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UniProtKB - P04963 (PRXC_LEPFU)
Protein
Chloroperoxidase
Gene
CPO
Organism
Leptoxyphium fumago (Caldariomyces fumago)
Status
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.
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
Catalytic activityi
- RH + Cl(-) + H(2)O(2) = RCl + 2 H(2)O. EC:1.11.1.10
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 50 | Iron (heme axial ligand) | 1 | |
Metal bindingi | 125 | Manganese | 1 | |
Metal bindingi | 126 | Manganese; via carbonyl oxygen | 1 | |
Metal bindingi | 129 | Manganese | 1 | |
Active sitei | 204 | 1 |
GO - Molecular functioni
- chloride peroxidase activity Source: UniProtKB-EC
- metal ion binding Source: UniProtKB-KW
Keywordsi
Molecular function | Oxidoreductase, Peroxidase |
Ligand | Chloride, Heme, Iron, Manganese, Metal-binding |
Enzyme and pathway databases
BRENDAi | 1.11.1.10, 1053 |
Protein family/group databases
PeroxiBasei | 4070, 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 |
Organismi | Leptoxyphium fumago (Caldariomyces fumago) |
Taxonomic identifieri | 5474 [NCBI] |
Taxonomic lineagei | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Dothideomycetes › Dothideomycetidae › Capnodiales › Capnodiaceae › Leptoxyphium |
Pathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 50 | C → H: Retains most of the chlorination, peroxidation, epoxidation, and catalase activities. 1 Publication | 1 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 20 | Add BLAST | 20 | |
ChainiPRO_0000023631 | 21 – 319 | ChloroperoxidaseAdd BLAST | 299 | |
PropeptideiPRO_0000023632 | 322 – 373 | Add BLAST | 52 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 21 | Pyrrolidone carboxylic acid1 Publication | 1 | |
Glycosylationi | 33 | N-linked (GlcNAc...) asparagine | 1 | |
Disulfide bondi | 100 ↔ 108 | |||
Glycosylationi | 114 | N-linked (GlcNAc...) asparagine | 1 | |
Glycosylationi | 237 | N-linked (GlcNAc...) asparagine | 1 | |
Glycosylationi | 259 | O-linked (Man) threonine | 1 | |
Glycosylationi | 260 | O-linked (Man) serine | 1 | |
Glycosylationi | 262 | O-linked (Man) serine | 1 | |
Glycosylationi | 263 | O-linked (Man) serine | 1 | |
Glycosylationi | 269 | O-linked (Man) serineCurated | 1 | |
Glycosylationi | 271 | O-linked (Man) threonine | 1 | |
Glycosylationi | 272 | O-linked (Man) serine | 1 | |
Glycosylationi | 273 | O-linked (Man) threonine | 1 | |
Glycosylationi | 296 | O-linked (Man...) threonine | 1 | |
Glycosylationi | 304 | O-linked (Man...) threonine | 1 | |
Glycosylationi | 314 | O-linked (Man...) threonine | 1 |
Post-translational modificationi
N- and O-glycosylated.
Keywords - PTMi
Cleavage on pair of basic residues, Disulfide bond, Glycoprotein, Pyrrolidone carboxylic acidStructurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P04963 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P04963 |
Family & Domainsi
Sequence similaritiesi
Belongs to the chloroperoxidase family.Curated
Keywords - Domaini
SignalFamily and domain databases
Gene3Di | 1.10.489.10, 1 hit |
InterProi | View protein in InterPro IPR000028, Chloroperoxidase IPR036851, Chloroperoxidase-like_sf |
Pfami | View protein in Pfam PF01328, Peroxidase_2, 1 hit |
SUPFAMi | SSF47571, SSF47571, 2 hits |
PROSITEi | View protein in PROSITE PS51405, HEME_HALOPEROXIDASE, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P04963-1 [UniParc]FASTAAdd to basket
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
Sequence cautioni
The sequence AAA33026 differs from that shown. Reason: Frameshift.Curated
The sequence CAA28172 differs from that shown. Reason: Frameshift.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 |
PIRi | A28557 |
Similar proteinsi
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 |
PIRi | A28557 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1CPO | X-ray | 1.90 | A | 22-319 | [»] | |
2CIV | X-ray | 1.80 | A | 22-319 | [»] | |
2CIW | X-ray | 1.15 | A | 22-319 | [»] | |
2CIX | X-ray | 1.80 | A | 22-319 | [»] | |
2CIY | X-ray | 1.70 | A | 22-319 | [»] | |
2CIZ | X-ray | 1.30 | A | 22-319 | [»] | |
2CJ0 | X-ray | 1.75 | A | 22-319 | [»] | |
2CJ1 | X-ray | 1.70 | A | 22-319 | [»] | |
2CJ2 | X-ray | 1.60 | A | 22-319 | [»] | |
2CPO | X-ray | 2.10 | A | 22-319 | [»] | |
2J18 | X-ray | 1.75 | A | 22-319 | [»] | |
2J19 | X-ray | 1.75 | A | 22-319 | [»] | |
2J5M | X-ray | 1.75 | A | 22-319 | [»] | |
SMRi | P04963 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein family/group databases
PeroxiBasei | 4070, CfuHalPrx |
Enzyme and pathway databases
BRENDAi | 1.11.1.10, 1053 |
Miscellaneous databases
EvolutionaryTracei | P04963 |
Family and domain databases
Gene3Di | 1.10.489.10, 1 hit |
InterProi | View protein in InterPro IPR000028, Chloroperoxidase IPR036851, Chloroperoxidase-like_sf |
Pfami | View protein in Pfam PF01328, Peroxidase_2, 1 hit |
SUPFAMi | SSF47571, SSF47571, 2 hits |
PROSITEi | View protein in PROSITE PS51405, HEME_HALOPEROXIDASE, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | PRXC_LEPFU | |
Accessioni | P04963Primary (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: | June 2, 2021 | |
This is version 119 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Fungal Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families