[1]	NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. PubMed=7744081 [NCBI, ExPASy, EBI, Israel, Japan] Simons B.H., Barnett P., Vollenbroek E.G.M., Dekker H.L., Muijsers A.O., Messerschmidt A., Wever R.; "Primary structure and characterization of the vanadium chloroperoxidase from the fungus Curvularia inaequalis."; Eur. J. Biochem. 229:566-574(1995).
[2]	X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). DOI=10.1073/pnas.93.1.392; PubMed=8552646 [NCBI, ExPASy, EBI, Israel, Japan] Messerschmidt A., Wever R.; "X-ray structure of a vanadium-containing enzyme: chloroperoxidase from the fungus Curvularia inaequalis."; Proc. Natl. Acad. Sci. U.S.A. 93:392-396(1996).

Comments

CATALYTIC ACTIVITY: 2 RH + 2 Cl^- + H₂O₂ = 2 RCl + 2 H₂O.
COFACTOR: Vanadium.
SUBCELLULAR LOCATION: Secreted.
PTM: The N-terminus is blocked.

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

X85369; CAA59686.1; -; mRNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

S69334; S69334.

3D structure databases

PDB

1IDQ; X-ray; 2.03 A; A=1-609.	[ExPASy / RCSB / EBI]
1IDU; X-ray; 2.24 A; A=1-609.	[ExPASy / RCSB / EBI]
1VNC; X-ray; 2.10 A; A=1-609.	[ExPASy / RCSB / EBI]
1VNE; X-ray; 2.15 A; A=1-609.	[ExPASy / RCSB / EBI]
1VNF; X-ray; 2.35 A; A=1-609.	[ExPASy / RCSB / EBI]
1VNG; X-ray; 2.20 A; A=1-609.	[ExPASy / RCSB / EBI]
1VNH; X-ray; 2.11 A; A=1-609.	[ExPASy / RCSB / EBI]
1VNI; X-ray; 2.15 A; A=1-609.	[ExPASy / RCSB / EBI]
1VNS; X-ray; 1.66 A; A=1-609.	[ExPASy / RCSB / EBI]
3BB0; X-ray; 1.50 A; A=1-609.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1IDQ; -.
1IDU; -.
1VNC; -.
1VNE; -.
1VNF; -.
1VNG; -.
1VNH; -.
1VNI; -.
1VNS; -.
3BB0; -.

ModBase

P49053.

Protein family/group databases

PeroxiBase

5892; CinaVCPo.

Family and domain databases

InterPro

IPR016119; Br/Cl_peroxidase_C.
IPR016118; P_Acid_Pase/Cl_peroxidase_N.
IPR000326; P_Acid_Pase_2/haloperoxidase.
Graphical view of domain structure.

Gene3D

G3DSA:1.10.606.10; Br/Cl_peroxidase_C; 1.
G3DSA:1.20.144.10; P_Acid_Pase/Cl_peroxidase_N; 1.

Pfam

PF01569; PAP2; 1.
Pfam graphical view of domain structure.

Other

P49053; -.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Chloride; Direct protein sequencing; Metal-binding; Oxidoreductase; Peroxidase; Secreted; Vanadium.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 609`	`609`	`Vanadium chloroperoxidase.`	`PRO_0000097055`
`ACT_SITE`	`404 404`
`METAL`	`496 496`		`Vanadium.`
`CONFLICT`	`454 454`		`P -> S (in Ref. 1; AA sequence).`
`HELIX`	`16 20`	`5`
`HELIX`	`22 40`	`19`
`HELIX`	`47 68`	`22`
`STRAND`	`72 74`	`3`
`STRAND`	`77 79`	`3`
`HELIX`	`85 87`	`3`
`HELIX`	`98 114`	`17`
`TURN`	`123 128`	`6`
`HELIX`	`131 147`	`17`
`HELIX`	`157 173`	`17`
`TURN`	`176 179`	`4`
`STRAND`	`202 207`	`6`
`STRAND`	`215 218`	`4`
`HELIX`	`226 229`	`4`
`HELIX`	`248 250`	`3`
`HELIX`	`254 268`	`15`
`HELIX`	`280 288`	`9`
`TURN`	`295 297`	`3`
`HELIX`	`300 314`	`15`
`STRAND`	`317 319`	`3`
`STRAND`	`321 323`	`3`
`HELIX`	`325 356`	`32`
`HELIX`	`361 366`	`6`
`TURN`	`371 373`	`3`
`HELIX`	`403 419`	`17`
`TURN`	`420 422`	`3`
`STRAND`	`436 439`	`4`
`HELIX`	`442 444`	`3`
`STRAND`	`445 447`	`3`
`STRAND`	`449 453`	`5`
`HELIX`	`461 463`	`3`
`STRAND`	`466 468`	`3`
`STRAND`	`474 477`	`4`
`HELIX`	`479 492`	`14`
`HELIX`	`498 501`	`4`
`HELIX`	`504 507`	`4`
`HELIX`	`530 532`	`3`
`STRAND`	`538 541`	`4`
`STRAND`	`544 549`	`6`
`HELIX`	`552 565`	`14`
`HELIX`	`573 575`	`3`

Sequence information

Length: 609 AA [This is the length of the unprocessed precursor]

Molecular weight: 67531 Da [This is the MW of the unprocessed precursor]

CRC64: A7B710DDF937D3E9 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MGSVTPIPLP KIDEPEEYNT NYILFWNHVG LELNRVTHTV GGPLTGPPLS ARALGMLHLA 

        70         80         90        100        110        120 
IHDAYFSICP PTDFTTFLSP DTENAAYRLP SPNGANDARQ AVAGAALKML SSLYMKPVEQ 

       130        140        150        160        170        180 
PNPNPGANIS DNAYAQLGLV LDRSVLEAPG GVDRESASFM FGEDVADVFF ALLNDPRGAS 

       190        200        210        220        230        240 
QEGYHPTPGR YKFDDEPTHP VVLIPVDPNN PNGPKMPFRQ YHAPFYGKTT KRFATQSEHF 

       250        260        270        280        290        300 
LADPPGLRSN ADETAEYDDA VRVAIAMGGA QALNSTKRSP WQTAQGLYWA YDGSNLIGTP 

       310        320        330        340        350        360 
PRFYNQIVRR IAVTYKKEED LANSEVNNAD FARLFALVDV ACTDAGIFSW KEKWEFEFWR 

       370        380        390        400        410        420 
PLSGVRDDGR PDHGDPFWLT LGAPATNTND IPFKPPFPAY PSGHATFGGA VFQMVRRYYN 

       430        440        450        460        470        480 
GRVGTWKDDE PDNIAIDMMI SEELNGVNRD LRQPYDPTAP IEDQPGIVRT RIVRHFDSAW 

       490        500        510        520        530        540 
ELMFENAISR IFLGVHWRFD AAAARDILIP TTTKDVYAVD NNGATVFQNV EDIRYTTRGT 

       550        560        570        580        590        600 
REDPEGLFPI GGVPLGIEIA DEIFNNGLKP TPPEIQPMPQ ETPVQKPVGQ QPVKGMWEEE 


QAPVVKEAP

P49053 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