PRXV_ASCNO
ID PRXV_ASCNO Reviewed; 557 AA.
AC P81701;
DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2000, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Vanadium-dependent bromoperoxidase;
DE Short=V-BPO;
DE EC=1.11.1.18;
DE AltName: Full=Vanadium haloperoxidase;
OS Ascophyllum nodosum (Knotted wrack) (Brown seaweed).
OC Eukaryota; Sar; Stramenopiles; Ochrophyta; PX clade; Phaeophyceae; Fucales;
OC Fucaceae; Ascophyllum.
OX NCBI_TaxID=52969;
RN [1] {ECO:0007744|PDB:1QI9}
RP PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH
RP VANADATE, PYROGLUTAMATE FORMATION AT GLN-1, COFACTOR, FUNCTION, SUBUNIT,
RP AND REACTION MECHANISM.
RX PubMed=10543953; DOI=10.1006/jmbi.1999.3179;
RA Weyand M., Hecht H.-J., Kiess M., Liaud M.-F., Vilter H., Schomburg D.;
RT "X-ray structure determination of a vanadium-dependent haloperoxidase from
RT Ascophyllum nodosum at 2.0-A resolution.";
RL J. Mol. Biol. 293:595-611(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE OF 320-556, PROTEIN SEQUENCE OF 326-341; 383-426;
RP 471-479 AND 481-556, AND FUNCTION.
RX PubMed=8564812;
RA Vilter H.;
RT "Vanadium-dependent haloperoxidases.";
RL Met. Ions Biol. Syst. 31:325-362(1995).
CC -!- FUNCTION: Catalyzes the halogenation of organic substrates in the
CC presence of hydrogen peroxide. {ECO:0000269|PubMed:10543953,
CC ECO:0000269|PubMed:8564812}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RH + Br(-) + H2O2 = RBr + 2 H2O.; EC=1.11.1.18;
CC Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=vanadate; Xref=ChEBI:CHEBI:35169;
CC Evidence={ECO:0000269|PubMed:10543953};
CC Note=Binds 1 vanadate ion per subunit. {ECO:0000269|PubMed:10543953};
CC -!- SUBUNIT: Homodimer; disulfide-linked. {ECO:0000269|PubMed:10543953}.
CC -!- SIMILARITY: Belongs to the vanadium-dependent haloperoxidase family.
CC {ECO:0000305}.
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DR PDB; 1QI9; X-ray; 2.05 A; A/B=2-556.
DR PDBsum; 1QI9; -.
DR AlphaFoldDB; P81701; -.
DR SMR; P81701; -.
DR PeroxiBase; 5895; AnoVBPo.
DR BRENDA; 1.11.1.18; 8891.
DR EvolutionaryTrace; P81701; -.
DR GO; GO:0019806; F:bromide 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 SUPFAM; SSF48317; SSF48317; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond; Metal-binding;
KW Oxidoreductase; Peroxidase; Pyrrolidone carboxylic acid; Vanadium.
