[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE. DOI=10.1016/0378-1119(93)90356-8; PubMed=8344520 [NCBI, ExPASy, EBI, Israel, Japan] Wolfframm C., Lingens F., Mutzel R., van Pee K.-H.; "Chloroperoxidase-encoding gene from Pseudomonas pyrrocinia: sequence, expression in heterologous hosts, and purification of the enzyme."; Gene 130:131-135(1993).
[2]	MUTAGENESIS. DOI=10.1016/0167-4838(95)00055-Y; PubMed=7632719 [NCBI, ExPASy, EBI, Israel, Japan] Pelletier I., Altenbuchner J., Mattes R.; "A catalytic triad is required by the non-heme haloperoxidases to perform halogenation."; Biochim. Biophys. Acta 1250:149-157(1995).

Comments

FUNCTION: Chlorinates and brominates suitable organic compounds. Involved in the biosynthesis of the antibiotic pyrrolnitrin.
CATALYTIC ACTIVITY: 2 RH + 2 Cl^- + H₂O₂ = 2 RCl + 2 H₂O.
SUBUNIT: Homodimer.
SIMILARITY: Belongs to the bacterial non-heme bromo- and chloro-peroxidases 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

M60743; AAA02837.1; -; Unassigned_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

JN0828; JN0828.

3D structure databases

HSSP

P49323; 1A88. [HSSP ENTRY / PDB]

SMR

P25026; 4-278.

ModBase

P25026.

Protein family/group databases

PeroxiBase

5912; PpyrHalNPrx.

Ontologies

GO:0016691;	Molecular function: chloride peroxidase activity (inferred from electronic annotation from EC).
QuickGo view.

Family and domain databases

InterPro

IPR003089; AB_hydrolase.
IPR000073; AB_hydrolase_1.
IPR000639; Epox_hydrolase-like.
Graphical view of domain structure.

Pfam

PF00561; Abhydrolase_1; 1.
Pfam graphical view of domain structure.

PRINTS

PR00111; ABHYDROLASE.
PR00412; EPOXHYDRLASE.

Other

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

Keywords

Antibiotic biosynthesis; Chloride; Direct protein sequencing; Oxidoreductase; Peroxidase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed.`
`CHAIN`	`2 278`	`277`	`Non-heme chloroperoxidase.`	`PRO_0000207061`
`ACT_SITE`	`97 97`
`ACT_SITE`	`229 229`
`ACT_SITE`	`258 258`
`MUTAGEN`	`97 97`		`S->A,C: Very low activity.`
`MUTAGEN`	`229 229`		`D->A: Loss of activity.`
`MUTAGEN`	`258 258`		`H->Q: Loss of activity.`

Sequence information

Length: 278 AA [This is the length of the unprocessed precursor]

Molecular weight: 30454 Da [This is the MW of the unprocessed precursor]

CRC64: BD7BEA57466BE463 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPYVTTKDNV EIFYKDWGPK DAQPIVFHHG WPLSGDDWDA QMLFFVQKGY RVIAHDRRGH 

        70         80         90        100        110        120 
GRSAQVSDGH DMDHYAADAF AVVEALDLRN AVHIGHSTGG GEVARYVAND GQPAGRVAKA 

       130        140        150        160        170        180 
VLVSAVPPLM LKTESNPEGL PIEVFDGFRK ALADNRAQFF LDVPTGPFYG FNRAGATVHQ 

       190        200        210        220        230        240 
GVIRNWWRQG MEGSAKAHYD GIKAFSETDQ TEDLKSITVP TLVLHGEDDQ IVPIADAALK 

       250        260        270 
SIKLLQNGTL KTYPGYSHGM LTVNADVLNA DLLAFVQA

P25026 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