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Reviewed, UniProtKB/Swiss-Prot Q31MN3 (KATG_SYNE7)

Last modified September 1, 2009. Version 27. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Catalase-peroxidase
      Short name=CP
    EC=1.11.1.6
    EC=1.11.1.7
Alternative name(s):
    Peroxidase/catalase
Gene names
Name: katG
Ordered Locus Names: Synpcc7942_1656
OrganismSynechococcus elongatus (strain PCC 7942) (Anacystis nidulans R2) [Complete proteome] [HAMAP]
Taxonomic identifier1140 [NCBI]
Taxonomic lineageBacteria › Cyanobacteria › Chroococcales › Synechococcus

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Protein attributes

Sequence length720 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. HAMAP MF_01961

Catalytic activity

2 H2O2 = O2 + 2 H2O. HAMAP MF_01961

Donor + H2O2 = oxidized donor + 2 H2O. HAMAP MF_01961

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per dimer. Ref.1

Subunit structure

Homodimer. Ref.1

Post-translational modification

The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme. HAMAP MF_01961

Sequence similarities

Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=4.2 mM for H2O2 for catalase activity HAMAP MF_01961

pH dependence:

Optimum pH is 6.5 for catalase activity. Active from pH 4.5 to 8.5.

Sequence caution

The sequence BAA09601.1 differs from that shown. Reason: Frameshift at positions 574 and 594.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – 720719Catalase-peroxidase HAMAP MF_01961
PRO_0000345095

Sites

Active site951Proton acceptor HAMAP MF_01961
Metal binding2631Iron (heme axial ligand) HAMAP MF_01961
Site911Transition state stabilizer By similarity

Amino acid modifications

Cross-link94 ↔ 222Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-248) HAMAP MF_01961
Cross-link222 ↔ 248Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-94) HAMAP MF_01961

Experimental info

Sequence conflict561K → Q in BAA09601. Ref.1
Sequence conflict601Missing in BAA09601. Ref.1
Sequence conflict1931V → F in BAA09601. Ref.1
Sequence conflict327 – 3293RML → AVCS in BAA09601. Ref.1
Sequence conflict3391S → N in BAA09601. Ref.1
Sequence conflict5041A → P in BAA09601. Ref.1
Sequence conflict5141A → S in BAA09601. Ref.1
Sequence conflict5201S → T in BAA09601. Ref.1
Sequence conflict5361A → K in BAA09601. Ref.1
Sequence conflict6251G → V in BAA09601. Ref.1

Secondary structure

1 ...................................................................................................................... 720
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
Q31MN3-1 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 93A4C2E9990F1A2F

FASTA72080,078
        10         20         30         40         50         60 
MTATQGKCPV MHGGATTVNI STAEWWPKAL NLDILSQHDR KTNPMGPDFN YQEEVKKLDV 

        70         80         90        100        110        120 
AALKQDLQAL MTDSQDWWPA DWGHYGGLMI RLTWHAAGTY RIADGRGGAG TGNQRFAPLN 

       130        140        150        160        170        180 
SWPDNTNLDK ARRLLWPIKQ KYGNKLSWAD LIAYAGTIAY ESMGLKTFGF AFGREDIWHP 

       190        200        210        220        230        240 
EKDIYWGPEK EWVPPSTNPN SRYTGDRELE NPLAAVTMGL IYVNPEGVDG NPDPLKTAHD 

       250        260        270        280        290        300 
VRVTFARMAM NDEETVALTA GGHTVGKCHG NGNAALLGPE PEGADVEDQG LGWINKTQSG 

       310        320        330        340        350        360 
IGRNAVTSGL EGAWTPHPTQ WDNGYFRMLL NYDWELKKSP AGAWQWEPIN PREEDLPVDV 

       370        380        390        400        410        420 
EDPSIRRNLV MTDADMAMKM DPEYRKISER FYQDPAYFAD VFARAWFKLT HRDMGPKARY 

       430        440        450        460        470        480 
IGPDVPQEDL IWQDPIPAGN RNYDVQAVKD RIAASGLSIS ELVSTAWDSA RTYRNSDKRG 

       490        500        510        520        530        540 
GANGARIRLA PQKDWEGNEP DRLAKVLAVL EGIAAATGAS VADVIVLAGN VGVEQAARAA 

       550        560        570        580        590        600 
GVEIVLPFAP GRGDATAEQT DTESFAVLEP IHDGYRNWLK QDYAATPEEL LLDRTQLLGL 

       610        620        630        640        650        660 
TAPEMTVLIG GLRVLGTNHG GTKHGVFTDR EGVLTNDFFV NLTDMNYLWK PAGKNLYEIC 

       670        680        690        700        710        720 
DRKTNQVKWT ATRVDLVFGS NSILRAYSEL YAQDDNKEKF VRDFVAAWTK VMNADRFDLD

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References

« Hide 'large scale' references
[1]"The catalase-peroxidase of Synechococcus PCC 7942: purification, nucleotide sequence analysis and expression in Escherichia coli."
Mutsuda M., Ishikawa T., Takeda T., Shigeoka S.
Biochem. J. 316:251-257(1996) [PubMed: 8645214] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-15, BIOPHYSICOCHEMICAL PROPERTIES, HEME-BINDING, SUBUNIT.
[2]"Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M., Kyrpides N., Lykidis A., Richardson P.
Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"Crystal structure of catalase-peroxidase from Synechococcus PCC 7942."
Wada K., Tada T.
Submitted (MAR-2004) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.4 ANGSTROMS) IN COMPLEX WITH HEME.

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Cross-references

Sequence databases

D61378 Genomic DNA. Translation: BAA09601.1. Frameshift.
CP000100 Genomic DNA. Translation: ABB57686.1.
PIRS71130.
RefSeqYP_400673.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1UB2X-ray2.40A1-720[»]
ModBaseSearch...

Protein-protein interaction databases

STRINGQ31MN3.

Protein family/group databases

PeroxiBase2426. SeCP01_PCC7942.

Genome annotation databases

GeneID3775727.
GenomeReviewsGene locus Synpcc7942_1656 in contig CP000100_GR.
KEGGsyf:Synpcc7942_1656.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ31MN3.

Enzyme and pathway databases

BioCycSELO1140:SYNPCC7942_1656-MON.

Family and domain databases

HAMAPMF_01961.
[Tree]
InterProIPR000763. Catalase_proxase.
IPR002016. Haem_peroxidase_pln/fun/bac.
IPR019794. Peroxidases_AS.
IPR019793. Peroxidases_heam-ligand_BS.
[Graphical view]
PfamPF00141. peroxidase. 2 hits.
[Graphical view]
PRINTSPR00460. BPEROXIDASE.
PR00458. PEROXIDASE.
TIGRFAMsTIGR00198. cat_per_HPI. 1 hit.
PROSITEPS00435. PEROXIDASE_1. False negative.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 2 hits.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameKATG_SYNE7
AccessionPrimary (citable) accession number: Q31MN3
Secondary accession number(s): Q55110
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: December 6, 2005
Last modified: September 1, 2009
This is version 27 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents