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UniProtKB/Swiss-Prot entry P04963


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PRXC_CALFU
Primary accession number P04963
Secondary accession numbers Q92216 Q9HFP2
Integrated into Swiss-Prot on August 13, 1987
Sequence was last modified on March 27, 2002 (Sequence version 3)
Annotations were last modified on    September 2, 2008 (Entry version 77)
Name and origin of the protein
Protein name Chloroperoxidase [Precursor]
Synonyms EC 1.11.1.10
Chloride peroxidase
CPO
Gene name
Name: CPO
From
Caldariomyces fumago (Leptoxyphium fumago) [TaxID: 5474] 
Taxonomy Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes; Dothideomycetidae; Capnodiales; Capnodiaceae; mitosporic Capnodiaceae; Leptoxyphium.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=ATCC 16373 / DSM 1256 / SC 3815;
DOI=10.1093/nar/14.20.8061; PubMed=3774552 [NCBI, ExPASy, EBI, Israel, Japan]
Fang G.-H., Kenigsberg P., Axley M.J., Nuell M., Hager L.P.;
"Cloning and sequencing of chloroperoxidase cDNA.";
Nucleic Acids Res. 14:8061-8071(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2828306 [NCBI, ExPASy, EBI, Israel, Japan]
Nuell M.J., Fang G.-H., Axley M.J., Kenigsberg P., Hager L.P.;
"Isolation and nucleotide sequence of the chloroperoxidase gene from Caldariomyces fumago.";
J. Bacteriol. 170:1007-1011(1988).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1074/jbc.M010571200; PubMed=11278701 [NCBI, ExPASy, EBI, Israel, Japan]
Conesa A., an de Velde F., van Rantwijk F., Sheldon R.A., van den Hondel C.A.M.J.J., Punt P.J.;
"Expression of the Caldariomyces fumago Chloroperoxidase in Aspergillus niger and characterization of the recombinant enzyme.";
J. Biol. Chem. 276:17635-17640(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-175.
PubMed=3771564 [NCBI, ExPASy, EBI, Israel, Japan]
Axley M.J., Kenigsberg P., Hager L.P.;
"Fructose induces and glucose represses chloroperoxidase mRNA levels.";
J. Biol. Chem. 261:15058-15061(1986).
[5]
SEQUENCE REVISION TO C-TERMINUS.
Hager L.P.;
Unpublished observations (FEB-1996).
[6]
DETERMINATION OF HEME LIGAND.
PubMed=3198598 [NCBI, ExPASy, EBI, Israel, Japan]
Blanke S.R., Hager L.P.;
"Identification of the fifth axial heme ligand of chloroperoxidase.";
J. Biol. Chem. 263:18739-18743(1988).
[7]
MUTAGENESIS OF CYS-50.
DOI=10.1073/pnas.96.22.12412; PubMed=10535936 [NCBI, ExPASy, EBI, Israel, Japan]
Yi X., Mroczko M., Manoj K.M., Wang X., Hager L.P.;
"Replacement of the proximal heme thiolate ligand in chloroperoxidase with a histidine residue.";
Proc. Natl. Acad. Sci. U.S.A. 96:12412-12417(1999).
[8]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
STRAIN=ATCC 16373 / DSM 1256 / SC 3815;
DOI=10.1016/S0969-2126(01)00274-X; PubMed=8747463 [NCBI, ExPASy, EBI, Israel, Japan]
Sundaramoorthy M., Terner J., Poulos T.L.;
"The crystal structure of chloroperoxidase: a heme peroxidase-cytochrome P450 functional hybrid.";
Structure 3:1367-1377(1995).
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: 2 RH + 2 Cl- + H2O2 = 2 RCl + 2 H2O.
  • COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per subunit.
  • COFACTOR: Binds 1 manganese ion per subunit.
  • PTM: N- and O-glycosylated.
  • SIMILARITY: 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:
    • Sequence=AAA33026.1; Type=Frameshift; Positions=316;
    • Sequence=CAA28172.1; Type=Frameshift; Positions=316;
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X04486; CAA28172.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M19025; AAA33026.1; ALT_FRAME; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ300448; CAC16733.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M28651; AAA33025.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A28557; A28557.
