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Reviewed, UniProtKB/Swiss-Prot Q87I38 (KATG2_VIBPA)

Last modified February 9, 2010. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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

Names and origin

Protein namesRecommended name:
    Catalase-peroxidase 2
      Short name=CP 2
    EC=1.11.1.6
    EC=1.11.1.7
Alternative name(s):
    Peroxidase/catalase 2
Gene names
Name: katG2
Ordered Locus Names: VPA0768
OrganismVibrio parahaemolyticus [Complete proteome] [HAMAP]
Taxonomic identifier670 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length724 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

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 By similarity. HAMAP MF_01961

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

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functioncatalase activity

Inferred from electronic annotation. Source: HAMAP

heme binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 724724Catalase-peroxidase 2 HAMAP MF_01961
PRO_0000354951

Sites

Active site991Proton acceptor By similarity
Metal binding2671Iron (heme axial ligand) By similarity
Site951Transition state stabilizer By similarity

Amino acid modifications

Cross-link98 ↔ 226Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-252) By similarity
Cross-link226 ↔ 252Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-98) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q87I38-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 6F552DAA3ECD9EA9

FASTA72480,704
        10         20         30         40         50         60 
MSNTNGGSVG KCPVMHGGQT STDKSVMDWW PNALNLDILH QHDSKTNPFG PDFNYKEELK 

        70         80         90        100        110        120 
KLDVDALKQD LKDLMTNSQV WWPADWGHYG GLMIRMAWHA AGSYRIADGR GGAATGNQRF 

       130        140        150        160        170        180 
APLNSWPDNA NLDKARRLLW PIKRKYGNKL SWADLIILAG NMAYESMGFK TFGFGFGRED 

       190        200        210        220        230        240 
IWHPEKDTYW GSEQEWLAPS GAKNSRYSGE RDLENPLAAV MMGLIYVNPE GVDGNPDPLK 

       250        260        270        280        290        300 
TAQDMRVTFA RMAMNDEETV ALTAGGHTVG KCHGNGDAAN LGPDPEGADV HEQGLGWMNH 

       310        320        330        340        350        360 
KTRGIGRDTV TSGLEGAWTT HPTQWDNGYF YLLFKYDWEL KKSPAGAWQW EPIDIEEQDK 

       370        380        390        400        410        420 
PVDVEDGSKR YNPIMTDADM ALKMDPEYRK ISERFQQDPA YFEDMFARAW FKLTHRDMGP 

       430        440        450        460        470        480 
KSCYLGPDVP SEDLIWQDPT PAGKTDYNVD LVKGKIEASG LSIADLVATA WDSARTYRGS 

       490        500        510        520        530        540 
DRRGGANGAR IRLAPQKDWQ GNEPERLSRV LAVLESIAAE EGCSVADAIV LAGNVGIELA 

       550        560        570        580        590        600 
ARAAGHDVSV PFAPGRGDAS QDMTDVESFE VLEPVADGFR NWLKKDYVVK PEELLLDRAQ 

       610        620        630        640        650        660 
LMGLTAPEMT VLIGGLRVLG SNYGGSKDGV FTDRVGTLSN DFFVNLTDMA YTWKPAGENQ 

       670        680        690        700        710        720 
YEIRDRKTDQ VKWTATRVDL VFGSNSILRS YAEVYAQDDN QEKFIHDFVA AWTKVMNADR 


FDLQ 

« Hide

References

[1]"Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism distinct from that of V. cholerae."
Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K., Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S., Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.
Lancet 361:743-749(2003) [PubMed: 12620739] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: RIMD 2210633 / Serotype O3:K6.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000032 Genomic DNA. Translation: BAC62111.1.
RefSeqNP_800278.1.

3D structure databases

HSSPHSSP built from PDB template 1ITK based on UniProtKB O59651.
ModBaseSearch...

Protein family/group databases

PeroxiBase2656. VpCP02_RIMD2210633.

Genome annotation databases

GeneID1191457.
GenomeReviewsGene locus VPA0768 in contig BA000032_GR.
KEGGvpa:VPA0768.
NMPDRfig|223926.1.peg.3848.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG285610.
OMAWPNALNL.

Enzyme and pathway databases

BioCycVPAR223926:VPA0768-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]
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. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKATG2_VIBPA
AccessionPrimary (citable) accession number: Q87I38
Entry history
Integrated into UniProtKB/Swiss-Prot: November 25, 2008
Last sequence update: June 1, 2003
Last modified: February 9, 2010
This is version 48 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)

Relevant documents

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