Reviewed, UniProtKB/Swiss-Prot P49053 (PRXC_CURIN)

Names and origin

Protein names

Recommended name:
    Vanadium chloroperoxidase
    EC=1.11.1.10
Alternative name(s):
    Vanadium chloride peroxidase
      Short name=VCPO

Gene names

Name:

CPO

Organism

Curvularia inaequalis

Taxonomic identifier

38902 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Dothideomycetes › Pleosporomycetidae › Pleosporales › Pleosporaceae › mitosporic Cochliobolus › Curvularia

Protein attributes

Sequence length	609 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Catalytic activity	RH + Cl(-) + H(2)O(2) = RCl + 2 H(2)O.
Cofactor	Vanadium.
Subcellular location	Secreted.
Post-translational modification	The N-terminus is blocked.

Ontologies

Keywords
Cellular component	Secreted
Ligand	Chloride Metal-binding Vanadium
Molecular function	Oxidoreductase Peroxidase
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	extracellular region Inferred from electronic annotation. Source: UniProtKB-KW membrane Inferred from electronic annotation. Source: InterPro
Molecular function	chloride ion binding Inferred from electronic annotation. Source: UniProtKB-KW chloride peroxidase activity Inferred from electronic annotation. Source: EC vanadium 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

Chain

1 – 609

609

Vanadium chloroperoxidase

PRO_0000097055

Sites

Active site

404

1

Metal binding

496

1

Vanadium

Experimental info

Sequence conflict

454

1

P → S AA sequence Ref.1

Secondary structure

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609

Helix Strand Turn

Details...

Helix

16 – 20

5

Helix

22 – 40

19

Helix

47 – 68

22

Beta strand

72 – 74

3

Beta 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

Beta strand

202 – 207

6

Beta 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

Beta strand

317 – 319

3

Beta strand

321 – 323

3

Helix

325 – 356

32

Helix

361 – 366

6

Turn

371 – 373

3

Helix

403 – 419

17

Turn

420 – 422

3

Beta strand

436 – 439

4

Helix

442 – 444

3

Beta strand

445 – 447

3

Beta strand

449 – 453

5

Helix

461 – 463

3

Beta strand

466 – 468

3

Beta strand

474 – 477

4

Helix

479 – 492

14

Helix

498 – 501

4

Helix

504 – 507

4

Helix

530 – 532

3

Beta strand

538 – 541

4

Beta strand

544 – 549

6

Helix

552 – 565

14

Helix

573 – 575

3

Sequences

	Sequence		Length	Mass (Da)
	P49053-1 [UniParc]. Last modified February 1, 1996. Version 1. Checksum: A7B710DDF937D3E9	FASTA	609	67,531
	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

References

[1]	"Primary structure and characterization of the vanadium chloroperoxidase from the fungus Curvularia inaequalis." Simons B.H., Barnett P., Vollenbroek E.G.M., Dekker H.L., Muijsers A.O., Messerschmidt A., Wever R. Eur. J. Biochem. 229:566-574(1995) [PubMed: 7744081] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[2]	"X-ray structure of a vanadium-containing enzyme: chloroperoxidase from the fungus Curvularia inaequalis." Messerschmidt A., Wever R. Proc. Natl. Acad. Sci. U.S.A. 93:392-396(1996) [PubMed: 8552646] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X85369 mRNA. Translation: CAA59686.1.

PIR

S69334.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1IDQ	X-ray	2.03	A	1-609	[»]
1IDU	X-ray	2.24	A	1-609	[»]
1VNC	X-ray	2.10	A	1-609	[»]
1VNE	X-ray	2.15	A	1-609	[»]
1VNF	X-ray	2.35	A	1-609	[»]
1VNG	X-ray	2.20	A	1-609	[»]
1VNH	X-ray	2.11	A	1-609	[»]
1VNI	X-ray	2.15	A	1-609	[»]
1VNS	X-ray	1.66	A	1-609	[»]
3BB0	X-ray	1.50	A	1-609	[»]

ModBase

Search...

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]

Gene3D

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

Pfam

PF01569. PAP2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

LinkHub

P49053.

Entry information

Entry name

PRXC_CURIN

Accession

Primary (citable) accession number: P49053

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1996
Last sequence update:	February 1, 1996
Last modified:	November 25, 2008
This is version 63 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)