PRXV_CORPI
ID PRXV_CORPI Reviewed; 598 AA.
AC O81959;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Vanadium-dependent bromoperoxidase;
DE Short=V-BPO;
DE EC=1.11.1.18;
DE AltName: Full=Vanadium haloperoxidase;
OS Corallina pilulifera (Red coralline alga).
OC Eukaryota; Rhodophyta; Florideophyceae; Corallinophycidae; Corallinales;
OC Corallinaceae; Corallinoideae; Corallina.
OX NCBI_TaxID=78447;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9645486; DOI=10.1016/s0014-5793(98)00500-6;
RA Shimonishi M., Kuwamoto S., Inoue H., Wever R., Ohshiro T., Izumi Y.,
RA Tanabe T.;
RT "Cloning and expression of the gene for a vanadium-dependent
RT bromoperoxidase from a marine macro-alga, Corallina pilulifera.";
RL FEBS Lett. 428:105-110(1998).
RN [2] {ECO:0007744|PDB:1UP8}
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH CALCIUM AND
RP PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND ENZYME STABILITY.
RX PubMed=15776268; DOI=10.1007/s00775-005-0639-3;
RA Garcia-Rodriguez E., Ohshiro T., Aibara T., Izumi Y., Littlechild J.;
RT "Enhancing effect of calcium and vanadium ions on thermal stability of
RT bromoperoxidase from Corallina pilulifera.";
RL J. Biol. Inorg. Chem. 10:275-282(2005).
CC -!- FUNCTION: Catalyzes the halogenation of organic substrates in the
CC presence of hydrogen peroxide. {ECO:0000269|PubMed:15776268}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RH + Br(-) + H2O2 = RBr + 2 H2O.; EC=1.11.1.18;
CC Evidence={ECO:0000269|PubMed:15776268};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:15776268};
CC Note=Binds 1 Ca(2+) ion per subunit. The binding is important for
CC enzyme stability. {ECO:0000269|PubMed:15776268};
CC -!- COFACTOR:
CC Name=vanadate; Xref=ChEBI:CHEBI:35169;
CC Evidence={ECO:0000269|PubMed:15776268};
CC Note=Binds 1 vanadate ion per subunit. {ECO:0000269|PubMed:15776268};
CC -!- SUBUNIT: Homododecamer. {ECO:0000269|PubMed:15776268}.
CC -!- SIMILARITY: Belongs to the vanadium-dependent haloperoxidase family.
CC {ECO:0000305}.
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DR EMBL; D87657; BAA31261.1; -; mRNA.
DR PDB; 1UP8; X-ray; 2.20 A; A/B/C/D=1-598.
DR PDBsum; 1UP8; -.
DR AlphaFoldDB; O81959; -.
DR SMR; O81959; -.
DR PeroxiBase; 5894; CpiVBPo01.
DR EvolutionaryTrace; O81959; -.
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; Metal-binding; Oxidoreductase; Peroxidase; Vanadium.
FT CHAIN 1..598
FT /note="Vanadium-dependent bromoperoxidase"
FT /id="PRO_0000401200"
FT ACT_SITE 480
FT /evidence="ECO:0000250"
FT ACT_SITE 487
FT /evidence="ECO:0000250"
FT BINDING 361
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1UP8"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1UP8"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1UP8"
FT BINDING 368
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1UP8"
FT BINDING 370
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1UP8"
FT BINDING 400
FT /ligand="vanadate"
FT /ligand_id="ChEBI:CHEBI:35169"
FT /evidence="ECO:0000250|UniProtKB:P81701"
FT BINDING 408
FT /ligand="vanadate"
FT /ligand_id="ChEBI:CHEBI:35169"
FT /evidence="ECO:0000250|UniProtKB:P81701"
FT BINDING 485
FT /ligand="vanadate"
FT /ligand_id="ChEBI:CHEBI:35169"
FT /evidence="ECO:0000250|UniProtKB:P81701"
FT BINDING 486
FT /ligand="vanadate"
FT /ligand_id="ChEBI:CHEBI:35169"
FT /evidence="ECO:0000250|UniProtKB:P81701"
FT BINDING 487
FT /ligand="vanadate"
FT /ligand_id="ChEBI:CHEBI:35169"
FT /evidence="ECO:0000250|UniProtKB:P81701"
FT BINDING 547
FT /ligand="vanadate"
FT /ligand_id="ChEBI:CHEBI:35169"
FT /evidence="ECO:0000250|UniProtKB:P81701"
FT BINDING 553
FT /ligand="vanadate"
FT /ligand_id="ChEBI:CHEBI:35169"
FT /evidence="ECO:0000250|UniProtKB:P81701"
FT HELIX 11..28
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 74..86
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:1UP8"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 113..118
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1UP8"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 155..169
FT /evidence="ECO:0007829|PDB:1UP8"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 184..195
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:1UP8"
FT TURN 222..226
FT /evidence="ECO:0007829|PDB:1UP8"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:1UP8"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1UP8"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 265..270
FT /evidence="ECO:0007829|PDB:1UP8"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:1UP8"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:1UP8"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:1UP8"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 325..334
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 339..350
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:1UP8"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 378..401
FT /evidence="ECO:0007829|PDB:1UP8"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 409..424
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 434..439
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 441..457
FT /evidence="ECO:0007829|PDB:1UP8"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:1UP8"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 486..501
FT /evidence="ECO:0007829|PDB:1UP8"
FT TURN 503..505
FT /evidence="ECO:0007829|PDB:1UP8"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:1UP8"
FT STRAND 516..523
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 532..550
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 555..576
FT /evidence="ECO:0007829|PDB:1UP8"
FT HELIX 577..579
FT /evidence="ECO:0007829|PDB:1UP8"
FT STRAND 587..589
FT /evidence="ECO:0007829|PDB:1UP8"
FT STRAND 595..597
FT /evidence="ECO:0007829|PDB:1UP8"
SQ SEQUENCE 598 AA; 65313 MW; 88B81B678B7FACE0 CRC64;
MGIPADNLQS RAKASFDTRV AAAELALNRG VVPSFANGEE LLYRNPDPDN TDPSFIASFT
KGLPHDDNGA IIDPDDFLAF VRAINSGDEK EIADLTLGPA RDPETGLPIW RSDLANSLEL
EVRGWENSSA GLTFDLEGPD AQSIAMPPAP VLTSPELVAE IAELYLMALG REIEFSEFDS
PKNAEYIQFA IDQLNGLEWF NTPAKLGDPP AEIRRRRGEV TVGNLFRGIL PGSEVGPYLS
QYIIVGSKQI GSATVGNKTL VSPNAADEFD GEIAYGSITI SQRVRIATPG RDFMTDLKVF
LDVQDAADFR GFESYEPGAR LIRTIRDLAT WVHFDALYEA YLNACLILLA NGVPFDPNLP
FQQEDKLDNQ DVFVNFGSAH VLSLVTEVAT RALKAVRYQK FNIHRRLRPE ATGGLISVNK
IAPQKGESIF PEVDLAVEEL GDILEKAEIS NRKQNIADGD PDPDPSFLLP MAFAEGSPFH
PSYGSGHAVV AGACVTILKA FFDSGIEIDQ VFEVDKDEDK LVKSSFKGTL TVAGELNKLA
DNIAIGRNMA GVHYFSDQFE SLLLGEQVAI GILEEQSLTY GENFFFNLPK FDGTTIQI
