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Protein

Chloroperoxidase

Gene

CPO

Organism
Leptoxyphium fumago (Caldariomyces fumago)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

Cofactori

Protein has several cofactor binding sites:
  • heme bNote: Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit.
  • Mn2+Note: Binds 1 Mn2+ ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi50Iron (heme axial ligand)1
Metal bindingi125Manganese1
Metal bindingi126Manganese; via carbonyl oxygen1
Metal bindingi129Manganese1
Active sitei2041

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Ligandi

Chloride, Heme, Iron, Manganese, Metal-binding

Protein family/group databases

PeroxiBasei4070. CfuHalPrx.

Names & Taxonomyi

Protein namesi
Recommended name:
Chloroperoxidase (EC:1.11.1.10)
Alternative name(s):
Chloride peroxidase
Short name:
CPO
Gene namesi
Name:CPO
OrganismiLeptoxyphium fumago (Caldariomyces fumago)
Taxonomic identifieri5474 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesDothideomycetidaeCapnodialesCapnodiaceaeLeptoxyphium

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi50C → H: Retains most of the chlorination, peroxidation, epoxidation, and catalase activities. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 20Add BLAST20
ChainiPRO_000002363121 – 319ChloroperoxidaseAdd BLAST299
PropeptideiPRO_0000023632322 – 373Add BLAST52

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei21Pyrrolidone carboxylic acid1
Glycosylationi33N-linked (GlcNAc...)1
Disulfide bondi100 ↔ 108
Glycosylationi114N-linked (GlcNAc...)1
Glycosylationi237N-linked (GlcNAc...)1
Glycosylationi259O-linked (Man)1
Glycosylationi260O-linked (Man)1
Glycosylationi262O-linked (Man)1
Glycosylationi263O-linked (Man)1
Glycosylationi269O-linked (Man)Curated1
Glycosylationi271O-linked (Man)1
Glycosylationi272O-linked (Man)1
Glycosylationi273O-linked (Man)1
Glycosylationi296O-linked (Man...)1
Glycosylationi304O-linked (Man...)1
Glycosylationi314O-linked (Man...)1

Post-translational modificationi

N- and O-glycosylated.

Keywords - PTMi

Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acid

Structurei

Secondary structure

1373
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi23 – 25Combined sources3
Turni27 – 31Combined sources5
Helixi51 – 58Combined sources8
Beta strandi67 – 69Combined sources3
Helixi71 – 82Combined sources12
Helixi86 – 104Combined sources19
Beta strandi111 – 115Combined sources5
Helixi116 – 119Combined sources4
Turni121 – 124Combined sources4
Beta strandi130 – 132Combined sources3
Helixi153 – 162Combined sources10
Turni163 – 165Combined sources3
Beta strandi167 – 169Combined sources3
Helixi171 – 188Combined sources18
Turni191 – 193Combined sources3
Helixi198 – 212Combined sources15
Turni218 – 222Combined sources5
Helixi228 – 237Combined sources10
Helixi242 – 244Combined sources3
Helixi255 – 267Combined sources13
Turni311 – 314Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP04963.
SMRiP04963.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP04963.

Family & Domainsi

Sequence similaritiesi

Belongs to the chloroperoxidase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di1.10.489.10. 1 hit.
InterProiIPR000028. Chloroperoxidase.
[Graphical view]
PfamiPF01328. Peroxidase_2. 1 hit.
[Graphical view]
SUPFAMiSSF47571. SSF47571. 2 hits.
PROSITEiPS51405. HEME_HALOPEROXIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P04963-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFSKVLPFVG AVAALPHSVR QEPGSGIGYP YDNNTLPYVA PGPTDSRAPC
60 70 80 90 100
PALNALANHG YIPHDGRAIS RETLQNAFLN HMGIANSVIE LALTNAFVVC
110 120 130 140 150
EYVTGSDCGD SLVNLTLLAE PHAFEHDHSF SRKDYKQGVA NSNDFIDNRN
160 170 180 190 200
FDAETFQTSL DVVAGKTHFD YADMNEIRLQ RESLSNELDF PGWFTESKPI
210 220 230 240 250
QNVESGFIFA LVSDFNLPDN DENPLVRIDW WKYWFTNESF PYHLGWHPPS
260 270 280 290 300
PAREIEFVTS ASSAVLAASV TSTPSSLPSG AIGPGAEAVP LSFASTMTPF
310 320 330 340 350
LLATNAPYYA QDPTLGPNDK REAAPAATTS MAVFKNPYLE AIGTQDIKNQ
360 370
QAYVSSKAAA MASAMAANKA RNL
Length:373
Mass (Da):40,504
Last modified:March 27, 2002 - v3
Checksum:iB90085902112E83D
GO

Sequence cautioni

The sequence AAA33026 differs from that shown. Reason: Frameshift at position 316.Curated
The sequence CAA28172 differs from that shown. Reason: Frameshift at position 316.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04486 mRNA. Translation: CAA28172.1. Frameshift.
M19025 Genomic DNA. Translation: AAA33026.1. Frameshift.
AJ300448 Genomic DNA. Translation: CAC16733.1.
M28651 mRNA. Translation: AAA33025.1.
PIRiA28557.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04486 mRNA. Translation: CAA28172.1. Frameshift.
M19025 Genomic DNA. Translation: AAA33026.1. Frameshift.
AJ300448 Genomic DNA. Translation: CAC16733.1.
M28651 mRNA. Translation: AAA33025.1.
PIRiA28557.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
ProteinModelPortaliP04963.
SMRiP04963.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

PeroxiBasei4070. CfuHalPrx.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP04963.

Family and domain databases

Gene3Di1.10.489.10. 1 hit.
InterProiIPR000028. Chloroperoxidase.
[Graphical view]
PfamiPF01328. Peroxidase_2. 1 hit.
[Graphical view]
SUPFAMiSSF47571. SSF47571. 2 hits.
PROSITEiPS51405. HEME_HALOPEROXIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPRXC_LEPFU
AccessioniPrimary (citable) accession number: P04963
Secondary accession number(s): Q92216, Q9HFP2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: March 27, 2002
Last modified: November 2, 2016
This is version 107 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Caution

The O-glycosylation on Ser-269 is identified in PubMed:8747463 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.Curated

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.