[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 Hager L.P.; Unpublished observations (FEB-1996).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: RH + Cl^- + H₂O₂ = 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.

Ontologies

GO:0031404;	Molecular function: chloride ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0016691;	Molecular function: chloride peroxidase activity (inferred from electronic annotation from EC).
GO:0005506;	Molecular function: iron ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0030145;	Molecular function: manganese ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

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]

PROSITE

PS51405; HEME_HALOPEROXIDASE; 1.
PROSITE graphical view of domain structure (profiles).

Other

P04963; -.

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

Feature table viewer

Feature aligner

`Key`	`From 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

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools