Q7UUW9 (KATG_RHOBA) 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:	RB3010

Organism

Rhodopirellula baltica (strain SH1)

Taxonomic identifier

243090 [NCBI]

Taxonomic lineage

Bacteria › Planctomycetes › Planctomycetacia › Planctomycetales › Planctomycetaceae › Rhodopirellula

Protein attributes

Sequence length	857 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.
Caution	Differs from other katG proteins because it has a much longer N-terminus.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	Complete proteome 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: 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 – 857	857	Catalase-peroxidase HAMAP MF_01961		PRO_0000354891
Sites
	Active site	208	1	Proton acceptor By similarity
	Metal binding	371	1	Iron (heme axial ligand) By similarity
	Site	204	1	Transition state stabilizer By similarity
Amino acid modifications
	Cross-link	207 ↔ 330		Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-356) By similarity
	Cross-link	330 ↔ 356		Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-207) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q7UUW9 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: F28CF3153C2D7330	FASTA	857	93,632
	10 20 30 40 50 60 MRLVHGKDAV NALDVSWLSP ILVRDPTSPS ESAWDLFATF MRTRTMKSTA TNMNQHPTTA 70 80 90 100 110 120 QICRRFATRL FRGTVSIRPL TLTLGCLAAS ASASLVAQET ATNAAASQAD AISKCPVMGN 130 140 150 160 170 180 PAGPNRHTVS GAMGNGDWWP NQLNLDMLHQ NSVKSNPMGE DFDYAAAFNS LDLAAVKADI 190 200 210 220 230 240 KELMNTSQDW WPSDYGHYGP LFIRMAWHSA GTYRVSDGRG GASDGTQRFA PLNSWPDNAN 250 260 270 280 290 300 LDKARRLLWP IKQKYGSKIS WADLMVLTGN CALEDMGFET FGFAGGREDV WEPQKDVYWG 310 320 330 340 350 360 PETEWLGDKR YSGDRDLQNP LAAVQMGLIY VNPEGPNGKP DPIAAAKDIR ETFGRMAMND 370 380 390 400 410 420 EETVALIAGG HTFGKAHGAA SPDGNMGVEP EGEGLAAQGL GWINTHGTGN AGDTITSGLE 430 440 450 460 470 480 GAWTSTPAEW SHGYFENLFG YEWKLVKSPA GAWQWTPTDE NAKGTVPDAH DASKSHAPMM 490 500 510 520 530 540 FTTDLALRMD PEYGKISRRF HDNPEQFEKA FAKAWYKLTH RDMGPVSRLL GDSVPEPQLW 550 560 570 580 590 600 QDPIPEATFD VIGSKEIEQL KQKILATNLT SSQLVSTAWA SASTFRNSDM RGGANGARIR 610 620 630 640 650 660 LAPQKDWEVN EPAELASVLT TLEGVQKEFN ASRKDGKQVS MADLIVLGGC AGVEAAAMKA 670 680 690 700 710 720 GHAIQVPFTP GRTDATQEMT DVESFEPLKP IADGFRNYQG HNADRPAEEM LVDKANLLSL 730 740 750 760 770 780 TAPEMTVLVG GMRALDTNAG AGPLADLGKL TKRPGALTND FFVNLLDMNT VWKQSPMCEH 790 800 810 820 830 840 FFEGRDRESG NLKWTASRVD LVFGSNSQLR GIAEVYASED AKEKFVKDFV NAWTKVMNLD 850 RFDVNDSEST ETQVAAK

References

[1]

"Complete genome sequence of the marine planctomycete Pirellula sp. strain 1." Gloeckner F.O., Kube M., Bauer M., Teeling H., Lombardot T., Ludwig W., Gade D., Beck A., Borzym K., Heitmann K., Rabus R., Schlesner H., Amann R., Reinhardt R. Proc. Natl. Acad. Sci. U.S.A. 100:8298-8303(2003) [PubMed: 12835416] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SH1.

Cross-references

Sequence databases
EMBL GenBank DDBJ	BX294138 Genomic DNA. Translation: CAD72958.1.
RefSeq	NP_865274.1. NC_005027.1.
3D structure databases
HSSP	HSSP built from PDB template 1ITK based on UniProtKB O59651.
ProteinModelPortal	Q7UUW9.
SMR	Q7UUW9. Positions 135-844.
ModBase	Search...
Protein family/group databases
PeroxiBase	2389. RbaCP01_SH.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1793861.
GenomeReviews	Gene locus RB3010 in contig BX119912_GR.
KEGG	rba:RB3010.
NMPDR	fig|243090.1.peg.1614.
PATRIC	23244217. VBIRhoBal59814_1394.
Phylogenomic databases
HOGENOM	HBG285610.
OMA	KRHAPSM.
PhylomeDB	Q7UUW9.
ProtClustDB	PRK15061.
Enzyme and pathway databases
BioCyc	PSP117:RB3010-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. 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_RHOBA

Accession

Primary (citable) accession number: Q7UUW9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2008
Last sequence update:	October 1, 2003
Last modified:	January 25, 2012
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program