Q5LLG6 (KATG_SILPO) 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:	SPOA0061

Encoded on

Plasmid megaplasmid Spo

Organism

Silicibacter pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3) [Complete proteome] [HAMAP]

Taxonomic identifier

246200 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Alphaproteobacteria › Rhodobacterales › Rhodobacteraceae › Ruegeria

Protein attributes

Sequence length	731 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 Plasmid
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 – 731	731	Catalase-peroxidase HAMAP MF_01961		PRO_0000354933
Sites
	Active site	99	1	Proton acceptor By similarity
	Metal binding	267	1	Iron (heme axial ligand) By similarity
	Site	95	1	Transition state stabilizer By similarity
Amino acid modifications
	Cross-link	98 ↔ 226		Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-252) By similarity
	Cross-link	226 ↔ 252		Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-98) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q5LLG6 [UniParc]. Last modified February 1, 2005. Version 1. Checksum: 6F0349CCA0187025	FASTA	731	78,773
	10 20 30 40 50 60 MDGNDAPNAG QCPVMHGHAA GTGMRNHHWW PNQINLKVLH QHSSKSDPMG AQFNYAEAFK 70 80 90 100 110 120 SLDLDALKAD LTALMTDSQD WWPADYGHYG PLFIRMTWHA AGTYRTADGR GGGSTGNQRF 130 140 150 160 170 180 APLNSWPDNG NLDKARRLLW PIKKKYGDKI SWADLLILTG NVALESMGFK TFGFAGGRPD 190 200 210 220 230 240 IWEPEEDIYW GSEGEWLAPS DTANSRYSGA RDLENPLAAV QMGLIYVNPE GPDGNPDIVA 250 260 270 280 290 300 SGHDVIETFG RMAMDEAETV ALVAGGHTFG KAHGNGPASA VGPEPEAAPI EAMGLGWLST 310 320 330 340 350 360 HGSGKGADAI TSGIEGAWKP HPTTWDMGYF KVLFKYDWEL TKSPAGANIW LATNVEDEDM 370 380 390 400 410 420 VEDAFDPSKK HRPMMTTADL SLRYHPKLLP HAKRFAEDPA AFADAFARAW FKLTHRDMGP 430 440 450 460 470 480 RARYLGKEVP AEELIWQDPI PAGTQIDADD AAALKAQILA SGLSVSDMVS TAWASASTFR 490 500 510 520 530 540 GSDMRGGANG ARIRLAPQKD WEVNEPAKLA RVLGVLEGIQ AGFSSGGKSV SMADLIVLAG 550 560 570 580 590 600 CAGVEQAAKA GGHQIEVPFT SGRGDASAEQ TDAESFAVME PVMDGFRNYQ ARELSTSPEE 610 620 630 640 650 660 MLVDRAQLLG LSAPEMTVLV AGLRVLGANH GGSAHGVLTN RPGVLSSDFL TNLLDMGTEW 670 680 690 700 710 720 KPSGKGVYEG RDRASGAARW TATRVDLVFG SNSQLRALAE RYAQDDAEAS FVADFVAAWV 730 KVMNADRFDL T

References

[1]

"Genome sequence of Silicibacter pomeroyi reveals adaptations to the marine environment." Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B., Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.M., Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E., Sheldon W.M. , Ye W., Miller T.R., Carlton J., Rasko D.A., Paulsen I.T., Ren Q., Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J., Haft D.H., Selengut J., Ward N. Nature 432:910-913(2004) [PubMed: 15602564] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700808 / DSM 15171 / DSS-3.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000032 Genomic DNA. Translation: AAV97201.1.
RefSeq	YP_164892.1. NC_006569.1.
3D structure databases
HSSP	HSSP built from PDB template 1ITK based on UniProtKB O59651.
ProteinModelPortal	Q5LLG6.
SMR	Q5LLG6. Positions 23-730.
ModBase	Search...
Protein family/group databases
PeroxiBase	2384. SpoCP01.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	3196563.
GenomeReviews	Gene locus SPOA0061 in contig CP000032_GR.
KEGG	sil:SPOA0061.
NMPDR	fig|246200.3.peg.310.
PATRIC	23381426. VBIRuePom114501_4038.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG285610.
OMA	WPNALNL.
ProtClustDB	PRK15061.
Enzyme and pathway databases
BioCyc	RPOM246200:SPO_A0061-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. 2 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KATG_SILPO

Accession

Primary (citable) accession number: Q5LLG6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 25, 2008
Last sequence update:	February 1, 2005
Last modified:	January 25, 2012
This is version 50 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program