Q939D2 (KATG_BURPS) 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:	BPSL2865

Organism

Burkholderia pseudomallei (strain K96243) [Reference proteome] [HAMAP]

Taxonomic identifier

272560 [NCBI]

Taxonomic lineage

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

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-Rule MF_01961 2 H2O2 = O2 + 2 H2O. HAMAP-Rule 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-Rule 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) Ref.6 Ref.9 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.
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: HAMAP heme binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
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-Rule MF_01961

PRO_0000345092

Sites

Active site

92

1

Proton acceptor

Metal binding

259

1

Iron (heme axial ligand)

Site

88

1

Transition state stabilizer

Amino acid modifications

Cross-link

91 ↔ 218

Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-244) HAMAP-Rule MF_01961

Cross-link

218 ↔ 244

Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91) HAMAP-Rule MF_01961

Secondary structure

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728

Helix Strand Turn

Details...

Helix

19 – 22

4

Helix

29 – 32

4

Helix

37 – 39

3

Helix

48 – 53

6

Helix

57 – 68

12

Helix

78 – 80

3

Helix

83 – 94

12

Turn

99 – 101

3

Helix

110 – 112

3

Helix

116 – 118

3

Helix

120 – 122

3

Helix

125 – 131

7

Helix

133 – 139

7

Helix

140 – 142

3

Helix

145 – 159

15

Beta strand

192 – 194

3

Beta strand

198 – 200

3

Turn

201 – 203

3

Beta strand

211 – 213

3

Beta strand

217 – 219

3

Helix

224 – 226

3

Helix

230 – 242

13

Turn

243 – 245

3

Helix

248 – 258

11

Beta strand

266 – 268

3

Helix

270 – 272

3

Helix

277 – 279

3

Helix

282 – 284

3

Helix

298 – 300

3

Beta strand

302 – 305

4

Helix

320 – 327

8

Beta strand

330 – 334

5

Beta strand

340 – 344

5

Helix

367 – 374

8

Helix

376 – 387

12

Helix

389 – 405

17

Helix

411 – 413

3

Helix

425 – 427

3

Helix

440 – 452

13

Helix

457 – 468

12

Turn

473 – 475

3

Helix

484 – 486

3

Helix

490 – 492

3

Helix

494 – 496

3

Helix

498 – 517

20

Helix

527 – 545

19

Helix

563 – 565

3

Helix

568 – 571

4

Helix

572 – 574

3

Beta strand

577 – 579

3

Helix

580 – 582

3

Beta strand

584 – 587

4

Helix

593 – 603

11

Helix

608 – 621

14

Helix

625 – 627

3

Helix

643 – 648

6

Beta strand

653 – 657

5

Beta strand

664 – 669

6

Turn

670 – 672

3

Beta strand

675 – 680

6

Helix

681 – 684

4

Helix

685 – 687

3

Helix

690 – 699

10

Helix

705 – 720

16

Turn

721 – 723

3

Helix

725 – 727

3

Sequences

	Sequence		Length	Mass (Da)
	Q939D2 [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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-protein interaction databases

STRING

272560.BPSL2865.

Protein family/group databases

PeroxiBase

2303. BpCP01_K96243.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

3092072.

KEGG

bps:BPSL2865.

PATRIC

19266145. VBIBurPse99623_3268.

Phylogenomic databases

eggNOG

COG0376.

HOGENOM

HOG000218110.

KO

K03782.

OMA

KRHAPSM.

ProtClustDB

PRK15061.

Enzyme and pathway databases

BioCyc

BPSE272560:GJNI-2941-MONOMER.

BRENDA

1.11.1.6. 1031.

SABIO-RK

Q939D2.

Family and domain databases

HAMAP

MF_01961. Catal-peroxid.

InterPro

IPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
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.

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...

Other

EvolutionaryTrace

Q939D2.

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 1, 2013
This is version 84 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program