[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 24-31 AND 250-254, SUBCELLULAR LOCATION, AND SUBUNIT. STRAIN=KIM; PubMed=10322012 [NCBI, ExPASy, EBI, Israel, Japan] Garcia E., Nedialkov Y.A., Elliott J., Motin V.L., Brubaker R.R.; "Molecular characterization of KatY (antigen 5), a thermoregulated chromosomally encoded catalase-peroxidase of Yersinia pestis."; J. Bacteriol. 181:3114-3122(1999).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=CO-92 / Biovar Orientalis; DOI=10.1038/35097083; PubMed=11586360 [NCBI, ExPASy, EBI, Israel, Japan] 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., 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.; "Genome sequence of Yersinia pestis, the causative agent of plague."; Nature 413:523-527(2001).
[3]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=KIM5 / Biovar Mediaevalis; DOI=10.1128/JB.184.16.4601-4611.2002; PubMed=12142430 [NCBI, ExPASy, EBI, Israel, Japan] 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., Matson J.S., Blattner F.R., Perry R.D.; "Genome sequence of Yersinia pestis KIM."; J. Bacteriol. 184:4601-4611(2002).
[4]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=91001 / Biovar Mediaevalis; DOI=10.1093/dnares/11.3.179; PubMed=15368893 [NCBI, ExPASy, EBI, Israel, Japan] 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., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H., Wang J., Huang P., Yang R.; "Complete genome sequence of Yersinia pestis strain 91001, an isolate avirulent to humans."; DNA Res. 11:179-197(2004).

Comments

FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity (By similarity).
CATALYTIC ACTIVITY: 2 H₂O₂ = O₂ + 2 H₂O.
CATALYTIC ACTIVITY: Donor + H₂O₂ = oxidized donor + 2 H₂O.
COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per dimer (By similarity).
SUBUNIT: Homotetramer.
SUBCELLULAR LOCATION: Periplasm.
PTM: The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme (By similarity).
SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF135170; AAD37313.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL590842; CAL21910.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE009952; AAM84455.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AE017042; AAS60640.1; ALT_INIT; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

AC0403; AC0403.

RefSeq

NP_668204.1; -.
NP_991763.1; -.

3D structure databases

HSSP

Q939D2; 1MWV. [HSSP ENTRY / PDB]

ModBase

Q9X6B0.

Protein family/group databases

PeroxiBase

2640; YpCP01.

Enzyme and pathway databases

BioCyc

YPES187410:Y0870-MON; -.
YPES214092:YPO3319-MON; -.
YPES229193:YP0367-MON; -.

Ontologies

GO:0042597;	Cellular component: periplasmic space (inferred from electronic annotation from UniProtKB-KW).
GO:0004096;	Molecular function: catalase activity (inferred from electronic annotation from InterPro).
GO:0020037;	Molecular function: heme binding (inferred from electronic annotation from InterPro).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0042744;	Biological process: hydrogen peroxide catabolic process (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

HAMAP

MF_01961; -; 1.
PBIL [Tree]

InterPro

IPR000763; Catalase_proxase.
IPR002016; Haem_peroxidase_pln/fun/bac.
Graphical view of domain structure.

Pfam

PF00141; peroxidase; 2.
Pfam graphical view of domain structure.

PRINTS

PR00460; BPEROXIDASE.
PR00458; PEROXIDASE.

TIGRFAMs

TIGR00198; cat_per_HPI; 1.

PROSITE

PS00435; PEROXIDASE_1; 1.
PS00436; PEROXIDASE_2; 1.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).

Genome annotation databases

GeneID

1145817; -.
2764071; -.

GenomeReviews

AE009952_GR; y0870.
AE017042_GR; YP_0367.
AL590842_GR; YPO3319.

KEGG

ype:YPO3319; -.
ypk:y0870; -.
ypm:YP_0367; -.

Phylogenomic databases

HOGENOM

Q9X6B0; -.

Genome annotation databases

CMR

Q9X6B0; YPO3319.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Direct protein sequencing; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Periplasm; Peroxidase; Signal.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 23`	`23`
`CHAIN`	`24 737`	`714`	`Catalase-peroxidase.`	`PRO_0000055578`
`ACT_SITE`	`103 103`		`Proton acceptor (By similarity).`
`METAL`	`264 264`		`Iron (heme axial ligand) (By similarity).`
`SITE`	`99 99`	`1`	`Transition state stabilizer (By similarity).`
`CROSSLNK`	`102 223`		`Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-249) (By similarity).`
`CROSSLNK`	`223 249`		`Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-102) (By similarity).`

Sequence information

Length: 737 AA [This is the length of the unprocessed precursor]

Molecular weight: 81365 Da [This is the MW of the unprocessed precursor]

CRC64: DB870BC41ABD469A [This is a checksum on the sequence]

        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

Q9X6B0 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools