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P04963

- PRXC_CALFU

UniProt

P04963 - PRXC_CALFU

Protein

Chloroperoxidase

Gene

CPO

Organism
Caldariomyces fumago (Leptoxyphium fumago)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 100 (01 Oct 2014)
      Sequence version 3 (27 Mar 2002)
      Previous versions | rss
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    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

    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)Curated
    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.
    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

    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 1, 2014
    This is version 100 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

    External Data

    Dasty 3