B1Y7V8 (KATG_LEPCP) 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:	Lcho_0281

Organism

Leptothrix cholodnii (strain ATCC 51168 / LMG 8142 / SP-6) (Leptothrix discophora (strain SP-6)) [Complete proteome] [HAMAP]

Taxonomic identifier

395495 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Leptothrix

Protein attributes

Sequence length	723 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity By similarity. HAMAP MF_01961
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 dimer By similarity.
Subunit structure	Homodimer or homotetramer By similarity. HAMAP MF_01961
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
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
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
	Chain	1 – 723	723	Catalase-peroxidase HAMAP MF_01961		PRO_0000354826
Sites
	Active site	97	1	Proton acceptor By similarity
	Metal binding	265	1	Iron (heme axial ligand) By similarity
	Site	93	1	Transition state stabilizer By similarity
Amino acid modifications
	Cross-link	96 ↔ 224		Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-250) By similarity
	Cross-link	224 ↔ 250		Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-96) By similarity

Sequences

	Sequence		Length	Mass (Da)
	B1Y7V8 [UniParc]. Last modified May 20, 2008. Version 1. Checksum: D01F682DA9F5BA77	FASTA	723	78,888
	10 20 30 40 50 60 MDPKTSAGQC PVMHGANTTA AQSNTAWWPN ALNLDILHQH DTKTNPLGEG YRYREAVKQL 70 80 90 100 110 120 DVAALKADLT ALMTRSQPWW PADWGHYGGL MIRMAWHAAG SYRVADGRGG AGTGNQRFAP 130 140 150 160 170 180 LNSWPDNANL DKARRLLWPI KKKYGAKISW ADLIVLAGNV AYESMGLKTY GFAFGREDIW 190 200 210 220 230 240 HPEKDIYWGS EKAWLAPTGG EGSRYSGQRD LENPLAAVMM GLIYVNPEGV DGQPDPLKTA 250 260 270 280 290 300 QDVRVTFARM AMDDEETVAL TAGGHTVGKS HGNGSAANLG PAPEGADVHE QGLGWNNHSS 310 320 330 340 350 360 RGIGRDTVTS GIEGAWTTHP TQWDNGYFKL LLGYDWELKK SPAGAWQWEP VGIKEDDKPV 370 380 390 400 410 420 DVEDPSIRLN PIMTDADMAM KMDPAYRRIS ERFAADQAYF SEVFARAWFK LTHRDLGPKS 430 440 450 460 470 480 RYIGPEIPAE DLLWQDPVPV GPTAYDVGAV KSRIATSGLS VGELVATAWD SARTWRGSDY 490 500 510 520 530 540 RGGANGARIR LAPQKDWAGN EPERLARVLA VLEPIAAAAG ASVADVIVLA GNVGVELAAK 550 560 570 580 590 600 AAGFDVTVPF APGRGDATQA QTDVESFEVL EPVADGFRNW QQRSFAVQPE EMLLDRAQLM 610 620 630 640 650 660 GLSAPEMTVL VGGLRVLGAN HGGSKHGVFT DRVGALTNDF FVTLTDMAHA WVPTGRNSYE 670 680 690 700 710 720 IRERASGVVK YTATRADLVF GSNSVLRAYA EVYAQDDSRE KFVRDFVAAW VKVMNADRYE LQG

References

[1]

"Complete sequence of Leptothrix cholodnii SP-6." US DOE Joint Genome Institute Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. , Kyrpides N., Lykidis A., Emerson D., Richardson P. Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51168 / LMG 8142 / SP-6.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP001013 Genomic DNA. Translation: ACB32556.1.
RefSeq	YP_001789321.1. NC_010524.1.
3D structure databases
ProteinModelPortal	B1Y7V8.
SMR	B1Y7V8. Positions 23-721.
ModBase	Search...
Protein-protein interaction databases
STRING	B1Y7V8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	6160343.
GenomeReviews	Gene locus Lcho_0281 in contig CP001013_GR.
KEGG	lch:Lcho_0281.
PATRIC	22390833. VBILepCho83238_0286.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG285610.
OMA	WPNALNL.
ProtClustDB	PRK15061.
Enzyme and pathway databases
BioCyc	LCHO395495:LCHO_0281-MONOMER.
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. [Graphical view]
KO	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. False negative. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KATG_LEPCP

Accession

Primary (citable) accession number: B1Y7V8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2008
Last sequence update:	May 20, 2008
Last modified:	January 25, 2012
This is version 27 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program