PRXC_CURIN
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 03-AUG-2022, entry version 106.
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:MON-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 Gene3D; 1.10.606.10; -; 1.
DR InterPro; IPR016119; Br/Cl_peroxidase_C.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR041067; VCPO_N.
DR Pfam; PF01569; PAP2; 1.
DR Pfam; PF17897; VCPO_N; 1.
DR SUPFAM; SSF48317; SSF48317; 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
