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Reviewed, UniProtKB/Swiss-Prot Q9X6B0 (KATG_YERPE)

Last modified June 16, 2009. Version 75. 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
      Short name=CP
    EC=1.11.1.6
    EC=1.11.1.7
Alternative name(s):
    Peroxidase/catalase
    Antigen 5
Gene names
Name: katG
Synonyms: katY
Ordered Locus Names: YPO3319, y0870, YP_0367
OrganismYersinia pestis [Complete proteome] [HAMAP]
Taxonomic identifier632 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length737 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity By similarity.

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.

Subunit structure

Homotetramer. Ref.1

Subcellular location

Periplasm. Ref.1

Post-translational modification

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

Sequence similarities

Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Ontologies

Keywords
   Biological processHydrogen peroxide
   Cellular componentPeriplasm
   DomainSignal
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
Peroxidase
   Technical termComplete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological processhydrogen peroxide catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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

Signal peptide1 – 2323 Ref.1
Chain24 – 737714Catalase-peroxidase HAMAP MF_01961
PRO_0000055578

Sites

Active site1031Proton acceptor By similarity
Metal binding2641Iron (heme axial ligand) By similarity
Site991Transition state stabilizer By similarity

Amino acid modifications

Cross-link102 ↔ 223Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-249) By similarity
Cross-link223 ↔ 249Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-102) By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9X6B0-1 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: DB870BC41ABD469A

FASTA73781,365
        10         20         30         40         50         60 
MLKKILPVLI TLAIVHNTPT AWAAEAPKTD SFYLPKSLDL SPLRLHNIES NPYGKDFNYA 

        70         80         90        100        110        120 
QQFKTLDLEA VKKDIKTVLT TSQDWWPADY GNYGPFFIRM AWHGAGTYRI YDGRGGADGG 

       130        140        150        160        170        180 
QQRFEPLNSW PDNANLDKAR RLLWPIKKKY GAKISWGDLM VLTGNVALES MGFKTLGFAG 

       190        200        210        220        230        240 
GREDDWQSDL VYWGAGNKML SDNRDKNGKL PKPLAATQMG LIYVNPEGPN GKPDPVAAAK 

       250        260        270        280        290        300 
DIREAFARMA MNDEETVALI AGGHTFGKAH GAASPEKCLG AAPGEAGLEQ QGLGWANKCG 

       310        320        330        340        350        360 
SGNGKDTITS GLEGAWTTDP THFTMQYLSN LYKHEWVLTK SPAGAWQWKP KNAANVVPDA 

       370        380        390        400        410        420 
TDPTKFHPLM MFTTDIALKV DPEYKKITTR FLENPEEFKM AFARAWFKLT HRDMGPAARY 

       430        440        450        460        470        480 
LGDEVPKETF IWQDPLPAAN YKMIDSADIS ELKDKILKTG LSDTKLIKTA WASASTFRGT 

       490        500        510        520        530        540 
DFRGGDNGAR IRLAPQKDWP VNDPAELHSV LAALMEVQNN FNKDRSDGKK VSLSDLIVLG 

       550        560        570        580        590        600 
GNAAIEDAAK KAGYSISIPF TPGRTDASQE ETDVSSFAVL EPTADGFRNY YDAKRNTLSP 

       610        620        630        640        650        660 
IASLIDRANK LELTVPEMTV LIGGLRVLDV NSGGSKAGVL TNTPGQLNNN FFVNLLDMST 

       670        680        690        700        710        720 
KWTKSPKAEG YFDGYDRKTG KLKWTASSVD LVFGSNPELR AVAEVYASDD AKEKFVHDFT 

       730 
KVWEKVMNLD RFDIKNN 

« Hide

References

« Hide 'large scale' references
[1]"Molecular characterization of KatY (antigen 5), a thermoregulated chromosomally encoded catalase-peroxidase of Yersinia pestis."
Garcia E., Nedialkov Y.A., Elliott J., Motin V.L., Brubaker R.R.
J. Bacteriol. 181:3114-3122(1999) [PubMed: 10322012] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 24-31 AND 250-254, SUBCELLULAR LOCATION, SUBUNIT.
Strain: KIM.
[2]"Genome sequence of Yersinia pestis, the causative agent of plague."
Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G., Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L., Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M., Chillingworth T., Cronin A., Davies R.M. expand/collapse author list , Davis P., Dougan G., Feltwell T., Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S., Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S., Barrell B.G.
Nature 413:523-527(2001) [PubMed: 11586360] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: CO-92 / Biovar Orientalis.
[3]"Genome sequence of Yersinia pestis KIM."
Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P., Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D., Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A., Nilles M.L. expand/collapse author list , Matson J.S., Blattner F.R., Perry R.D.
J. Bacteriol. 184:4601-4611(2002) [PubMed: 12142430] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KIM5 / Biovar Mediaevalis.
[4]"Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans."
Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D., Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L., Dai R. expand/collapse author list , Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R.
DNA Res. 11:179-197(2004) [PubMed: 15368893] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 91001 / Biovar Mediaevalis.

Cross-references

Sequence databases

AF135170 Genomic DNA. Translation: AAD37313.1.
AL590842 Genomic DNA. Translation: CAL21910.1.
AE009952 Genomic DNA. Translation: AAM84455.1. Different initiation.
AE017042 Genomic DNA. Translation: AAS60640.1. Different initiation.
PIRAC0403.
RefSeqNP_668204.1.
NP_991763.1.
YP_002348215.1.

3D structure databases

HSSPHSSP built from PDB template 1MWV based on UniProtKB Q939D2.
ModBaseSearch...

Protein family/group databases

PeroxiBase2640. YpCP01.

Genome annotation databases

GeneID1145817.
1176138.
2764071.
GenomeReviewsGene locus y0870 in contig AE009952_GR.
Gene locus YP_0367 in contig AE017042_GR.
Gene locus YPO3319 in contig AL590842_GR.
KEGGype:YPO3319.
ypk:y0870.
ypm:YP_0367.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ9X6B0.
OMAQ9X6B0. GTDMRGG.

Enzyme and pathway databases

BioCycYPES187410:Y0870-MON.
YPES214092:YPO3319-MON.
YPES229193:YP0367-MON.
BRENDA1.11.1.6. 142588.

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. 1 hit.
PS00436. PEROXIDASE_2. 1 hit.
PS50873. PEROXIDASE_4. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKATG_YERPE
AccessionPrimary (citable) accession number: Q9X6B0
Secondary accession number(s): Q0WBX3
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: November 1, 1999
Last modified: June 16, 2009
This is version 75 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