Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P04963 (PRXC_CALFU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 99. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Chloroperoxidase

EC=1.11.1.10
Alternative name(s):
Chloride peroxidase
Short name=CPO
Gene names
Name:CPO
OrganismCaldariomyces fumago (Leptoxyphium fumago)
Taxonomic identifier5474 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesDothideomycetidaeCapnodialesCapnodiaceaemitosporic CapnodiaceaeLeptoxyphium

Protein attributes

Sequence length373 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes peroxidative halogenations involved in the biosynthesis of clardariomycin (2,2-dichloro-1,3-cyclo-pentenedione). The enzyme also has potent catalase activity and in the absence of halide ion, acts as a peroxidase similar to plant peroxidases.

Catalytic activity

RH + Cl- + H2O2 = RCl + 2 H2O.

Cofactor

Binds 1 heme B (iron-protoporphyrin IX) group per subunit.

Binds 1 manganese ion per subunit.

Post-translational modification

N- and O-glycosylated.

Sequence similarities

Belongs to the chloroperoxidase family.

Caution

The O-glycosylation on Ser-269 is identified in Ref.8 as D-xylose based on weak electron density. Such a modification has not been reported in the fungi, and the saccharide is probably D-mannose as at the other positions.

Sequence caution

The sequence AAA33026.1 differs from that shown. Reason: Frameshift at position 316.

The sequence CAA28172.1 differs from that shown. Reason: Frameshift at position 316.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020
Chain21 – 319299Chloroperoxidase
PRO_0000023631
Propeptide322 – 37352
PRO_0000023632

Sites

Active site2041
Metal binding501Iron (heme axial ligand)
Metal binding1251Manganese
Metal binding1261Manganese; via carbonyl oxygen
Metal binding1291Manganese

Amino acid modifications

Modified residue211Pyrrolidone carboxylic acid
Glycosylation331N-linked (GlcNAc...)
Glycosylation1141N-linked (GlcNAc...)
Glycosylation2371N-linked (GlcNAc...)
Glycosylation2591O-linked (Man)
Glycosylation2601O-linked (Man)
Glycosylation2621O-linked (Man)
Glycosylation2631O-linked (Man)
Glycosylation2691O-linked (Man) Probable
Glycosylation2711O-linked (Man)
Glycosylation2721O-linked (Man)
Glycosylation2731O-linked (Man)
Glycosylation2961O-linked (Man...)
Glycosylation3041O-linked (Man...)
Glycosylation3141O-linked (Man...)
Disulfide bond100 ↔ 108

Experimental info

Mutagenesis501C → H: Retains most of the chlorination, peroxidation, epoxidation, and catalase activities. Ref.7

Secondary structure

......................................... 373
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P04963 [UniParc].

Last modified March 27, 2002. Version 3.
Checksum: B90085902112E83D

FASTA37340,504
        10         20         30         40         50         60 
MFSKVLPFVG AVAALPHSVR QEPGSGIGYP YDNNTLPYVA PGPTDSRAPC PALNALANHG 

        70         80         90        100        110        120 
YIPHDGRAIS RETLQNAFLN HMGIANSVIE LALTNAFVVC EYVTGSDCGD SLVNLTLLAE 

       130        140        150        160        170        180 
PHAFEHDHSF SRKDYKQGVA NSNDFIDNRN FDAETFQTSL DVVAGKTHFD YADMNEIRLQ 

       190        200        210        220        230        240 
RESLSNELDF PGWFTESKPI QNVESGFIFA LVSDFNLPDN DENPLVRIDW WKYWFTNESF 

       250        260        270        280        290        300 
PYHLGWHPPS PAREIEFVTS ASSAVLAASV TSTPSSLPSG AIGPGAEAVP LSFASTMTPF 

       310        320        330        340        350        360 
LLATNAPYYA QDPTLGPNDK REAAPAATTS MAVFKNPYLE AIGTQDIKNQ QAYVSSKAAA 

       370 
MASAMAANKA RNL 

« Hide

References

[1]"Cloning and sequencing of chloroperoxidase cDNA."
Fang G.-H., Kenigsberg P., Axley M.J., Nuell M., Hager L.P.
Nucleic Acids Res. 14:8061-8071(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
Strain: ATCC 16373 / DSM 1256 / SC 3815.
[2]"Isolation and nucleotide sequence of the chloroperoxidase gene from Caldariomyces fumago."
Nuell M.J., Fang G.-H., Axley M.J., Kenigsberg P., Hager L.P.
J. Bacteriol. 170:1007-1011(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Expression of the Caldariomyces fumago Chloroperoxidase in Aspergillus niger and characterization of the recombinant enzyme."
Conesa A., an de Velde F., van Rantwijk F., Sheldon R.A., van den Hondel C.A.M.J.J., Punt P.J.
J. Biol. Chem. 276:17635-17640(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Fructose induces and glucose represses chloroperoxidase mRNA levels."
Axley M.J., Kenigsberg P., Hager L.P.
J. Biol. Chem. 261:15058-15061(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-175.
[5]Hager L.P.
Unpublished observations (FEB-1996)
Cited for: SEQUENCE REVISION TO C-TERMINUS.
[6]"Identification of the fifth axial heme ligand of chloroperoxidase."
Blanke S.R., Hager L.P.
J. Biol. Chem. 263:18739-18743(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: DETERMINATION OF HEME LIGAND.
[7]"Replacement of the proximal heme thiolate ligand in chloroperoxidase with a histidine residue."
Yi X., Mroczko M., Manoj K.M., Wang X., Hager L.P.
Proc. Natl. Acad. Sci. U.S.A. 96:12412-12417(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF CYS-50.
[8]"The crystal structure of chloroperoxidase: a heme peroxidase-cytochrome P450 functional hybrid."
Sundaramoorthy M., Terner J., Poulos T.L.
Structure 3:1367-1377(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Strain: ATCC 16373 / DSM 1256 / SC 3815.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04486 mRNA. Translation: CAA28172.1. Frameshift.
M19025 Genomic DNA. Translation: AAA33026.1. Frameshift.
AJ300448 Genomic DNA. Translation: CAC16733.1.
M28651 mRNA. Translation: AAA33025.1.
PIRA28557.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CPOX-ray1.90A22-319[»]
2CIVX-ray1.80A22-319[»]
2CIWX-ray1.15A22-319[»]
2CIXX-ray1.80A22-319[»]
2CIYX-ray1.70A22-319[»]
2CIZX-ray1.30A22-319[»]
2CJ0X-ray1.75A22-319[»]
2CJ1X-ray1.70A22-319[»]
2CJ2X-ray1.60A22-319[»]
2CPOX-ray2.10A22-319[»]
2J18X-ray1.75A22-319[»]
2J19X-ray1.75A22-319[»]
2J5MX-ray1.75A22-319[»]
ProteinModelPortalP04963.
SMRP04963. Positions 21-319.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

PeroxiBase4070. CfuHalPrx.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.489.10. 1 hit.
InterProIPR000028. Chloroperoxidase.
[Graphical view]
PfamPF01328. Peroxidase_2. 1 hit.
[Graphical view]
SUPFAMSSF47571. SSF47571. 2 hits.
PROSITEPS51405. HEME_HALOPEROXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP04963.

Entry information

Entry namePRXC_CALFU
AccessionPrimary (citable) accession number: P04963
Secondary accession number(s): Q92216, Q9HFP2
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: March 27, 2002
Last modified: October 16, 2013
This is version 99 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references