3D structure databases
PDB
1CPO; X-ray; 1.90 A; A=21-319.[ExPASy / RCSB / EBI]
2CIV; X-ray; 1.80 A; A=21-319.[ExPASy / RCSB / EBI]
2CIW; X-ray; 1.15 A; A=21-319.[ExPASy / RCSB / EBI]
2CIX; X-ray; 1.80 A; A=21-319.[ExPASy / RCSB / EBI]
2CIY; X-ray; 1.70 A; A=21-319.[ExPASy / RCSB / EBI]
2CIZ; X-ray; 1.30 A; A=21-319.[ExPASy / RCSB / EBI]
2CJ0; X-ray; 1.75 A; A=21-319.[ExPASy / RCSB / EBI]
2CJ1; X-ray; 1.70 A; A=21-319.[ExPASy / RCSB / EBI]
2CJ2; X-ray; 1.60 A; A=21-319.[ExPASy / RCSB / EBI]
2CPO; X-ray; 2.10 A; A=21-319.[ExPASy / RCSB / EBI]
2J18; X-ray; 1.75 A; A=21-319.[ExPASy / RCSB / EBI]
2J19; X-ray; 1.75 A; A=21-319.[ExPASy / RCSB / EBI]
2J5M; X-ray; 1.75 A; A=22-319.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1CPO; -.
2CIV; -.
2CIW; -.
2CIX; -.
2CIY; -.
2CIZ; -.
2CJ0; -.
2CJ1; -.
2CJ2; -.
2CPO; -.
2J18; -.
2J19; -.
2J5M; -.
ModBase P04963.
Protein family/group databases
PeroxiBase 4070; CfuHalPrx.
Family and domain databases
InterPro IPR000028; Chloroperoxidase.
Graphical view of domain structure.
Gene3D G3DSA:1.10.489.10; Chloroperoxidase; 1.
Pfam PF01328; Peroxidase_2; 1.
Pfam graphical view of domain structure.
ProDom PD040763; Chloroperoxidase; 1.
[Domain structure / List of seq. sharing at least 1 domain]
BLOCKS P04963.
Other
LinkHub P04963; -.
ProtoNet P04963.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Chloride; Cleavage on pair of basic residues; Direct protein sequencing; Glycoprotein; Heme; Iron; Manganese; Metal-binding; Oxidoreductase; Peroxidase; Pyrrolidone carboxylic acid; Signal.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    20  20      
CHAIN   21   319  299     Chloroperoxidase. PRO_0000023631
PROPEP   322   373  52      PRO_0000023632
ACT_SITE   204   204         
METAL   50    50        Iron (heme axial ligand). 
METAL   125   125        Manganese. 
METAL   126   126        Manganese; via carbonyl oxygen. 
METAL   129   129        Manganese. 
MOD_RES   21    21        Pyrrolidone carboxylic acid. 
CARBOHYD   33    33        N-linked (GlcNAc...). 
CARBOHYD   114   114        N-linked (GlcNAc...). 
CARBOHYD   237   237        N-linked (GlcNAc...). 
CARBOHYD   259   259        O-linked (Man). 
CARBOHYD   260   260        O-linked (Man). 
CARBOHYD   262   262        O-linked (Man). 
CARBOHYD   263   263        O-linked (Man). 
CARBOHYD   269   269        O-linked (Man) (Probable). 
CARBOHYD   271   271        O-linked (Man). 
CARBOHYD   272   272        O-linked (Man). 
CARBOHYD   273   273        O-linked (Man). 
CARBOHYD   296   296        O-linked (Man...). 
CARBOHYD   304   304        O-linked (Man...). 
CARBOHYD   314   314        O-linked (Man...). 
DISULFID   100   108         
MUTAGEN   50    50        C->H: Retains most of the chlorination, peroxidation, epoxidation, and catalase activities. 
HELIX   23    25  3      
TURN   27    31  5      
HELIX   51    58  8      
STRAND   67    69  3      
HELIX   71    82  12      
HELIX   86   104  19      
STRAND   111   115  5      
HELIX   116   119  4      
TURN   121   124  4      
STRAND   130   132  3      
HELIX   153   162  10      
TURN   163   165  3      
STRAND   167   169  3      
HELIX   171   188  18      
TURN   191   193  3      
HELIX   198   212  15      
TURN   218   222  5      
HELIX   228   237  10      
HELIX   242   244  3      
HELIX   255   267  13      
Sequence information
Length: 373 AA [This is the length of the unprocessed precursor] Molecular weight: 40504 Da [This is the MW of the unprocessed precursor] CRC64: B90085902112E83D [This is a checksum on the sequence]
        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 

P04963 in FASTA format

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