Catalase-peroxidase - Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)

Preferred order of sections

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
Synonyms:	perA
Ordered Locus Names:	AF_2233

Organism

Archaeoglobus fulgidus (strain ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126)

Taxonomic identifier

224325 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Archaeoglobi › Archaeoglobales › Archaeoglobaceae › Archaeoglobus

Protein attributes

Sequence length	741 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Displays also NADH oxidase, INH lyase and isonicotinoyl-NAD synthase activity. 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.
Biophysicochemical properties	Kinetic parameters: K_M=32 mM for H₂O₂ for the catalase reaction (at pH 5.5-6.0) Ref.2 K_M=3.8 mM for H₂O₂ for the catalase reaction (at pH 7.0) K_M=95 mM for H₂O₂ for the peroxidase reaction K_M=16 mM for ABTS for the peroxidase reaction V_max=11760 µmol/min/mg enzyme for H₂O₂ for the catalase reaction (at pH 5.5-6.0) V_max=5500 µmol/min/mg enzyme for H₂O₂ for the catalase reaction (at pH 7.0) V_max=12 µmol/min/mg enzyme for ABTS for the peroxidase reaction pH dependence: Optimum pH is 4.5 for the peroxidase reaction.

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 – 741

741

Catalase-peroxidase HAMAP MF_01961

PRO_0000055579

Sites

Active site

87

1

Proton acceptor By similarity

Metal binding

249

1

Iron (heme axial ligand) By similarity

Site

83

1

Transition state stabilizer By similarity

Amino acid modifications

Cross-link

86 ↔ 208

Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-234) By similarity

Cross-link

208 ↔ 234

Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-86) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O28050 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: A931DF34F050FC63
Show »

FASTA

741

84,854

        10         20         30         40         50         60 
MMRQGGVMVG ARKRWITDWW PNRLNLKILR QNLQNPYGED YDYVEEVENL DIDAVIRDLK 

        70         80         90        100        110        120 
ELMRSSQDWW PADFGHYGPL FIRLAWHSAG SYRIFDGRGG ARDGSIRFPP RINWPDNINL 

       130        140        150        160        170        180 
DKAIRLLWPI KKKYGRKLSW ADLIILAGTV AMEDMGVKLF GFALGREDIF EPDESPDWGP 

       190        200        210        220        230        240 
EEEMLTAKRG EKEELERPFA ATEMGLIYVN PEGPGGNPDP LGSAQEIRVA FRRMGMNDEE 

       250        260        270        280        290        300 
TVALIAGGHA FGKCHGAGPA DYLGPDPSSS PIEMQGLGWK YNYGKGKGSD TFTSGLEVTW 

       310        320        330        340        350        360 
SPTPTKFGIN YLRILFTYEW ELEKSPAGKN QWVAKDAPEI IPDAHDPNKK HRPRMLTADL 

       370        380        390        400        410        420 
ALRFDPEFSK IARRFLENPE EFEKAFAIAW YKLTHRDMGP KDCYIGKYVP EETFVWQDPL 

       430        440        450        460        470        480 
PRRDYELVDE KDVEELKRRI LASGLSLSQL VYFAWASAST YRNSDRRGGA NGARIRLKPM 

       490        500        510        520        530        540 
SVWEVNHPEE LKKVIAAYEK IQQEFNEGAK GSEKRISIAD LIVLGGIAAV EEAARRAGFS 

       550        560        570        580        590        600 
VKVPFIPGRV DAQQEHVDEE FYRVIEPFAD GFRNYFRYPE RINERDVYTT PEYFLVDKAN 

       610        620        630        640        650        660 
LLTLTVPEMV VLIGGMRALG ANYSHSDYGV LTERPGVLSN DFFVNLLDMS VEWRAADDYR 

       670        680        690        700        710        720 
YTFEGYDRKS GELRWRATRV DLILGHHDEL RAVAEVYGCD DAKEKFVKDF AAVCAKVMHL 

       730        740 
DRFDLWRSNR KLYKEITAGL R

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The complete genome sequence of the hyperthermophilic, sulphate-reducing archaeon Archaeoglobus fulgidus." Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A., Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L., Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D., Quackenbush J., Lee N.H., Sutton G.G. Venter J.C. Nature 390:364-370(1997) [PubMed: 9389475] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126.
[2]	"Comparative study of catalase-peroxidases (KatGs)." Singh R., Wiseman B., Deemagarn T., Jha V., Switala J., Loewen P.C. Arch. Biochem. Biophys. 471:207-214(2008) [PubMed: 18178143] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE000782 Genomic DNA. Translation: AAB89022.1.
PIR	A69529.
RefSeq	NP_071058.1. NC_000917.1.
3D structure databases
ProteinModelPortal	O28050.
SMR	O28050. Positions 18-725.
ModBase	Search...
Protein family/group databases
PeroxiBase	1858. AfCP01.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	1485464.
GenomeReviews	Gene locus AF_2233 in contig AE000782_GR.
KEGG	afu:AF2233.
NMPDR	fig\|224325.1.peg.2219.
TIGR	AF_2233.
Phylogenomic databases
HOGENOM	HBG285610.
OMA	KRHAPSM.
PhylomeDB	O28050.
ProtClustDB	PRK15061.
Enzyme and pathway databases
BioCyc	AFUL224325:AF_2233-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_ARCFU

Accession

Primary (citable) accession number: O28050

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	January 1, 1998
Last modified:	December 14, 2011
This is version 83 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents