P73911 (KATG_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Catalase-peroxidase
Short name=CP
EC=1.11.1.21

Alternative name(s):
Peroxidase/catalase

Gene names

Name:	katG
Ordered Locus Names:	sll1987

Organism

Synechocystis sp. (strain PCC 6803 / Kazusa)

Taxonomic identifier

1111708 [NCBI]

Taxonomic lineage

Bacteria › Cyanobacteria › Chroococcales › Synechocystis

Protein attributes

Sequence length	754 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Displays also NADH oxidase, isoniazid hydrazine lyase and isonicotinoyl-NAD synthase activity. HAMAP MF_01961
Catalytic activity	Donor + H2O2 = oxidized donor + 2 H2O. HAMAP MF_01961 2 H2O2 = O2 + 2 H2O. HAMAP MF_01961
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per dimer. Ref.3 Ref.4
Subunit structure	Homodimer. Ref.3 Ref.4
Post-translational modification	The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme. HAMAP MF_01961
Miscellaneous	In contrast to the M.tuberculosis enzyme, no Trp radical is formed on the proximal Trp residue (Trp-341). HAMAP MF_01961
Sequence similarities	Belongs to the peroxidase family. Peroxidase/catalase subfamily.
Biophysicochemical properties	Kinetic parameters: KM=20 mM for H2O2 for the catalase reaction (at pH 5.5-6.0) Ref.3 Ref.4 Ref.9 KM=3.1 mM for H2O2 for the catalase reaction (at pH 7.0) KM=1000 µM for H2O2 for the peroxidase reaction KM=7 µM for ABTS for the peroxidase reaction Vmax=6000 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 5.5-6.0) Vmax=5400 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 7.0) Vmax=9.3 µmol/min/mg enzyme for ABTS for the peroxidase reaction pH dependence: Optimum pH is 4.25 for the peroxidase reaction and 6.5 for the catalase reaction.
Mass spectrometry	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. Ref.3

Ontologies

Keywords
Biological process	Hydrogen peroxide
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Organic radical
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	catalase activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed HAMAP MF_01961
	Chain	2 – 754	753	Catalase-peroxidase HAMAP MF_01961		PRO_0000345096
Sites
	Active site	106	1	Tryptophan radical intermediate
	Active site	123	1	Proton acceptor By similarity
	Metal binding	290	1	Iron (heme axial ligand) By similarity
	Site	119	1	Transition state stabilizer By similarity
Amino acid modifications
	Cross-link	122 ↔ 249		Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-275) HAMAP MF_01961
	Cross-link	249 ↔ 275		Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-122) HAMAP MF_01961

Sequences

	Sequence		Length	Mass (Da)
	P73911 [UniParc]. Last modified February 1, 1997. Version 1. Checksum: AC5709DB6468D4F7	FASTA	754	84,446
	10 20 30 40 50 60 MGTQPARKLR NRVFPHPHNH RKEKPMANDQ VPASKCPVMH GANTTGQNGN LNWWPNALNL 70 80 90 100 110 120 DILHQHDRKT NPMDDGFNYA EAFQQLDLAA VKQDLHHLMT DSQSWWPADW GHYGGLMIRM 130 140 150 160 170 180 AWHAAGTYRI ADGRGGAATG NQRFAPLNSW PDNVNLDKAR RLLWPIKKKY GNKLSWGDLI 190 200 210 220 230 240 ILAGTMAYES MGLKVYGFAG GREDIWHPEK DIYWGAEKEW LASSDHRYGS EDRESLENPL 250 260 270 280 290 300 AAVQMGLIYV NPEGVDGHPD PLCTAQDVRT TFARMAMNDE ETVALTAGGH TVGKCHGNSK 310 320 330 340 350 360 AELIGPEPEG ADVVEQGLGW HNQNGKGVGR ETMSSGIEGA WTTHPTQWDN GYFYMLFNHE 370 380 390 400 410 420 WELKKSPAGA WQWEPVNIKE EDKPVDVEDP NIRHNPIMTD ADMAMIKDPI YRQISERFYR 430 440 450 460 470 480 EPDYFAEVFA KAWFKLTHRD LGPKSRYLGP DVPQEDLIWQ DPIPPVDYTL SEGEIKELEQ 490 500 510 520 530 540 QILASGLTVS ELVCTAWDSA RTFRSSDYRG GANGARIRLE PQKNWPGNEP TRLAKVLAVL 550 560 570 580 590 600 ENIQANFAKP VSLADLIVLG GGAAIAKAAL DGGIEVNVPF LPGRGDATQA MTDAESFTPL 610 620 630 640 650 660 EPIHDGYRNW LKQDYAVSPE ELLLERTQLM GLTAPEMTVL IGGMRVLGTN HGGTKHGVFT 670 680 690 700 710 720 DRVGVLSNDF FVNLTDMAYQ WRPAGNNLYE IGDRQTGEVK WTATKVDLVF GSNSILRSYA 730 740 750 EVYAQDDNRE KFVRDFVAAW TKVMNADRFD LPRG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 8905231] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 27184 / PCC 6803 / N-1.
[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: 10543446] [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: 9919646] [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: 14527675] [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: 14611246] [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: 16574230] [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: 17260948] [Abstract] Cited for: CATALYTIC MECHANISM.
[9]	"Comparative study of catalase-peroxidases (KatGs)." Singh R., Wiseman B., Deemagarn T., Jha V., Switala J., Loewen P.C. Arch. Biochem. Biophys. 471:207-214(2008) [PubMed: 18178143] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D83990 Genomic DNA. Translation: BAA20459.1. BA000022 Genomic DNA. Translation: BAA17975.1.
PIR	S75113.
RefSeq	NP_441295.1. NC_000911.1.
3D structure databases
HSSP	HSSP built from PDB template 1ITK based on UniProtKB O59651.
ProteinModelPortal	P73911.
SMR	P73911. Positions 53-751.
ModBase	Search...
Protein-protein interaction databases
IntAct	P73911. 8 interactions.
STRING	P73911.
Protein family/group databases
PeroxiBase	2479. SYspCP01_PCC6803.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	954640.
GenomeReviews	Gene locus sll1987 in contig BA000022_GR.
KEGG	syn:sll1987.
NMPDR	fig|1148.1.peg.1396.
PATRIC	23839946. VBISynSp132158_1534.
Phylogenomic databases
eggNOG	COG0376.
HOGENOM	HBG285610.
OMA	WPNALNL.
PhylomeDB	P73911.
ProtClustDB	PRK15061.
Enzyme and pathway databases
BioCyc	SSP1148:SLL1987-MONOMER.
Family and domain databases
HAMAP	MF_01961. Catal-peroxid. [Tree]
InterPro	IPR000763. Catalase_peroxidase. IPR010255. Haem_peroxidase. IPR002016. Haem_peroxidase_pln/fun/bac. IPR019794. Peroxidases_AS. [Graphical view]
KO	K03782.
Pfam	PF00141. peroxidase. 2 hits. [Graphical view]
PRINTS	PR00460. BPEROXIDASE. PR00458. PEROXIDASE.
SUPFAM	SSF48113. Peroxidase_super. 2 hits.
TIGRFAMs	TIGR00198. Cat_per_HPI. 1 hit.
PROSITE	PS00435. PEROXIDASE_1. False negative. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KATG_SYNY3

Accession

Primary (citable) accession number: P73911
Secondary accession number(s): P97083, Q79EX5

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 22, 2008
Last sequence update:	February 1, 1997
Last modified:	January 25, 2012
This is version 77 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program