Reviewed, UniProtKB/Swiss-Prot P25026 (PRXC_PSEPY)

Names and origin

Protein names

Recommended name:
    Non-heme chloroperoxidase
    EC=1.11.1.10
Alternative name(s):
    Chloride peroxidase
    Chloroperoxidase P
      Short name=CPO-P

Gene names

Name:	cpo
Synonyms:	cpoP

Organism

Pseudomonas pyrrocinia

Taxonomic identifier

60550 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › Burkholderia cepacia complex

Protein attributes

Sequence length	278 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Chlorinates and brominates suitable organic compounds. Involved in the biosynthesis of the antibiotic pyrrolnitrin.
Catalytic activity	RH + Cl- + H2O2 = RCl + 2 H2O.
Subunit structure	Homodimer.
Sequence similarities	Belongs to the bacterial non-heme bromo- and chloro-peroxidases family.

Ontologies

Keywords
Biological process	Antibiotic biosynthesis
Ligand	Chloride
Molecular function	Oxidoreductase Peroxidase
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	antibiotic biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	chloride ion binding Inferred from electronic annotation. Source: UniProtKB-KW chloride peroxidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 278	277	Non-heme chloroperoxidase		PRO_0000207061
Sites
	Active site	97	1
	Active site	229	1
	Active site	258	1
Experimental info
	Mutagenesis	97	1	S → A or C: Very low activity.
	Mutagenesis	229	1	D → A: Loss of activity.
	Mutagenesis	258	1	H → Q: Loss of activity.

Sequences

	Sequence		Length	Mass (Da)
	P25026-1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: BD7BEA57466BE463	FASTA	278	30,454
	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

References

[1]	"Chloroperoxidase-encoding gene from Pseudomonas pyrrocinia: sequence, expression in heterologous hosts, and purification of the enzyme." Wolfframm C., Lingens F., Mutzel R., van Pee K.-H. Gene 130:131-135(1993) [PubMed: 8344520] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]	"A catalytic triad is required by the non-heme haloperoxidases to perform halogenation." Pelletier I., Altenbuchner J., Mattes R. Biochim. Biophys. Acta 1250:149-157(1995) [PubMed: 7632719] [Abstract] Cited for: MUTAGENESIS.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M60743 Unassigned DNA. Translation: AAA02837.1.
PIR	JN0828.
3D structure databases
HSSP	HSSP built from PDB template 1A88 based on UniProtKB P49323.
SMR	P25026. Positions 4-278.
ModBase	Search...
Protein family/group databases
MEROPS	S33.992.
PeroxiBase	5912. PpyrHalNPrx.
Enzyme and pathway databases
BRENDA	1.11.1.10. 229215.
Family and domain databases
InterPro	IPR000073. AB_hydrolase_1. [Graphical view]
Pfam	PF00561. Abhydrolase_1. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PRXC_PSEPY

Accession

Primary (citable) accession number: P25026

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	January 23, 2007
Last modified:	May 26, 2009
This is version 64 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)