Catalase-peroxidase - Burkholderia pseudomallei

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Q939D2 (KATG_BURPS) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 75. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

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:	BPSL2865

Organism

Burkholderia pseudomallei (Pseudomonas pseudomallei)

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	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 subunit.
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: K_M=56 mM for H₂O₂ for the catalase reaction (at pH 5.5-6.0) Ref.6 Ref.9 K_M=4.5 mM for H₂O₂ for the catalase reaction (at pH 7.0) K_M=700 µM for H₂O₂ for the peroxidase reaction K_M=300 µM for ABTS for the peroxidase reaction K_M=12.5 µM for NADH for the oxidase reaction V_max=11900 µmol/min/mg enzyme for H₂O₂ for the catalase reaction (at pH 5.5-6.0) V_max=4300 µmol/min/mg enzyme for H₂O₂ for the catalase reaction (at pH 7.0) V_max=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.
Sequence caution	The sequence AAK72466.3 differs from that shown. Reason: Erroneous initiation. The sequence CAH36875.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	3D-structure Complete proteome Direct protein sequencing 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

Removed Ref.3

Chain

2 – 728

727

Catalase-peroxidase HAMAP MF_01961

PRO_0000345092

Sites

Active site

Proton acceptor

Metal binding

259

Iron (heme axial ligand)

Site

Transition state stabilizer

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

Secondary structure

728

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

Q939D2 [UniParc].

Last modified July 22, 2008. Version 3.
Checksum: FB6EC6E5261F6740
Show »

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

« Hide

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. 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

EMBL
GenBank
DDBJ

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

RefSeq

YP_109459.1. NC_006350.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q939D2.

SMR

Q939D2. Positions 14-728.

ModBase

Search...

Protein family/group databases

PeroxiBase

2303. BpCP01_K96243.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3092072.

GenomeReviews

Gene locus BPSL2865 in contig BX571965_GR.

KEGG

bps:BPSL2865.

PATRIC

19266145. VBIBurPse99623_3268.

Phylogenomic databases

HOGENOM

HBG285610.

OMA

KRHAPSM.

ProtClustDB

PRK15061.

Enzyme and pathway databases

BioCyc

BPSE272560:BPSL2865-MONOMER.

BRENDA

1.11.1.6. 1031.

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.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]

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. 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:	January 25, 2012
This is version 75 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents