass includes mass of a C-terminal His6 tag,
expressed in E.coli.; Evidence={ECO:0000269|PubMed:10543446};
-!- MISCELLANEOUS: In contrast to the M.tuberculosis enzyme, no Trp
radical is formed on the proximal Trp residue (Trp-341).
-!- SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase
subfamily. {ECO:0000255|HAMAP-Rule:MF_01961}.
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EMBL; D83990; BAA20459.1; -; Genomic_DNA.
EMBL; BA000022; BAA17975.1; -; Genomic_DNA.
PIR; S75113; S75113.
ProteinModelPortal; P73911; -.
SMR; P73911; -.
IntAct; P73911; 8.
STRING; 1148.SYNGTS_1399; -.
PeroxiBase; 2479; SYspCP01_PCC6803.
PaxDb; P73911; -.
PRIDE; P73911; -.
EnsemblBacteria; BAA17975; BAA17975; BAA17975.
KEGG; syn:sll1987; -.
HOGENOM; HOG000218110; -.
InParanoid; P73911; -.
KO; K03782; -.
OMA; PEEDIYW; -.
PhylomeDB; P73911; -.
BRENDA; 1.11.1.21; 382.
SABIO-RK; P73911; -.
Proteomes; UP000001425; Chromosome.
GO; GO:0005829; C:cytosol; IBA:GO_Central.
GO; GO:0005576; C:extracellular region; IBA:GO_Central.
GO; GO:0004096; F:catalase activity; IBA:GO_Central.
GO; GO:0020037; F:heme binding; IBA:GO_Central.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IBA:GO_Central.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IBA:GO_Central.
HAMAP; MF_01961; Catal_peroxid; 1.
InterPro; IPR000763; Catalase_peroxidase.
InterPro; IPR010255; Haem_peroxidase.
InterPro; IPR002016; Haem_peroxidase_pln/fun/bac.
InterPro; IPR019794; Peroxidases_AS.
PANTHER; PTHR30555; PTHR30555; 1.
Pfam; PF00141; peroxidase; 2.
PRINTS; PR00460; BPEROXIDASE.
PRINTS; PR00458; PEROXIDASE.
SUPFAM; SSF48113; SSF48113; 2.
TIGRFAMs; TIGR00198; cat_per_HPI; 1.
PROSITE; PS00436; PEROXIDASE_2; 1.
PROSITE; PS50873; PEROXIDASE_4; 2.
1: Evidence at protein level;
Complete proteome; Heme; Hydrogen peroxide; Iron; Metal-binding;
Organic radical; Oxidoreductase; Peroxidase; Reference proteome.
INIT_MET 1 1 Removed.
CHAIN 2 754 Catalase-peroxidase.
/FTId=PRO_0000345096.
ACT_SITE 106 106 Tryptophan radical intermediate.
{ECO:0000269|PubMed:16574230,
ECO:0000269|PubMed:17260948}.
ACT_SITE 123 123 Proton acceptor. {ECO:0000255|HAMAP-
Rule:MF_01961}.
METAL 290 290 Iron (heme axial ligand).
{ECO:0000255|HAMAP-Rule:MF_01961}.
SITE 119 119 Transition state stabilizer.
{ECO:0000255|HAMAP-Rule:MF_01961}.
CROSSLNK 122 249 Tryptophyl-tyrosyl-methioninium (Trp-Tyr)
(with M-275).
CROSSLNK 249 275 Tryptophyl-tyrosyl-methioninium (Tyr-Met)
(with W-122).
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


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