NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 33560 / CIP 702 / DSM 4688 / NCTC 11351;
PubMed=7670638 [NCBI, ExPASy, EBI, Israel, Japan]
Grant K.A., Park S.F.;
"Molecular characterization of katA from Campylobacter jejuni and generation of a catalase-deficient mutant of Campylobacter coli by interspecific allelic exchange.";
Microbiology 141:1369-1376(1995).

[2]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NCTC 11168 / Serotype O:2;
DOI=10.1038/35001088; PubMed=10688204 [NCBI, ExPASy, EBI, Israel, Japan]
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S., Barrell B.G.;
"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences.";
Nature 403:665-668(2000).

Comments

FUNCTION: Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.
CATALYTIC ACTIVITY: 2 H₂O₂ = O₂ + 2 H₂O.
COFACTOR: Heme group.
INTERACTION:
Q0PC74:fliY; NbExp=1; IntAct=EBI-1195173, EBI-1191111;
SIMILARITY: Belongs to the catalase family.

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

X85130; CAA59444.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AL111168; CAL35497.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

F81283; F81283.
I40767; I40767.

3D structure databases

HSSP

P42321; 1M85. [HSSP ENTRY / PDB]

ModBase

Q59296.

Protein-protein interaction databases

IntAct

Q59296; -.

Protein family/group databases

PeroxiBase

5383; CjejKat01.

Enzyme and pathway databases

BioCyc

CJEJ192222:CJ1385-MON; -.

Ontologies

GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.

Family and domain databases

InterPro

IPR002226; Catalase.
IPR011614; Catalase_N.
Graphical view of domain structure.

Gene3D

G3DSA:2.40.180.10; Catalase_N; 1.

PANTHER

PTHR11465; Catalase; 1.

Pfam

PF00199; Catalase; 1.
Pfam graphical view of domain structure.

PRINTS

PR00067; CATALASE.

ProDom

PD000510; Catalase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

PROSITE

PS00437; CATALASE_1; 1.
PS00438; CATALASE_2; FALSE_NEG.

BLOCKS

Q59296.

Genome annotation databases

GenomeReviews

AL111168_GR; Cj1385.

KEGG

cje:Cj1385; -.

CMR

Q59296; Cj1385.

Other

ProtoNet

Q59296.

UniRef

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

Keywords

Complete proteome; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 507`	`507`	`Catalase.`	`PRO_0000084983`
`ACT_SITE`	`52 52`		`By similarity.`
`ACT_SITE`	`124 124`		`By similarity.`
`METAL`	`334 334`		`Iron (heme axial ligand) (By similarity).`
`CONFLICT`	`23 23`		`T -> A (in Ref. 2; CAL35497).`
`CONFLICT`	`82 82`		`I -> V (in Ref. 2; CAL35497).`
`CONFLICT`	`177 177`		`R -> S (in Ref. 2; CAL35497).`
`CONFLICT`	`283 283`		`L -> F (in Ref. 2; CAL35497).`
`CONFLICT`	`440 440`		`T -> A (in Ref. 2; CAL35497).`
`CONFLICT`	`455 455`		`E -> K (in Ref. 2; CAL35497).`
`CONFLICT`	`472 507`		`FPIVSRIRAWRNHGHRCFLCEIVIRSQFHTTYEPEA -> LEK (in Ref. 2; CAL35497).`

Sequence information

Length: 507 AA [This is the length of the unprocessed precursor]

Molecular weight: 58416 Da [This is the MW of the unprocessed precursor]

CRC64: B1320894668E867E [This is a checksum on the sequence]

        10         20         30         40         50         60 
MKKLTNDFGN IIADNQNSLS AGTKGPLLMQ DYLLLEKLAH QNRERIPERT VHAKGSGAYG 

        70         80         90        100        110        120 
EIKITADLSA YTKAKIFQKG EITPLFLRFS TVAGEAGAAD AERDVRGFAI KFYTKEGNWD 

       130        140        150        160        170        180 
LVGNNTPTFF IRDAYKFPDF IHTQKRDPRT HLRSNNAAWD FWSLCPESLH QVTILMRDRG 

       190        200        210        220        230        240 
IPASYRHMHG FGSHTYSFIN DKNERFWVKF HFKTQQGIKN LTNQEAAELI AKDRESHQRD 

       250        260        270        280        290        300 
LYNAIENKDF PKWKVQVQIL AEKDIEKLGF NPFDLTKIWP HSLVPLMDIG EMILNKNPQN 

       310        320        330        340        350        360 
YFNEVEQAAF SPSNIVPGIG FSPDKMLQAR IFSYPDAQRY RIGTNYHLLP VNRAKSEVNT 

       370        380        390        400        410        420 
YNVAGAMNFD SYKNDAAYYE PNSYDNSPKE DKSYLEPDLV LEGVAQRYAP LDNDFYTQPR 

       430        440        450        460        470        480 
ALFNLMNDDQ KTQLFHNIAT SMEGVDEKII TRALEHFEKI SPDYAKGIKK AFPIVSRIRA 

       490        500 
WRNHGHRCFL CEIVIRSQFH TTYEPEA

Q59296 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