Reviewed, UniProtKB/Swiss-Prot Q9WXB9 (KATG2_LEGPN)

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

Organism

Legionella pneumophila

Taxonomic identifier

446 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Legionellales › Legionellaceae › Legionella

Protein attributes

Sequence length	749 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Important for stationary phase survival. 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. HAMAP MF_01961
Subunit structure	Homodimer or homotetramer By similarity. HAMAP MF_01961
Subcellular location	Periplasm Ref.1.
Induction	Induced during exponential growth and is the predominant peroxidase in stationary phase. Ref.1
Post-translational modification	The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme By similarity. HAMAP MF_01961
Sequence similarities	Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Periplasm
Domain	Signal
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
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
Cellular component	periplasmic space Inferred from electronic annotation. Source: UniProtKB-SubCell
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
	Signal peptide	1 – 27	27	Potential
	Chain	28 – 749	722	Catalase-peroxidase 2 HAMAP MF_01961		PRO_0000055569
Sites
	Active site	108	1	Proton acceptor By similarity
	Metal binding	270	1	Iron (heme axial ligand) By similarity
	Site	104	1	Transition state stabilizer By similarity
Amino acid modifications
	Cross-link	107 ↔ 229		Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-255) By similarity
	Cross-link	229 ↔ 255		Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-107) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9WXB9-1 [UniParc]. Last modified November 1, 1999. Version 1. Checksum: 19E7931C472973C8	FASTA	749	82,915
	10 20 30 40 50 60 MFKRTIPLFA AFTLAISPSI FPNYAHAQED KPKTNQYWWP KMLDLSPLRQ PNATSNPMGE 70 80 90 100 110 120 KFNYAEEFNS LDLNAVIEDL KKLMTTSQDW WPADYGNYGP LFIRMSWHAA GTYRIYDGRG 130 140 150 160 170 180 GANGGFQRFA PQNSWPDNAN LDKARRLLWP IKQKYGRKIS WADLLVLAGN VAMESMGFKT 190 200 210 220 230 240 IGFAGGREDA WEAININWGP EGKWLESKRQ DKDGKLEKPL AATVMGLIYV NPEGPNGVPD 250 260 270 280 290 300 PLAAAEKIRE TFGRMAMNDE ETVALIAGGH AFGKTHGAAS GKYLGPAPEA AGIEEQGFGW 310 320 330 340 350 360 KNSYGSGKGK DTITSGLEGA WTVTPTHWSH NYLQNLFNFN WVKTKSPGGA IQWVPENSNA 370 380 390 400 410 420 SSMVPDAFDP SKRHAPVMLT TDLALKFDPV YSKIAKRFLD NPKEFDDAFA RAWFKLIHRD 430 440 450 460 470 480 MGPRSRYLGS LVPKEAMIWQ DPVPPVDYKL VDANDIANLK GKILNSGLTT SELVKTAWAS 490 500 510 520 530 540 ASTFRGTDMR GGANGARIRL APQKDWPAND PQELAKVLKT LESIQNNFNN AQADGKKISL 550 560 570 580 590 600 ADLIVLGGNA AIEQAAKQAG YDIIVPFTPG RTDATQGMTD VKSFEVLEPK ADGFRNYFDK 610 620 630 640 650 660 SNNMSPPEML VEKASLLKLS VPEMTVLVGG MRVLNANTGQ NQYGVFTDKP GTLNNDFFIN 670 680 690 700 710 720 LLSMSTEWKK SSETEGIYEG YERKTGKLKW KATSVDLIFG ANSELRAVAE AYATDDAKEK 730 740 FIQDFINAWV KVMTADRFDI KAANANINS

References

[1]	"Catalase-peroxidases of Legionella pneumophila: cloning of the katA gene and studies of KatA function." Bandyopadhyay P., Steinman H.M. J. Bacteriol. 182:6679-6686(2000) [PubMed: 11073912] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION, SUBCELLULAR LOCATION. Strain: JR32.
[2]	"Legionella pneumophila catalase-peroxidase gene." Amemura-Maekawa J., Watanabe H. Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: AM511.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF276752 Genomic DNA. Translation: AAG37106.1. AB017595 Genomic DNA. Translation: BAA78342.1.
3D structure databases
SMR	Q9WXB9. Positions 34-740.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.11.1.6. 1454.
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]
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_LEGPN

Accession

Primary (citable) accession number: Q9WXB9
Secondary accession number(s): Q548R8

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	November 1, 1999
Last modified:	February 9, 2010
This is version 55 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)