PRXV_COROI
ID PRXV_COROI Reviewed; 598 AA.
AC Q8LLW7;
DT 30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Vanadium-dependent bromoperoxidase;
DE EC=1.11.1.18;
DE AltName: Full=Vanadium haloperoxidase;
OS Corallina officinalis (Coral seaweed).
OC Eukaryota; Rhodophyta; Florideophyceae; Corallinophycidae; Corallinales;
OC Corallinaceae; Corallinoideae; Corallina.
OX NCBI_TaxID=35170;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF HIS-480.
RX PubMed=12121762; DOI=10.1016/s0162-0134(02)00400-2;
RA Carter J.N., Beatty K.E., Simpson M.T., Butler A.;
RT "Reactivity of recombinant and mutant vanadium bromoperoxidase from the red
RT alga Corallina officinalis.";
RL J. Inorg. Biochem. 91:59-69(2002).
RN [2] {ECO:0007744|PDB:1QHB}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CALCIUM AND
RP PHOSPHATE, AND COFACTOR.
RX PubMed=10843856; DOI=10.1006/jmbi.2000.3806;
RA Isupov M.N., Dalby A.R., Brindley A.A., Izumi Y., Tanabe T.,
RA Murshudov G.N., Littlechild J.A.;
RT "Crystal structure of dodecameric vanadium-dependent bromoperoxidase from
RT the red algae Corallina officinalis.";
RL J. Mol. Biol. 299:1035-1049(2000).
CC -!- FUNCTION: Catalyzes the halogenation of organic substrates in the
CC presence of hydrogen peroxide. {ECO:0000269|PubMed:12121762}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=RH + Br(-) + H2O2 = RBr + 2 H2O.; EC=1.11.1.18;
CC Evidence={ECO:0000269|PubMed:12121762};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:10843856};
CC Note=Binds 1 Ca(2+) ion per subunit. The binding is important for
CC enzyme stability. {ECO:0000269|PubMed:10843856};
CC -!- COFACTOR:
CC Name=vanadate; Xref=ChEBI:CHEBI:35169;
CC Evidence={ECO:0000269|PubMed:10843856};
CC Note=Binds 1 vanadate ion per subunit. {ECO:0000269|PubMed:10843856};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 mM for bromide {ECO:0000269|PubMed:12121762};
CC KM=1.8 mM for iodide {ECO:0000269|PubMed:12121762};
CC KM=17 uM for H(2)O(2) {ECO:0000269|PubMed:12121762};
CC pH dependence:
CC Optimum pH is 6.0. {ECO:0000269|PubMed:12121762};
CC -!- SUBUNIT: Homododecamer. {ECO:0000269|PubMed:10843856,
CC ECO:0000269|PubMed:12121762}.
CC -!- SIMILARITY: Belongs to the vanadium-dependent haloperoxidase family.
CC {ECO:0000305}.
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DR EMBL; AF218810; AAM46061.1; -; mRNA.
DR PDB; 1QHB; X-ray; 2.30 A; A/B/C/D/E/F=1-598.
DR PDBsum; 1QHB; -.
DR AlphaFoldDB; Q8LLW7; -.
DR SMR; Q8LLW7; -.
DR PeroxiBase; 5901; CoVBPo.
DR KEGG; ag:AAM46061; -.
DR BRENDA; 1.11.1.18; 1611.
DR EvolutionaryTrace; Q8LLW7; -.
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 InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR Pfam; PF01569; PAP2; 1.
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_0000401199"
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:1QHB"
FT BINDING 363
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1QHB"
FT BINDING 365
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1QHB"
FT BINDING 368
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1QHB"
FT BINDING 370
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1QHB"
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 MUTAGEN 480
FT /note="H->A: Shows 4% of wild-type activity."
FT /evidence="ECO:0000269|PubMed:12121762"
FT HELIX 11..28
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 39..41
FT /evidence="ECO:0007829|PDB:1QHB"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 74..86
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 89..93
FT /evidence="ECO:0007829|PDB:1QHB"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 113..117
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:1QHB"
FT STRAND 136..139
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 155..169
FT /evidence="ECO:0007829|PDB:1QHB"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 175..177
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 181..183
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 184..194
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 198..201
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:1QHB"
FT TURN 222..226
FT /evidence="ECO:0007829|PDB:1QHB"
FT TURN 231..234
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 241..243
FT /evidence="ECO:0007829|PDB:1QHB"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:1QHB"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 265..270
FT /evidence="ECO:0007829|PDB:1QHB"
FT STRAND 272..275
FT /evidence="ECO:0007829|PDB:1QHB"
FT STRAND 278..281
FT /evidence="ECO:0007829|PDB:1QHB"
FT STRAND 284..287
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:1QHB"
FT STRAND 315..321
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 325..334
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 339..351
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 378..401
FT /evidence="ECO:0007829|PDB:1QHB"
FT TURN 402..404
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 409..424
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 434..439
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 441..458
FT /evidence="ECO:0007829|PDB:1QHB"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:1QHB"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 486..501
FT /evidence="ECO:0007829|PDB:1QHB"
FT TURN 503..505
FT /evidence="ECO:0007829|PDB:1QHB"
FT STRAND 512..514
FT /evidence="ECO:0007829|PDB:1QHB"
FT STRAND 516..523
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 532..550
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 555..576
FT /evidence="ECO:0007829|PDB:1QHB"
FT HELIX 577..579
FT /evidence="ECO:0007829|PDB:1QHB"
FT STRAND 587..589
FT /evidence="ECO:0007829|PDB:1QHB"
FT STRAND 595..597
FT /evidence="ECO:0007829|PDB:1QHB"
SQ SEQUENCE 598 AA; 65459 MW; BC784E370D748F01 CRC64;
MGIPADNLQS RAKASFDTRV SAAELALARG VVPSLANGEE LLYRNPDPEN GDPSFIVSFT
KGLPHDDNGA IIDPDDFLAF VRAINSGDEK EIADLTLGPA RDPDTGLPIW RSDLANSLEL
EVRGWENSSA GLTFDLEGPD AQSIAMPPAP VLTSPELIAE IAELYLMALG REIEFSEFDS
PKNAEYIQFA IDQLNGLEWF NTPAMLGDPP AEIRRRRGEV TVGNLFRGIL PGSEVGPYLS
QYIIVGSKQI GSATGGNKTL VSPNAADEFD GEIAYGSITI SQRVRIATPG RDFMTDLKVF
LDVQDAADFR GFESYEPGAR LIRTIRDLAT WVHFDALYEA YLNACLILLA NRVPFDPNIP
FQQEDKLDNQ DVFVNFGDAH VLSLVTEVAT RALKAVRYQK FNIHRRLRPE ATGGLISVNK
IAAEKGESVF PEVDLAVEEL EDILEKAEIS NRKQNIADGD PDPDPSFLLP QAFAEGSPFH
PSYGSGHAVV AGACVTILKA FFDSNFQIDQ VFEVDKDEDK LVKSSFKGTL TVAGELNKLA
DNIAIGRNMA GVHYFSDQFE SILLGEQVAI GILEEQSLTY GENFFFNLPK FDGTTIQI
