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Protein

Catalase-peroxidase

Gene

katG

Organism
Synechocystis sp. (strain PCC 6803 / Kazusa)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Displays also NADH oxidase, isoniazid hydrazine lyase and isonicotinoyl-NAD synthase activity.

Catalytic activityi

Donor + H2O2 = oxidized donor + 2 H2O.UniRule annotation
2 H2O2 = O2 + 2 H2O.UniRule annotation

Cofactori

heme bNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer.

Kineticsi

  1. KM=20 mM for H2O2 for the catalase reaction (at pH 5.5-6.0)3 Publications
  2. KM=3.1 mM for H2O2 for the catalase reaction (at pH 7.0)3 Publications
  3. KM=1000 µM for H2O2 for the peroxidase reaction3 Publications
  4. KM=7 µM for ABTS for the peroxidase reaction3 Publications
  1. Vmax=6000 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 5.5-6.0)3 Publications
  2. Vmax=5400 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 7.0)3 Publications
  3. Vmax=9.3 µmol/min/mg enzyme for ABTS for the peroxidase reaction3 Publications

pH dependencei

Optimum pH is 4.25 for the peroxidase reaction and 6.5 for the catalase reaction.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei106 – 1061Tryptophan radical intermediate
Sitei119 – 1191Transition state stabilizerUniRule annotation
Active sitei123 – 1231Proton acceptorUniRule annotation
Metal bindingi290 – 2901Iron (heme axial ligand)UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Hydrogen peroxide

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

BRENDAi1.11.1.21. 382.
SABIO-RKP73911.

Protein family/group databases

PeroxiBasei2479. SYspCP01_PCC6803.

Names & Taxonomyi

Protein namesi
Recommended name:
Catalase-peroxidaseUniRule annotation (EC:1.11.1.21UniRule annotation)
Short name:
CPUniRule annotation
Alternative name(s):
Peroxidase/catalaseUniRule annotation
Gene namesi
Name:katGUniRule annotation
Ordered Locus Names:sll1987
OrganismiSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifieri1111708 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechocystis
Proteomesi
  • UP000001425 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 754753Catalase-peroxidasePRO_0000345096Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki122 ↔ 249Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-275)
Cross-linki249 ↔ 275Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-122)

Post-translational modificationi

The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme.

Keywords - PTMi

Organic radical

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

IntActiP73911. 8 interactions.

Structurei

3D structure databases

ProteinModelPortaliP73911.
SMRiP73911. Positions 53-751.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peroxidase family. Peroxidase/catalase subfamily.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000218110.
InParanoidiP73911.
KOiK03782.
OMAiTESKCPF.
OrthoDBiEOG6RRKKM.
PhylomeDBiP73911.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid.
InterProiIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
[Graphical view]
PfamiPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 2 hits.
TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
PROSITEiPS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P73911-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGTQPARKLR NRVFPHPHNH RKEKPMANDQ VPASKCPVMH GANTTGQNGN
60 70 80 90 100
LNWWPNALNL DILHQHDRKT NPMDDGFNYA EAFQQLDLAA VKQDLHHLMT
110 120 130 140 150
DSQSWWPADW GHYGGLMIRM AWHAAGTYRI ADGRGGAATG NQRFAPLNSW
160 170 180 190 200
PDNVNLDKAR RLLWPIKKKY GNKLSWGDLI ILAGTMAYES MGLKVYGFAG
210 220 230 240 250
GREDIWHPEK DIYWGAEKEW LASSDHRYGS EDRESLENPL AAVQMGLIYV
260 270 280 290 300
NPEGVDGHPD PLCTAQDVRT TFARMAMNDE ETVALTAGGH TVGKCHGNSK
310 320 330 340 350
AELIGPEPEG ADVVEQGLGW HNQNGKGVGR ETMSSGIEGA WTTHPTQWDN
360 370 380 390 400
GYFYMLFNHE WELKKSPAGA WQWEPVNIKE EDKPVDVEDP NIRHNPIMTD
410 420 430 440 450
ADMAMIKDPI YRQISERFYR EPDYFAEVFA KAWFKLTHRD LGPKSRYLGP
460 470 480 490 500
DVPQEDLIWQ DPIPPVDYTL SEGEIKELEQ QILASGLTVS ELVCTAWDSA
510 520 530 540 550
RTFRSSDYRG GANGARIRLE PQKNWPGNEP TRLAKVLAVL ENIQANFAKP
560 570 580 590 600
VSLADLIVLG GGAAIAKAAL DGGIEVNVPF LPGRGDATQA MTDAESFTPL
610 620 630 640 650
EPIHDGYRNW LKQDYAVSPE ELLLERTQLM GLTAPEMTVL IGGMRVLGTN
660 670 680 690 700
HGGTKHGVFT DRVGVLSNDF FVNLTDMAYQ WRPAGNNLYE IGDRQTGEVK
710 720 730 740 750
WTATKVDLVF GSNSILRSYA EVYAQDDNRE KFVRDFVAAW TKVMNADRFD

