Reviewed, UniProtKB/Swiss-Prot P04963 (PRXC_CALFU)

Names and origin

Protein names

Recommended name:
    Chloroperoxidase
    EC=1.11.1.10
Alternative name(s):
    Chloride peroxidase
      Short name=CPO

Gene names

Name:

CPO

Organism

Caldariomyces fumago (Leptoxyphium fumago)

Taxonomic identifier

5474 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Dothideomycetes › Dothideomycetidae › Capnodiales › Capnodiaceae › mitosporic Capnodiaceae › Leptoxyphium

Protein attributes

Sequence length	373 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (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	RH + Cl- + H2O2 = RCl + 2 H2O.
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per subunit. Binds 1 manganese ion per subunit.
Post-translational modification	N- and O-glycosylated.
Sequence similarities	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	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.

Ontologies

Keywords
Domain	Signal
Ligand	Chloride Heme Iron Manganese Metal-binding
Molecular function	Oxidoreductase Peroxidase
PTM	Cleavage on pair of basic residues Disulfide bond Glycoprotein Pyrrolidone carboxylic acid
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	chloride ion binding Inferred from electronic annotation. Source: UniProtKB-KW chloride peroxidase activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW manganese ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 20

20

Chain

21 – 319

299

Chloroperoxidase

PRO_0000023631

Propeptide

322 – 373

52

PRO_0000023632

Sites

Active site

204

1

Metal binding

50

1

Iron (heme axial ligand)

Metal binding

125

1

Manganese

Metal binding

126

1

Manganese; via carbonyl oxygen

Metal binding

129

1

Manganese

Amino acid modifications

Modified residue

21

1

Pyrrolidone carboxylic acid

Glycosylation

33

1

N-linked (GlcNAc...)

Glycosylation

114

1

N-linked (GlcNAc...)

Glycosylation

237

1

N-linked (GlcNAc...)

Glycosylation

259

1

O-linked (Man)

Glycosylation

260

1

O-linked (Man)

Glycosylation

262

1

O-linked (Man)

Glycosylation

263

1

O-linked (Man)

Glycosylation

269

1

O-linked (Man) Probable

Glycosylation

271

1

O-linked (Man)

Glycosylation

272

1

O-linked (Man)

Glycosylation

273

1

O-linked (Man)

Glycosylation

296

1

O-linked (Man...)

Glycosylation

304

1

O-linked (Man...)

Glycosylation

314

1

O-linked (Man...)

Disulfide bond

100 ↔ 108

Experimental info

Mutagenesis

50

1

C → H: Retains most of the chlorination, peroxidation, epoxidation, and catalase activities. Ref.7

Secondary structure

1

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373

Helix Strand Turn

Details...

Helix

23 – 25

3

Turn

27 – 31

5

Helix

51 – 58

8

Beta strand

67 – 69

3

Helix

71 – 82

12

Helix

86 – 104

19

Beta strand

111 – 115

5

Helix

116 – 119

4

Turn

121 – 124

4

Beta strand

130 – 132

3

Helix

153 – 162

10

Turn

163 – 165

3

Beta 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

Sequences

	Sequence		Length	Mass (Da)
	P04963-1 [UniParc]. Last modified March 27, 2002. Version 3. Checksum: B90085902112E83D	FASTA	373	40,504
	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

References

[1]	"Cloning and sequencing of chloroperoxidase cDNA." Fang G.-H., Kenigsberg P., Axley M.J., Nuell M., Hager L.P. Nucleic Acids Res. 14:8061-8071(1986) [PubMed: 3774552] [Abstract] 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: 2828306] [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: 11278701] [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: 3771564] [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: 3198598] [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: 10535936] [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: 8747463] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS). Strain: ATCC 16373 / DSM 1256 / SC 3815.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X04486 mRNA. Translation: CAA28172.1. Frameshift.
M19025 Genomic DNA. Translation: AAA33026.1. Frameshift.
AJ300448 Genomic DNA. Translation: CAC16733.1.
M28651 mRNA. Translation: AAA33025.1.

PIR

A28557.

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

Protein family/group databases

PeroxiBase

4070. CfuHalPrx.

Enzyme and pathway databases

BRENDA

1.11.1.10. 229210.

Family and domain databases

InterPro

IPR000028. Chloroperoxidase.
[Graphical view]

Gene3D

G3DSA:1.10.489.10. Chloroperoxidase. 1 hit.

Pfam

PF01328. Peroxidase_2. 1 hit.
[Graphical view]

ProDom

PD040763. Chloroperoxidase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS51405. HEME_HALOPEROXIDASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

PRXC_CALFU

Accession

Primary (citable) accession number: P04963
Secondary accession number(s): Q92216, Q9HFP2

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 13, 1987
Last sequence update:	March 27, 2002
Last modified:	June 16, 2009
This is version 83 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)