ID   PRXC_CURIN              Reviewed;         609 AA.
AC   P49053;
DT   01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 1.
DT   27-MAR-2024, entry version 111.
DE   RecName: Full=Vanadium chloroperoxidase {ECO:0000303|PubMed:7744081};
DE            EC=1.11.1.10 {ECO:0000269|PubMed:7744081};
DE   AltName: Full=Vanadium chloride peroxidase;
DE            Short=VCPO;
GN   Name=CPO;
OS   Curvularia inaequalis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Curvularia.
OX   NCBI_TaxID=38902;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, CATALYTIC
RP   ACTIVITY, COFACTOR, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND SUBUNIT.
RX   PubMed=7744081; DOI=10.1111/j.1432-1033.1995.tb20499.x;
RA   Simons B.H., Barnett P., Vollenbroek E.G.M., Dekker H.L., Muijsers A.O.,
RA   Messerschmidt A., Wever R.;
RT   "Primary structure and characterization of the vanadium chloroperoxidase
RT   from the fungus Curvularia inaequalis.";
RL   Eur. J. Biochem. 229:566-574(1995).
RN   [2] {ECO:0007744|PDB:1VNC}
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEX WITH VANADATE, COFACTOR,
RP   REACTION MECHANISM, AND ACTIVE SITE.
RX   PubMed=8552646; DOI=10.1073/pnas.93.1.392;
RA   Messerschmidt A., Wever R.;
RT   "X-ray structure of a vanadium-containing enzyme: chloroperoxidase from the
RT   fungus Curvularia inaequalis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 93:392-396(1996).
RN   [3] {ECO:0007744|PDB:1IDQ, ECO:0007744|PDB:1IDU}
RP   X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) IN COMPLEX WITH VANADATE, COFACTOR,
RP   AND REACTION MECHANISM.
RX   PubMed=9165086; DOI=10.1515/bchm.1997.378.3-4.309;
RA   Messerschmidt A., Prade L., Wever R.;
RT   "Implications for the catalytic mechanism of the vanadium-containing enzyme
RT   chloroperoxidase from the fungus Curvularia inaequalis by X-ray structures
RT   of the native and peroxide form.";
RL   Biol. Chem. 378:309-315(1997).
CC   -!- FUNCTION: Catalyzes the oxidation of chloride in the presence of
CC       hydrogen peroxide to hypochlorous acid (ClOH), which in turn can react
CC       with a nucleophilic acceptor (RH), to form a chlorinated compound.
CC       {ECO:0000269|PubMed:7744081}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=RH + Cl(-) + H2O2 = RCl + 2 H2O.; EC=1.11.1.10;
CC         Evidence={ECO:0000269|PubMed:7744081};
CC   -!- COFACTOR:
CC       Name=vanadate; Xref=ChEBI:CHEBI:35169;
CC         Evidence={ECO:0000269|PubMed:8552646, ECO:0000269|PubMed:9165086,
CC         ECO:0000305|PubMed:7744081};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:7744081}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7744081}.
CC   -!- DEVELOPMENTAL STAGE: Expression takes place in the secondary-growth
CC       phase initiated by nutrient depletion. {ECO:0000269|PubMed:7744081}.
CC   -!- PTM: The N-terminus is blocked. {ECO:0000269|PubMed:7744081}.
CC   -!- SIMILARITY: Belongs to the vanadium-dependent haloperoxidase family.
CC       {ECO:0000305}.
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DR   EMBL; X85369; CAA59686.1; -; mRNA.
DR   PIR; S69334; S69334.
DR   PDB; 1IDQ; X-ray; 2.03 A; A=1-609.
DR   PDB; 1IDU; X-ray; 2.24 A; A=1-609.
DR   PDB; 1VNC; X-ray; 2.10 A; A=1-609.
DR   PDB; 1VNE; X-ray; 2.15 A; A=1-609.
DR   PDB; 1VNF; X-ray; 2.35 A; A=1-609.
DR   PDB; 1VNG; X-ray; 2.20 A; A=1-609.
DR   PDB; 1VNH; X-ray; 2.11 A; A=1-609.
DR   PDB; 1VNI; X-ray; 2.15 A; A=1-609.
DR   PDB; 1VNS; X-ray; 1.66 A; A=1-609.
DR   PDB; 3BB0; X-ray; 1.50 A; A=1-609.
DR   PDBsum; 1IDQ; -.
DR   PDBsum; 1IDU; -.
DR   PDBsum; 1VNC; -.
DR   PDBsum; 1VNE; -.
DR   PDBsum; 1VNF; -.
DR   PDBsum; 1VNG; -.
DR   PDBsum; 1VNH; -.
DR   PDBsum; 1VNI; -.
DR   PDBsum; 1VNS; -.
DR   PDBsum; 3BB0; -.
DR   AlphaFoldDB; P49053; -.
DR   SMR; P49053; -.
DR   PeroxiBase; 5892; CinaVCPo.
DR   KEGG; ag:CAA59686; -.
DR   BioCyc; MetaCyc:MONOMER-15997; -.
DR   BRENDA; 1.11.1.B2; 1761.
DR   SABIO-RK; P49053; -.
DR   EvolutionaryTrace; P49053; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016691; F:chloride peroxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd03398; PAP2_haloperoxidase; 1.
DR   Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR   Gene3D; 1.10.606.10; Vanadium-containing Chloroperoxidase, domain 2; 1.
DR   InterPro; IPR016119; Br/Cl_peroxidase_C.
DR   InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR   InterPro; IPR041067; VCPO_N.
DR   PANTHER; PTHR34599; PEROXIDASE-RELATED; 1.
DR   PANTHER; PTHR34599:SF1; TRAF-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF17897; VCPO_N; 1.
DR   SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Chloride; Direct protein sequencing; Metal-binding;
KW   Oxidoreductase; Peroxidase; Secreted; Vanadium.
FT   CHAIN           1..609
FT                   /note="Vanadium chloroperoxidase"
FT                   /id="PRO_0000097055"
FT   REGION          569..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        404
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000305|PubMed:8552646"
FT   BINDING         353
FT                   /ligand="vanadate"
FT                   /ligand_id="ChEBI:CHEBI:35169"
FT                   /evidence="ECO:0000269|PubMed:8552646,
FT                   ECO:0000269|PubMed:9165086, ECO:0007744|PDB:1IDQ,
FT                   ECO:0007744|PDB:1VNC"
FT   BINDING         360
FT                   /ligand="vanadate"
FT                   /ligand_id="ChEBI:CHEBI:35169"
FT                   /evidence="ECO:0000269|PubMed:8552646,
FT                   ECO:0000269|PubMed:9165086, ECO:0007744|PDB:1IDQ,
FT                   ECO:0007744|PDB:1VNC"
FT   BINDING         402
FT                   /ligand="vanadate"
FT                   /ligand_id="ChEBI:CHEBI:35169"
FT                   /evidence="ECO:0000269|PubMed:8552646,
FT                   ECO:0000269|PubMed:9165086, ECO:0007744|PDB:1IDQ,
FT                   ECO:0007744|PDB:1VNC"
FT   BINDING         403
FT                   /ligand="vanadate"
FT                   /ligand_id="ChEBI:CHEBI:35169"
FT                   /evidence="ECO:0000269|PubMed:8552646,
FT                   ECO:0000269|PubMed:9165086, ECO:0007744|PDB:1IDQ,
FT                   ECO:0007744|PDB:1VNC"
FT   BINDING         404
FT                   /ligand="vanadate"
FT                   /ligand_id="ChEBI:CHEBI:35169"
FT                   /evidence="ECO:0000269|PubMed:8552646,
FT                   ECO:0000269|PubMed:9165086, ECO:0007744|PDB:1IDQ,
FT                   ECO:0007744|PDB:1VNC"
FT   BINDING         490
FT                   /ligand="vanadate"
FT                   /ligand_id="ChEBI:CHEBI:35169"
FT                   /evidence="ECO:0000269|PubMed:8552646,
FT                   ECO:0000269|PubMed:9165086, ECO:0007744|PDB:1IDQ,
FT                   ECO:0007744|PDB:1VNC"
FT   BINDING         496
FT                   /ligand="vanadate"
FT                   /ligand_id="ChEBI:CHEBI:35169"
FT                   /evidence="ECO:0000269|PubMed:8552646,
FT                   ECO:0000269|PubMed:9165086, ECO:0007744|PDB:1IDQ,
FT                   ECO:0007744|PDB:1VNC"
FT   CONFLICT        454
FT                   /note="P -> S (in Ref. 1; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   HELIX           16..20
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   HELIX           22..40
