Reviewed, UniProtKB/Swiss-Prot Q4F6N6 (KATG2_BURCJ)

Names and origin

Protein names

Recommended name:
    Catalase-peroxidase 2
      Short name=CP 2
    EC=1.11.1.6
    EC=1.11.1.7
Alternative name(s):
    Peroxidase/catalase 2

Gene names

Name:	katG2
Synonyms:	katA
Ordered Locus Names:	BceJ2315_55450
ORF Names:	BCAM2107

Organism

Burkholderia cepacia (strain J2315 / LMG 16656) (Burkholderia cenocepacia (strain J2315)) [Complete proteome] [HAMAP]

Taxonomic identifier

216591 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

Protein attributes

Sequence length	736 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Shows peroxidase specificity towards odianisidine, ABTS and pyrogallol, but methoxyphenol and 2-chloronaphthol are not peroxidized. Ref.1
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 dimer By similarity.
Subunit structure	Homodimer or homotetramer By similarity.
Post-translational modification	The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme By similarity.
Sequence similarities	Belongs to the peroxidase family. Peroxidase/catalase subfamily.
Biophysicochemical properties	pH dependence: Optimum pH is 5.5 for the peroxidase reaction and 6.0 for the catalase reaction. Active from pH 5.5 to 8.5. HAMAP MF_01961

Ontologies

Keywords
Biological process	Hydrogen peroxide
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	Complete proteome
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
	Chain	1 – 736	736	Catalase-peroxidase 2 HAMAP MF_01961		PRO_0000354740
Sites
	Active site	92	1	Proton acceptor By similarity
	Metal binding	268	1	Iron (heme axial ligand) By similarity
	Site	88	1	Transition state stabilizer By similarity
Amino acid modifications
	Cross-link	91 ↔ 227		Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-253) By similarity
	Cross-link	227 ↔ 253		Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-91) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q4F6N6-1 [UniParc]. Last modified August 30, 2005. Version 1. Checksum: 48CC314FEA9C30A3	FASTA	736	80,487
	10 20 30 40 50 60 MSNEGQCPFN HANGGGTTNR DWWPNELRLD LLSQHSSKTD PLDPGFNYAE AFNSLDLDAL 70 80 90 100 110 120 RKDLAALMTD SQDWWPADFG HYGPLFVRMA WHSAGTYRMG DGRGGAGRGQ QRFAPLNSWP 130 140 150 160 170 180 DNVSLDKARR LLWPIKQKYG QKISWADLLI LTGDVALTTM GFKTFGYAGG REDTWEPDRD 190 200 210 220 230 240 VYWGSETTWL GGDLRYDKGG ACESQHGGNA GRNLENPLAA VQMGLIYVNP EGPDGNPDPV 250 260 270 280 290 300 AAAYDIREVF GRMAMNDEET VALIAGGHAF GKTHGAGPAD NVGLEPEAAG LEQQGLGWKN 310 320 330 340 350 360 SFGTGKGADT ITSGLEVTWS DTPTQWGMGF FKNLFGYEWE LTKSPAGAHQ WVAKNAEPTI 370 380 390 400 410 420 PHAHDPSKKL LPTMLTTDLS LRFDPVYEKI SRHFMDNPDV FADAFARAWF KLTHRDMGPR 430 440 450 460 470 480 ARYLGPDVPT EELIWQDPIP AVDHVLVDDT DVAPLKETIL ASGLSVAELV STAWASASTF 490 500 510 520 530 540 RGSDKRGGAN GARIRLAPQK DWAVNEPARL AKVLKVLERI QGEFNSTQPG GKKISLADLI 550 560 570 580 590 600 VLAGGAGIEQ AAKRAGHDVV VPFAPGRMDA SQEQTDAHSF AVLEPVADGF RNFVKGKFAV 610 620 630 640 650 660 PAEALLIDKA QLLTLTAPQM TALVGGLRVL NVQTGDEKHG VFTDQPETLT VDFFRNLLDM 670 680 690 700 710 720 ATEWKPIAGE DTYEGRDRRT GELKWTGTRV DLVFGSNAVL RALSEVYASA DGEAKFIRDF 730 VAAWVKVMNL DRFDLA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a bifunctional catalase-peroxidase of Burkholderia cenocepacia." Charalabous P., Risk J.M., Jenkins R., Birss A.J., Hart C.A., Smalley J.W. FEMS Immunol. Med. Microbiol. 50:37-44(2007) [PubMed: 17371508] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[2]	"Genomic analysis of Burkholderia cenocepacia J2315, an epidemic cystic fibrosis pathogen." Holden M.T.G. Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	DQ112341 Genomic DNA. Translation: AAZ14051.1. AM747721 Genomic DNA. Translation: CAR55964.1.
RefSeq	YP_002234708.1.
3D structure databases
SMR	Q4F6N6. Positions 14-735.
ModBase	Search...
Protein family/group databases
PeroxiBase	2309. BcenCP01_J2315.
Genome annotation databases
GeneID	6929708.
GenomeReviews	Gene locus BceJ2315_55450 in contig AM747721_GR.
KEGG	bcj:BCAM2107.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	Q4F6N6. TLTAPQM.
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

KATG2_BURCJ

Accession

Primary (citable) accession number: Q4F6N6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2008
Last sequence update:	August 30, 2005
Last modified:	June 16, 2009
This is version 30 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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