FT CHAIN 1..557
FT /note="Vanadium-dependent bromoperoxidase"
FT /id="PRO_0000207068"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 411
FT ACT_SITE 418
FT BINDING 341
FT /ligand="vanadate"
FT /ligand_id="ChEBI:CHEBI:35169"
FT /evidence="ECO:0000269|PubMed:10543953,
FT ECO:0007744|PDB:1QI9"
FT BINDING 349
FT /ligand="vanadate"
FT /ligand_id="ChEBI:CHEBI:35169"
FT /evidence="ECO:0000269|PubMed:10543953,
FT ECO:0007744|PDB:1QI9"
FT BINDING 416
FT /ligand="vanadate"
FT /ligand_id="ChEBI:CHEBI:35169"
FT /evidence="ECO:0000269|PubMed:10543953,
FT ECO:0007744|PDB:1QI9"
FT BINDING 417
FT /ligand="vanadate"
FT /ligand_id="ChEBI:CHEBI:35169"
FT /evidence="ECO:0000269|PubMed:10543953,
FT ECO:0007744|PDB:1QI9"
FT BINDING 418
FT /ligand="vanadate"
FT /ligand_id="ChEBI:CHEBI:35169"
FT /evidence="ECO:0000269|PubMed:10543953,
FT ECO:0007744|PDB:1QI9"
FT BINDING 480
FT /ligand="vanadate"
FT /ligand_id="ChEBI:CHEBI:35169"
FT /evidence="ECO:0000269|PubMed:10543953,
FT ECO:0007744|PDB:1QI9"
FT BINDING 486
FT /ligand="vanadate"
FT /ligand_id="ChEBI:CHEBI:35169"
FT /evidence="ECO:0000269|PubMed:10543953,
FT ECO:0007744|PDB:1QI9"
FT MOD_RES 1
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:10543953"
FT DISULFID 3
FT /note="Interchain (with C-41)"
FT DISULFID 41
FT /note="Interchain (with C-3)"
FT DISULFID 77..86
FT DISULFID 441..462
FT DISULFID 544..555
FT CONFLICT 321
FT /note="S -> D (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 341
FT /note="K -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 403..404
FT /note="AI -> VY (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 407..408
FT /note="GS -> T (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 409
FT /note="P -> S (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 441..444
FT /note="CYPD -> AIR (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="N -> K (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT HELIX 15..37
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 50..52
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 68..80
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 83..86
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 98..100
FT /evidence="ECO:0007829|PDB:1QI9"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1QI9"
FT TURN 105..108
FT /evidence="ECO:0007829|PDB:1QI9"
FT STRAND 113..116
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 132..147
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:1QI9"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:1QI9"
FT TURN 200..202
FT /evidence="ECO:0007829|PDB:1QI9"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:1QI9"
FT STRAND 216..218
FT /evidence="ECO:0007829|PDB:1QI9"
FT STRAND 221..223
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 240..247
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 268..276
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 282..293
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 304..308
FT /evidence="ECO:0007829|PDB:1QI9"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 320..329
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 330..333
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 334..342
FT /evidence="ECO:0007829|PDB:1QI9"
FT TURN 343..345
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 350..361
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 371..374
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 377..390
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:1QI9"
FT STRAND 402..404
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 417..433
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 435..438
FT /evidence="ECO:0007829|PDB:1QI9"
FT STRAND 446..448
FT /evidence="ECO:0007829|PDB:1QI9"
FT STRAND 452..457
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 465..482
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 488..512
FT /evidence="ECO:0007829|PDB:1QI9"
FT STRAND 518..522
FT /evidence="ECO:0007829|PDB:1QI9"
FT STRAND 528..532
FT /evidence="ECO:0007829|PDB:1QI9"
FT STRAND 537..539
FT /evidence="ECO:0007829|PDB:1QI9"
FT STRAND 545..548
FT /evidence="ECO:0007829|PDB:1QI9"
FT HELIX 552..554
FT /evidence="ECO:0007829|PDB:1QI9"
SQ SEQUENCE 557 AA; 60344 MW; E3D8557AB92B16F4 CRC64;
QTCSTSDDAD DPTPPNERDD EAFASRVAAA KRELEGTGTV CQINNGETDL AAKFHKSLPH
DDLGQVDADA FAALEDCILN GDLSICEDVP VGNSEGDPVG RLVNPTAAFA IDISGPAFSA
TTIPPVPTLP SPELAAQLAE VYWMALARDV PFMQYGTDDI TVTAAANLAG MEGFPNLDAV
SIGSDGTVDP LSQLFRATFV GVETGPFISQ LLVNSFTIDS ITVEPKQETF APDVNYMVDF
DEWLNIQNGG PPAGPELLDD ELRFVRNARD LARVTFTDNI NTEAYRGALI LLGLDAFNRA
GVNGPFIDID RQAGFVNFGI SHYFRLIGAA ELAQRSSWYQ KWQVHRFARP EALGGTLHLT
IKGELNADFD LSLLENAELL KRVAAINAAQ NPNNEVTYLL PQAIQEGSPT HPSYPSGHAT
QNGAFATVLK ALIGLDRGGD CYPDPVYPDD DGLKLIDFRG SCLTFEGEIN KLAVNVAFGR
QMLGIHYRFD GIQGLLLGET ITVRTLHQEL MTFAEESTFE FRLFTGEVIK LFQDGTFTID
GFKCPGLVYT GVENCVS