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   HELIX           47..68
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   STRAND          72..74
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   STRAND          77..79
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   HELIX           85..87
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   HELIX           98..114
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   TURN            118..125
FT                   /evidence="ECO:0007829|PDB:1VNS"
FT   HELIX           131..147
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   HELIX           157..173
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   TURN            176..179
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   STRAND          202..207
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   STRAND          215..218
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   HELIX           226..229
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   HELIX           248..250
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   HELIX           254..268
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   HELIX           280..288
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   TURN            295..297
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   HELIX           300..314
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   STRAND          317..319
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   STRAND          321..323
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   HELIX           325..356
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   HELIX           361..366
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   TURN            371..373
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   STRAND          388..390
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   HELIX           403..419
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   TURN            420..422
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   STRAND          436..440
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   STRAND          444..447
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   STRAND          449..453
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   HELIX           461..463
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   STRAND          466..468
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   STRAND          473..477
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   HELIX           479..492
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   HELIX           498..501
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   HELIX           504..507
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   HELIX           530..532
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   STRAND          538..541
FT                   /evidence="ECO:0007829|PDB:1IDQ"
FT   STRAND          542..544
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   HELIX           552..565
FT                   /evidence="ECO:0007829|PDB:3BB0"
FT   HELIX           573..575
FT                   /evidence="ECO:0007829|PDB:3BB0"
SQ   SEQUENCE   609 AA;  67531 MW;  A7B710DDF937D3E9 CRC64;
     MGSVTPIPLP KIDEPEEYNT NYILFWNHVG LELNRVTHTV GGPLTGPPLS ARALGMLHLA
     IHDAYFSICP PTDFTTFLSP DTENAAYRLP SPNGANDARQ AVAGAALKML SSLYMKPVEQ
     PNPNPGANIS DNAYAQLGLV LDRSVLEAPG GVDRESASFM FGEDVADVFF ALLNDPRGAS
     QEGYHPTPGR YKFDDEPTHP VVLIPVDPNN PNGPKMPFRQ YHAPFYGKTT KRFATQSEHF
     LADPPGLRSN ADETAEYDDA VRVAIAMGGA QALNSTKRSP WQTAQGLYWA YDGSNLIGTP
     PRFYNQIVRR IAVTYKKEED LANSEVNNAD FARLFALVDV ACTDAGIFSW KEKWEFEFWR
     PLSGVRDDGR PDHGDPFWLT LGAPATNTND IPFKPPFPAY PSGHATFGGA VFQMVRRYYN
     GRVGTWKDDE PDNIAIDMMI SEELNGVNRD LRQPYDPTAP IEDQPGIVRT RIVRHFDSAW
     ELMFENAISR IFLGVHWRFD AAAARDILIP TTTKDVYAVD NNGATVFQNV EDIRYTTRGT
     REDPEGLFPI GGVPLGIEIA DEIFNNGLKP TPPEIQPMPQ ETPVQKPVGQ QPVKGMWEEE
     QAPVVKEAP
//