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P49053 (PRXC_CURIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Vanadium chloroperoxidase

EC=1.11.1.10
Alternative name(s):
Vanadium chloride peroxidase
Short name=VCPO
Gene names
Name:CPO
OrganismCurvularia inaequalis
Taxonomic identifier38902 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesPleosporomycetidaePleosporalesPleosporineaePleosporaceaeCurvularia

Protein attributes

Sequence length609 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Cofactor

Vanadium.

Subcellular location

Secreted.

Post-translational modification

The N-terminus is blocked.

Ontologies

Keywords
   Cellular componentSecreted
   LigandChloride
Metal-binding
Vanadium
   Molecular functionOxidoreductase
Peroxidase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

membrane

Inferred from electronic annotation. Source: InterPro

   Molecular_functionchloride peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 609609Vanadium chloroperoxidase
PRO_0000097055

Sites

Active site4041
Metal binding4961Vanadium

Experimental info

Sequence conflict4541P → S AA sequence Ref.1

Secondary structure

................................................................................. 609
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P49053 [UniParc].

Last modified February 1, 1996. Version 1.
Checksum: A7B710DDF937D3E9

FASTA60967,531
        10         20         30         40         50         60 
MGSVTPIPLP KIDEPEEYNT NYILFWNHVG LELNRVTHTV GGPLTGPPLS ARALGMLHLA 

        70         80         90        100        110        120 
IHDAYFSICP PTDFTTFLSP DTENAAYRLP SPNGANDARQ AVAGAALKML SSLYMKPVEQ 

       130        140        150        160        170        180 
PNPNPGANIS DNAYAQLGLV LDRSVLEAPG GVDRESASFM FGEDVADVFF ALLNDPRGAS 

       190        200        210        220        230        240 
QEGYHPTPGR YKFDDEPTHP VVLIPVDPNN PNGPKMPFRQ YHAPFYGKTT KRFATQSEHF 

       250        260        270        280        290        300 
LADPPGLRSN ADETAEYDDA VRVAIAMGGA QALNSTKRSP WQTAQGLYWA YDGSNLIGTP 

       310        320        330        340        350        360 
PRFYNQIVRR IAVTYKKEED LANSEVNNAD FARLFALVDV ACTDAGIFSW KEKWEFEFWR 

       370        380        390        400        410        420 
PLSGVRDDGR PDHGDPFWLT LGAPATNTND IPFKPPFPAY PSGHATFGGA VFQMVRRYYN 

       430        440        450        460        470        480 
GRVGTWKDDE PDNIAIDMMI SEELNGVNRD LRQPYDPTAP IEDQPGIVRT RIVRHFDSAW 

       490        500        510        520        530        540 
ELMFENAISR IFLGVHWRFD AAAARDILIP TTTKDVYAVD NNGATVFQNV EDIRYTTRGT 

       550        560        570        580        590        600 
REDPEGLFPI GGVPLGIEIA DEIFNNGLKP TPPEIQPMPQ ETPVQKPVGQ QPVKGMWEEE 


QAPVVKEAP 

« Hide

References

[1]"Primary structure and characterization of the vanadium chloroperoxidase from the fungus Curvularia inaequalis."
Simons B.H., Barnett P., Vollenbroek E.G.M., Dekker H.L., Muijsers A.O., Messerschmidt A., Wever R.
Eur. J. Biochem. 229:566-574(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]"X-ray structure of a vanadium-containing enzyme: chloroperoxidase from the fungus Curvularia inaequalis."
Messerschmidt A., Wever R.
Proc. Natl. Acad. Sci. U.S.A. 93:392-396(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X85369 mRNA. Translation: CAA59686.1.
PIRS69334.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1IDQX-ray2.03A1-609[»]
1IDUX-ray2.24A1-609[»]
1VNCX-ray2.10A1-609[»]
1VNEX-ray2.15A1-609[»]
1VNFX-ray2.35A1-609[»]
1VNGX-ray2.20A1-609[»]
1VNHX-ray2.11A1-609[»]
1VNIX-ray2.15A1-609[»]
1VNSX-ray1.66A1-609[»]
3BB0X-ray1.50A1-609[»]
ProteinModelPortalP49053.
SMRP49053. Positions 3-578.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

PeroxiBase5892. CinaVCPo.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15997.
SABIO-RKP49053.

Family and domain databases

Gene3D1.10.606.10. 1 hit.
1.20.144.10. 1 hit.
InterProIPR016119. Br/Cl_peroxidase_C.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
PfamPF01569. PAP2. 1 hit.
[Graphical view]
SUPFAMSSF48317. SSF48317. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP49053.

Entry information

Entry namePRXC_CURIN
AccessionPrimary (citable) accession number: P49053
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: February 1, 1996
Last modified: January 22, 2014
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references