Reviewed, UniProtKB/Swiss-Prot P83657 (CAT1_COMTR)

Names and origin

Protein names	Recommended name:     Catalase-1     EC=1.11.1.6
Organism	Comamonas terrigena
Taxonomic identifier	32013 [NCBI]
Taxonomic lineage	Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Comamonas

Protein attributes

Sequence length	57 AA.
Sequence status	Fragments.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic activity	2 H(2)O(2) = O(2) + 2 H(2)O.
Cofactor	Heme group.
Subunit structure	Homodimer.
Induction	Constitutively expressed. Inducible by oxidative stress in the exponential phase of bacterial growth.
Sequence similarities	Belongs to the catalase family.
Biophysicochemical properties	pH dependence: Active from pH 6.0 to 10.0. Temperature dependence: Activity decreases at temperatures above 55 degrees Celsius.
Mass spectrometry	Molecular weight is 55417 Da from positions 1 - ?. Determined by MALDI. Ref.1

Ontologies

Keywords
Biological process	Hydrogen peroxide
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	Direct protein sequencing
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
Molecular function	catalase activity Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – ›57	›57	Catalase-1		PRO_0000084984
Sites
	Metal binding	37	1	Iron (heme axial ligand) By similarity
Experimental info
	Non-adjacent residues	13 – 14	2
	Non-adjacent residues	32 – 33	2
	Non-adjacent residues	42 – 43	2
	Non-terminal residue	57	1

Sequences

	Sequence		Length	Mass (Da)
	P83657-1 [UniParc]. Last modified October 1, 2003. Version 1. Checksum: 22AC1B93B4F3D72E	FASTA	57	6,099
	10 20 30 40 50 THCLTTAAGA PVARFSTVAG ERGAADAERD IRRLFSYGDA ARRLGVNHQH IPVNAPR

References

[1]	"Expression, purification, and sequence analysis of catalase-1 from the soil bacterium Comamonas terrigena N3H." Zamocky M., Godocikova J., Gasperik J., Koller F., Polek B. Protein Expr. Purif. 36:115-123(2004) [PubMed: 15177292] [Abstract] Cited for: PROTEIN SEQUENCE, CATALYTIC ACTIVITY, MASS SPECTROMETRY. Strain: N3H.
[2]	"Oxidative stress-induced expression of catalases in Comamonas terrigena." Zamocky M., Polek B., Godocikova J., Koller F. Folia Microbiol. (Praha) 47:235-240(2002) [PubMed: 12094731] [Abstract] Cited for: CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, INDUCTION. Strain: N3H.

Cross-references

3D structure databases
ModBase	Search...
Protein family/group databases
PeroxiBase	4280. CterKat01.
Family and domain databases
InterPro	IPR002226. Catalase. IPR011614. Catalase_N. [Graphical view]
Pfam	PF00199. Catalase. 2 hits. [Graphical view]
ProDom	PD000510. Catalase. 2 hits. [Graphical view] [Entries sharing at least one domain]
PROSITE	PS00437. CATALASE_1. Partial match. PS00438. CATALASE_2. Partial match. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

CAT1_COMTR

Accession

Primary (citable) accession number: P83657

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 16, 2004
Last sequence update:	October 1, 2003
Last modified:	November 25, 2008
This is version 29 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)