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Q1GR67 (KATG_SPHAL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Catalase-peroxidase

Short name=CP
EC=1.11.1.21
Alternative name(s):
Peroxidase/catalase
Gene names
Name:katG
Ordered Locus Names:Sala_2146
OrganismSphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256) (Sphingomonas alaskensis) [Complete proteome] [HAMAP]
Taxonomic identifier317655 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaSphingomonadalesSphingomonadaceaeSphingopyxis

Protein attributes

Sequence length731 AA.
Sequence statusComplete.
Protein existenceInferred 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 processHydrogen peroxide
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncatalase activity

Inferred from electronic annotation. Source: InterPro

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 731731Catalase-peroxidase HAMAP MF_01961
PRO_0000354937

Sites

Active site991Proton acceptor By similarity
Metal binding2691Iron (heme axial ligand) By similarity
Site951Transition state stabilizer By similarity

Amino acid modifications

Cross-link98 ↔ 227Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-254) By similarity
Cross-link227 ↔ 254Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-98) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1GR67 [UniParc].

Last modified June 27, 2006. Version 1.
Checksum: 674F7F4DFC5A5A4C

FASTA73180,470
        10         20         30         40         50         60 
MNDQTPIGSG CPVHQPGGVR SLLGRTNKDW WPDMLATEIL TPNGPSNPMG EDFDYAKAFK 

        70         80         90        100        110        120 
SLDYYALKDD LKALMTDSQP WWPADYGHYG PFFIRMAWHA AGTYRTADGR GGANSGQQRF 

       130        140        150        160        170        180 
APLDSWPDNG NLDKARRLLW PIKQKYGNKI SWADLFILAG NVAIESMGGP VFGFGGGRVD 

       190        200        210        220        230        240 
VYEPERDIYW GSEDKWVNQG VQTRIDPAKG METIEGPLAA IQMGLIYVNP EGPQGNPHDD 

       250        260        270        280        290        300 
EGMARDMKET FKRMAMNDEE TVALTAGGHT FGKAHGNGDP SLLGPAPAGS DLAAQGFGWV 

       310        320        330        340        350        360 
SSHESGGIGE HAVTSGIEGA WTNTPREWTE NYFRLLFDYD YELVKSPAGA WQWQPINQKE 

       370        380        390        400        410        420 
EDMAPAAWDP GIKVPTMMTT ADMALKRDPA YRAISERFRN DHEAFKDAFA RAWFKLTHRD 

       430        440        450        460        470        480 
MGPKVRYLGP EVPDEDLIWQ DPIPAGTKPS DAEVQAVKDK IAASGLTVSQ LIKTAWASAS 

       490        500        510        520        530        540 
TFRKSDFRGG ANGARVRLAP QKDWEVNEPA MLARVLDTLD GLRGSLSMAD AIVLGGVVGL 

       550        560        570        580        590        600 
EKAIRDAGFN VAVPFTGGRG DATQEQTDVE SFEVMEPEAD AFRNYVGKKK LAVKVEEMML 

       610        620        630        640        650        660 
DKASLLGLSV PEMTVLIGGL RVLGANHGER GHGHFTRRSG QLTNDFFVNL LDMTNVWKAV 

       670        680        690        700        710        720 
EGSNDQEYVA TDRTTGGETW RATRADLIFG SNSELRAVAE VYAENGHEEK FVRDFVKAWT 

       730 
KVMNADRFDL A 

« Hide

References

[1]"Complete sequence of chromosome of Sphingopyxis alaskensis RB2256."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Munk A.C., Chertkov O., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Cavicchioli R., Robb F., Ertan H., Schut F., Ting L.M., Richardson P.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13593 / LMG 18877 / RB2256.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000356 Genomic DNA. Translation: ABF53855.1.
RefSeqYP_617188.1. NC_008048.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4080143.
GenomeReviewsGene locus Sala_2146 in contig CP000356_GR.
KEGGsal:Sala_2146.
NMPDRfig|317655.9.peg.2072.
PATRIC23693616. VBISphAla23391_2224.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG285610.
OMAWPNALNL.
ProtClustDBPRK15061.

Enzyme and pathway databases

BioCycSALA317655:SALA_2146-MONOMER.

Family and domain databases

HAMAPMF_01961. Catal-peroxid.
[Tree]
InterProIPR000763. Catalase_peroxidase.
IPR010255. Haem_peroxidase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
[Graphical view]
KOK03782.
PfamPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
SUPFAMSSF48113. Peroxidase_super. 2 hits.
TIGRFAMsTIGR00198. Cat_per_HPI. 1 hit.
PROSITEPS00435. PEROXIDASE_1. False negative.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKATG_SPHAL
AccessionPrimary (citable) accession number: Q1GR67
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: June 27, 2006
Last modified: January 25, 2012
This is version 42 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families