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P04963

- PRXC_CALFU

UniProt

P04963 - PRXC_CALFU

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Protein

Chloroperoxidase

Gene
CPO
Organism
Caldariomyces fumago (Leptoxyphium fumago)
Status
Reviewed - 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

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi50 – 501Iron (heme axial ligand)
Metal bindingi125 – 1251Manganese
Metal bindingi126 – 1261Manganese; via carbonyl oxygen
Metal bindingi129 – 1291Manganese
Active sitei204 – 2041

GO - Molecular functioni

  1. chloride peroxidase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
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
OrganismiCaldariomyces fumago (Leptoxyphium fumago)
Taxonomic identifieri5474 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaDothideomycetesDothideomycetidaeCapnodialesCapnodiaceaemitosporic CapnodiaceaeLeptoxyphium

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi50 – 501C → H: Retains most of the chlorination, peroxidation, epoxidation, and catalase activities. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2020Add
BLAST
Chaini21 – 319299ChloroperoxidasePRO_0000023631Add
BLAST
Propeptidei322 – 37352PRO_0000023632Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei21 – 211Pyrrolidone carboxylic acid
Glycosylationi33 – 331N-linked (GlcNAc...)
Disulfide bondi100 ↔ 108
Glycosylationi114 – 1141N-linked (GlcNAc...)
Glycosylationi237 – 2371N-linked (GlcNAc...)
Glycosylationi259 – 2591O-linked (Man)
Glycosylationi260 – 2601O-linked (Man)
Glycosylationi262 – 2621O-linked (Man)
Glycosylationi263 – 2631O-linked (Man)
Glycosylationi269 – 2691O-linked (Man) Inferred
Glycosylationi271 – 2711O-linked (Man)
Glycosylationi272 – 2721O-linked (Man)
Glycosylationi273 – 2731O-linked (Man)
Glycosylationi296 – 2961O-linked (Man...)
Glycosylationi304 – 3041O-linked (Man...)
Glycosylationi314 – 3141O-linked (Man...)

Post-translational modificationi

N- and O-glycosylated.

Keywords - PTMi

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

Structurei

Secondary structure

1
373
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi23 – 253
Turni27 – 315
Helixi51 – 588
Beta strandi67 – 693
Helixi71 – 8212
Helixi86 – 10419
Beta strandi111 – 1155
Helixi116 – 1194
Turni121 – 1244
Beta strandi130 – 1323
Helixi153 – 16210
Turni163 – 1653
Beta strandi167 – 1693
Helixi171 – 18818
Turni191 – 1933
Helixi198 – 21215
Turni218 – 2225
Helixi228 – 23710
Helixi242 – 2443
Helixi255 – 26713
Turni311 – 3144

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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. Positions 21-319.

Miscellaneous databases

EvolutionaryTraceiP04963.

Family & Domainsi

Sequence similaritiesi

Belongs to the chloroperoxidase family.

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

MFSKVLPFVG AVAALPHSVR QEPGSGIGYP YDNNTLPYVA PGPTDSRAPC    50
PALNALANHG YIPHDGRAIS RETLQNAFLN HMGIANSVIE LALTNAFVVC 100
EYVTGSDCGD SLVNLTLLAE PHAFEHDHSF SRKDYKQGVA NSNDFIDNRN 150
FDAETFQTSL DVVAGKTHFD YADMNEIRLQ RESLSNELDF PGWFTESKPI 200
QNVESGFIFA LVSDFNLPDN DENPLVRIDW WKYWFTNESF PYHLGWHPPS 250
PAREIEFVTS ASSAVLAASV TSTPSSLPSG AIGPGAEAVP LSFASTMTPF 300
LLATNAPYYA QDPTLGPNDK REAAPAATTS MAVFKNPYLE AIGTQDIKNQ 350
QAYVSSKAAA MASAMAANKA RNL 373
Length:373
Mass (Da):40,504
Last modified:March 27, 2002 - v3
Checksum:iB90085902112E83D
GO

Sequence cautioni

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 databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P04963.
SMRi P04963. Positions 21-319.
ModBasei Search...
MobiDBi Search...

Protein family/group databases

PeroxiBasei 4070. CfuHalPrx.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei P04963.

Family and domain databases

Gene3Di 1.10.489.10. 1 hit.
InterProi IPR000028. Chloroperoxidase.
[Graphical view ]
Pfami PF01328. Peroxidase_2. 1 hit.
[Graphical view ]
SUPFAMi SSF47571. SSF47571. 2 hits.
PROSITEi PS51405. HEME_HALOPEROXIDASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. 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.

Entry informationi

Entry nameiPRXC_CALFU
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: October 16, 2013
This is version 99 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 1 Publication 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.

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

External Data

Dasty 3