LPRG
Length:754
Mass (Da):84,446
Last modified:February 1, 1997 - v1
Checksum:iAC5709DB6468D4F7
GO

Mass spectrometryi

Molecular mass is 85122 Da from positions 2 - 754. Determined by MALDI. Reported mass includes mass of a C-terminal His6 tag, expressed in E.coli.1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83990 Genomic DNA. Translation: BAA20459.1.
BA000022 Genomic DNA. Translation: BAA17975.1.
PIRiS75113.

Genome annotation databases

EnsemblBacteriaiBAA17975; BAA17975; BAA17975.
KEGGisyn:sll1987.
PATRICi23839946. VBISynSp132158_1534.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83990 Genomic DNA. Translation: BAA20459.1.
BA000022 Genomic DNA. Translation: BAA17975.1.
PIRiS75113.

3D structure databases

ProteinModelPortaliP73911.
SMRiP73911. Positions 53-751.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP73911. 8 interactions.

Protein family/group databases

PeroxiBasei2479. SYspCP01_PCC6803.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA17975; BAA17975; BAA17975.
KEGGisyn:sll1987.
PATRICi23839946. VBISynSp132158_1534.

Phylogenomic databases

HOGENOMiHOG000218110.
InParanoidiP73911.
KOiK03782.
OMAiTESKCPF.
OrthoDBiEOG6RRKKM.
PhylomeDBiP73911.

Enzyme and pathway databases

BRENDAi1.11.1.21. 382.
SABIO-RKP73911.

Family and domain databases

HAMAPiMF_01961. Catal_peroxid.
InterProiIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
[Graphical view]
PfamiPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSiPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMiSSF48113. SSF48113. 2 hits.
TIGRFAMsiTIGR00198. cat_per_HPI. 1 hit.
PROSITEiPS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Nucleotide sequence of katG of Synechocystis sp. PCC 6803."
    Ushimaru T., Hayashi H., Murata N.
    Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "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."
    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.
    DNA Res. 3:109-136(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PCC 6803 / Kazusa.
  3. "Catalase-peroxidase from the cyanobacterium Synechocystis PCC 6803: cloning, overexpression in Escherichia coli, and kinetic characterization."
    Jakopitsch C., Ruker F., Regelsberger G., Dockal M., Peschek G.A., Obinger C.
    Biol. Chem. 380:1087-1096(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, HEME-BINDING, SUBUNIT, MASS SPECTROMETRY.
  4. "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."
    Regelsberger G., Obinger C., Zoder R., Altmann F., Peschek G.A.
    FEMS Microbiol. Lett. 170:1-12(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: BIOPHYSICOCHEMICAL PROPERTIES, HEME-BINDING, SUBUNIT.
  5. "Distal side tryptophan, tyrosine and methionine in catalase-peroxidases are covalently linked in solution."
    Jakopitsch C., Kolarich D., Petutschnig G., Furtmueller P.G., Obinger C.
    FEBS Lett. 552:135-140(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: COVALENT BOND.
  6. "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."
    Ivancich A., Jakopitsch C., Auer M., Un S., Obinger C.
    J. Am. Chem. Soc. 125:14093-14102(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: RADICAL INTERMEDIATE.
  7. "Identification of Trp106 as the tryptophanyl radical intermediate in Synechocystis PCC6803 catalase-peroxidase by multifrequency electron paramagnetic resonance spectroscopy."
    Jakopitsch C., Obinger C., Un S., Ivancich A.
    J. Inorg. Biochem. 100:1091-1099(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: RADICAL INTERMEDIATE.
  8. "Redox intermediates in the catalase cycle of catalase-peroxidases from Synechocystis PCC 6803, Burkholderia pseudomallei, and Mycobacterium tuberculosis."
    Jakopitsch C., Vlasits J., Wiseman B., Loewen P.C., Obinger C.
    Biochemistry 46:1183-1193(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC MECHANISM.
  9. Cited for: BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiKATG_SYNY3
AccessioniPrimary (citable) accession number: P73911
Secondary accession number(s): P97083, Q79EX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: February 1, 1997
Last modified: July 6, 2016
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

In contrast to the M.tuberculosis enzyme, no Trp radical is formed on the proximal Trp residue (Trp-341).

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Synechocystis PCC 6803
    Synechocystis (strain PCC 6803): entries and gene names

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.