Reviewed, UniProtKB/Swiss-Prot Q939D2 (KATG_BURPS)

Names and origin

Protein names

Recommended name:
    Catalase-peroxidase
      Short name=CP
    EC=1.11.1.6
    EC=1.11.1.7
Alternative name(s):
    Peroxidase/catalase

Gene names

Name:	katG
Ordered Locus Names:	BPSL2865

Organism

Burkholderia pseudomallei (Pseudomonas pseudomallei) [Complete proteome] [HAMAP]

Taxonomic identifier

28450 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length	728 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. Ref.4
Catalytic activity	2 H2O2 = O2 + 2 H2O. HAMAP MF_01961 Donor + H2O2 = oxidized donor + 2 H2O. HAMAP MF_01961
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit. HAMAP MF_01961
Subunit structure	Homodimer. Ref.7 Ref.8 Ref.9
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
Sequence similarities	Belongs to the peroxidase family. Peroxidase/catalase subfamily.
biophysicochemical properties	Kinetic parameters: KM=56 mM for H2O2 for the catalase reaction (at pH 5.5-6.0) HAMAP MF_01961 KM=4.5 mM for H2O2 for the catalase reaction (at pH 7.0) KM=700 µM for H2O2 for the peroxidase reaction KM=300 µM for ABTS for the peroxidase reaction KM=12.5 µM for NADH for the oxidase reaction Vmax=11900 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 5.5-6.0) Vmax=4300 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 7.0) Vmax=6.0 µmol/min/mg enzyme for ABTS for the peroxidase reaction pH dependence: Optimum pH is 4.5 for the peroxidase reaction, 6.0 for the catalase reaction, and 8.75 for the NADH oxidase reaction.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	catalase activity Inferred from electronic annotation. Source: HAMAP 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 Ref.3
	Chain	2 – 728	727	Catalase-peroxidase HAMAP MF_01961		PRO_0000345092
Sites
	Active site	92	1	Proton acceptor HAMAP MF_01961
	Metal binding	259	1	Iron (heme axial ligand) HAMAP MF_01961
	Site	88	1	Transition state stabilizer HAMAP MF_01961
Amino acid modifications
	Cross-link	91 ↔ 218		Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-244) HAMAP MF_01961
	Cross-link	218 ↔ 244		Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91) HAMAP MF_01961

