C1AV76 (KATG_RHOOB) 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:	ROP_53190

Organism

Rhodococcus opacus (strain B4) [Complete proteome] [HAMAP]

Taxonomic identifier

632772 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length	742 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 – 742	742	Catalase-peroxidase HAMAP MF_01961		PRO_1000189073
Sites
	Active site	110	1	Proton acceptor By similarity
	Metal binding	272	1	Iron (heme axial ligand) By similarity
	Site	106	1	Transition state stabilizer By similarity
Amino acid modifications
	Cross-link	109 ↔ 231		Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-257) By similarity
	Cross-link	231 ↔ 257		Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-109) By similarity

Sequences

	Sequence		Length	Mass (Da)
	C1AV76 [UniParc]. Last modified May 26, 2009. Version 1. Checksum: E8118FE5A00B43D6	FASTA	742	81,136
	10 20 30 40 50 60 MSDSCPVAHE GNTRSTSESE NPAIPSPTPT AHRPRTNRDW WPNQPELSVL HAHSSKSNPM 70 80 90 100 110 120 GENFDYTAEF AKLDVEALKR DVIDLMTDSQ DWWPADFGHY GGLFIRMSWH AAGTYRIADG 130 140 150 160 170 180 RGGGGQGAQR FAPLNSWPDN ASLDKARRLL WPVKQKYGKQ ISWSDLLVFA GNCALESMGF 190 200 210 220 230 240 KTFGFGFGRE DIWEPEEIYW GPEDTWLGDE RYSGDRDLSG PLGAVQMGLI YVNPEGPNGQ 250 260 270 280 290 300 PDPLAAARDI RETFGRMAMN DIETAALIAG GHTFGKTHGA GDADLVGPEP EAAPIEQQGL 310 320 330 340 350 360 GWKSAYGTGV GKDAITSGLE VVWTPTPTKW DNSFLEVLYG YEWELTKSPA GAWQWTAKDG 370 380 390 400 410 420 AGAGTIPDPF DSSAGRAPTM LTTDLSLRID PAYEKITRRW LDHPEEFAEE FAKAWYKLLH 430 440 450 460 470 480 RDMGPVTRYL GPWVPEAQLW QDPVPAVDHQ LIGDSEIAAL KGKILDSGLS ISQLVSTAWA 490 500 510 520 530 540 SAATFRGTDM RGGANGARIR LAPQKDWEIN SPAELSKVLQ TLEQIQQDFN SSQSGGVKVS 550 560 570 580 590 600 LADLIVLAGA AGVEKAAKNA GHDITVPFTP GRTDASQEQT DVESFAVLEP RADGFRNYLR 610 620 630 640 650 660 PGEKLPAEAL LVERAYMLNL TAPEMTVLIG GLRALNANFG QTGHGVFTDR PESLTNDFFV 670 680 690 700 710 720 NLLDMGTVWK GAASAENVYE GSDRVTGDAK WTATAVDLVF GSNSQLRALA EVYATDDAQQ 730 740 KFVQDFVSAW DKVMNLDRFD LD

References

[1]

"Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4." Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S. Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: B4.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP011115 Genomic DNA. Translation: BAH53566.1.
RefSeq	YP_002782511.1. NC_012522.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	C1AV76.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	7744337.
GenomeReviews	Gene locus ROP_53190 in contig AP011115_GR.
KEGG	rop:ROP_53190.
PATRIC	23228011. VBIRhoOpa21106_5378.
Organism-specific databases
CMR	Search...
Phylogenomic databases
OMA	KRHAPSM.
ProtClustDB	PRK15061.
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]
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. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KATG_RHOOB

Accession

Primary (citable) accession number: C1AV76

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 28, 2009
Last sequence update:	May 26, 2009
Last modified:	January 25, 2012
This is version 21 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program