Sequences

	Sequence		Length	Mass (Da)
	Q939D2-1 [UniParc]. Last modified July 22, 2008. Version 3. Checksum: FB6EC6E5261F6740	FASTA	728	79,446
	10 20 30 40 50 60 MSNEAKCPFH QAAGNGTSNR DWWPNQLDLS ILHRHSSLSD PMGKDFNYAQ AFEKLDLAAV 70 80 90 100 110 120 KRDLHALMTT SQDWWPADFG HYGGLFIRMA WHSAGTYRTA DGRGGAGEGQ QRFAPLNSWP 130 140 150 160 170 180 DNANLDKARR LLWPIKQKYG RAISWADLLI LTGNVALESM GFKTFGFAGG RADTWEPEDV 190 200 210 220 230 240 YWGSEKIWLE LSGGPNSRYS GDRQLENPLA AVQMGLIYVN PEGPDGNPDP VAAARDIRDT 250 260 270 280 290 300 FARMAMNDEE TVALIAGGHT FGKTHGAGPA SNVGAEPEAA GIEAQGLGWK SAYRTGKGAD 310 320 330 340 350 360 AITSGLEVTW TTTPTQWSHN FFENLFGYEW ELTKSPAGAH QWVAKGADAV IPDAFDPSKK 370 380 390 400 410 420 HRPTMLTTDL SLRFDPAYEK ISRRFHENPE QFADAFARAW FKLTHRDMGP RARYLGPEVP 430 440 450 460 470 480 AEVLLWQDPI PAVDHPLIDA ADAAELKAKV LASGLTVSQL VSTAWAAAST FRGSDKRGGA 490 500 510 520 530 540 NGARIRLAPQ KDWEANQPEQ LAAVLETLEA IRTAFNGAQR GGKQVSLADL IVLAGCAGVE 550 560 570 580 590 600 QAAKNAGHAV TVPFAPGRAD ASQEQTDVES MAVLEPVADG FRNYLKGKYR VPAEVLLVDK 610 620 630 640 650 660 AQLLTLSAPE MTVLLGGLRV LGANVGQSRH GVFTAREQAL TNDFFVNLLD MGTEWKPTAA 670 680 690 700 710 720 DADVFEGRDR ATGELKWTGT RVDLVFGSHS QLRALAEVYG SADAQEKFVR DFVAVWNKVM NLDRFDLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Burkholderia pseudomallei oxyR gene: expression analysis and mutant characterization." Loprasert S., Sallabhan R., Whangsuk W., Mongkolsuk S. Gene 296:161-169(2002) [PubMed: 12383513] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genomic plasticity of the causative agent of melioidosis, Burkholderia pseudomallei." Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A., Brown N.F., Challis G.L. , Cherevach I., Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S., Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J. Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004) [PubMed: 15377794] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K96243.
[3]	"Characterization of the catalase-peroxidase KatG from Burkholderia pseudomallei by mass spectrometry." Donald L.J., Krokhin O.V., Duckworth H.W., Wiseman B., Deemagarn T., Singh R., Switala J., Carpena X., Fita I., Loewen P.C. J. Biol. Chem. 278:35687-35692(2003) [PubMed: 12832453] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-5, COVALENT BOND.
[4]	"Catalase-peroxidases (KatG) exhibit NADH oxidase activity." Singh R., Wiseman B., Deemagarn T., Donald L.J., Duckworth H.W., Carpena X., Fita I., Loewen P.C. J. Biol. Chem. 279:43098-43106(2004) [PubMed: 15280362] [Abstract] Cited for: FUNCTION.
[5]	"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.
[6]	"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.
[7]	"Catalase-peroxidase KatG of Burkholderia pseudomallei at 1.7A resolution." Carpena X., Loprasert S., Mongkolsuk S., Switala J., Loewen P.C., Fita I. J. Mol. Biol. 327:475-489(2003) [PubMed: 12628252] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 15-728 IN COMPLEX WITH HEME, SUBUNIT.
[8]	"Structural characterization of the Ser324Thr variant of the catalase-peroxidase (KatG) from Burkholderia pseudomallei." Deemagarn T., Carpena X., Singh R., Wiseman B., Fita I., Loewen P.C. J. Mol. Biol. 345:21-28(2005) [PubMed: 15567407] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT THR-304 IN COMPLEX WITH HEME, SUBUNIT.
[9]	"A molecular switch and electronic circuit modulate catalase activity in catalase-peroxidases." Carpena X., Wiseman B., Deemagarn T., Singh R., Switala J., Ivancich A., Fita I., Loewen P.C. EMBO Rep. 6:1156-1162(2005) [PubMed: 16211084] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH HEME, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AY040244 Genomic DNA. Translation: AAK72466.3. Different initiation.
BX571965 Genomic DNA. Translation: CAH36875.1. Different initiation.

RefSeq

YP_109459.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1MWV	X-ray	1.70	A/B	15-728	[»]
1X7U	X-ray	1.90	A/B	1-728	[»]
2B2O	X-ray	1.90	A/B	15-728	[»]
2B2Q	X-ray	2.05	A/B	15-728	[»]
2B2R	X-ray	1.90	A/B	15-728	[»]
2B2S	X-ray	2.00	A/B	15-728	[»]
2DV1	X-ray	1.80	A/B	1-728	[»]
2DV2	X-ray	2.15	A/B	1-728	[»]
2FXG	X-ray	2.00	A/B	1-728	[»]
2FXH	X-ray	1.90	A/B	1-728	[»]
2FXJ	X-ray	1.95	A/B	1-728	[»]

ModBase

Search...

Protein family/group databases

PeroxiBase

2303. BpCP01.

Genome annotation databases

GeneID

3092072.

GenomeReviews

Gene locus BPSL2865 in contig BX571965_GR.

KEGG

bps:BPSL2865.

Organism-specific databases

CMR

Search...

Phylogenomic databases

HOGENOM

Q939D2.

Enzyme and pathway databases

BioCyc

BPSE272560:BPSL2865-MON.

BRENDA

1.11.1.6. 275934.

Family and domain databases

HAMAP

MF_01961.
[Tree]

InterPro

IPR000763. Catalase_proxase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]

Pfam

PF00141. peroxidase. 2 hits.
[Graphical view]

PRINTS

PR00460. BPEROXIDASE.
PR00458. PEROXIDASE.

TIGRFAMs

TIGR00198. cat_per_HPI. 1 hit.

PROSITE

PS00435. PEROXIDASE_1. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

KATG_BURPS

Accession

Primary (citable) accession number: Q939D2
Secondary accession number(s): Q63R09

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 22, 2008
Last sequence update:	July 22, 2008
Last modified:	May 26, 2009
This is version 57 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)