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Q8LLW7 (PRXV_COROI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Vanadium-dependent bromoperoxidase
EC=1.11.1.18
Alternative name(s):
Vanadium haloperoxidase
OrganismCorallina officinalis (Coral seaweed)
Taxonomic identifier35170 [NCBI]
Taxonomic lineageEukaryota › Rhodophyta › Florideophyceae › Corallinales › Corallinaceae › Corallinoideae › Corallina

Protein attributes

Sequence length598 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the halogenation of organic substrates in the presence of hydrogen peroxide. Ref.1

Catalytic activity

RH + HBr + H2O2 = RBr + 2 H2O. Ref.1

Cofactor

Binds 1 calcium ion per subunit. The binding is important for enzyme stability. Ref.2

Binds 1 vanadate ion per subunit. Ref.2

Subunit structure

Homododecamer. Ref.1

Sequence similarities

Belongs to the bacterial non-heme bromo- and chloro-peroxidases family.

Biophysicochemical properties

Kinetic parameters:

KM=1.2 mM for bromide Ref.1

KM=1.8 mM for iodide

KM=17 µM for H2O2

pH dependence:

Optimum pH is 6.0.

Ontologies

Keywords
   LigandMetal-binding
Vanadium
   Molecular functionOxidoreductase
Peroxidase
   Technical term3D-structure
Gene Ontology (GO)
   Cellular componentmembrane

Inferred from electronic annotation. Source: InterPro

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

peroxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 598598Vanadium-dependent bromoperoxidase
PRO_0000401199

Regions

Calcium binding361 – 37010
Region485 – 4873Vanadate binding By similarity
Compositional bias214 – 2174Poly-Arg

Sites

Active site4801 By similarity
Active site4871 By similarity
Binding site4001Vanadate By similarity
Binding site4081Vanadate By similarity
Binding site5471Vanadate By similarity
Binding site5531Vanadate By similarity

Experimental info

Mutagenesis4801H → A: Shows 4% of wild-type activity. Ref.1

Secondary structure

1 ........................................................................... 598
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8LLW7 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: BC784E370D748F01

FASTA59865,459
        10         20         30         40         50         60 
MGIPADNLQS RAKASFDTRV SAAELALARG VVPSLANGEE LLYRNPDPEN GDPSFIVSFT 

        70         80         90        100        110        120 
KGLPHDDNGA IIDPDDFLAF VRAINSGDEK EIADLTLGPA RDPDTGLPIW RSDLANSLEL 

       130        140        150        160        170        180 
EVRGWENSSA GLTFDLEGPD AQSIAMPPAP VLTSPELIAE IAELYLMALG REIEFSEFDS 

       190        200        210        220        230        240 
PKNAEYIQFA IDQLNGLEWF NTPAMLGDPP AEIRRRRGEV TVGNLFRGIL PGSEVGPYLS 

       250        260        270        280        290        300 
QYIIVGSKQI GSATGGNKTL VSPNAADEFD GEIAYGSITI SQRVRIATPG RDFMTDLKVF 

       310        320        330        340        350        360 
LDVQDAADFR GFESYEPGAR LIRTIRDLAT WVHFDALYEA YLNACLILLA NRVPFDPNIP 

       370        380        390        400        410        420 
FQQEDKLDNQ DVFVNFGDAH VLSLVTEVAT RALKAVRYQK FNIHRRLRPE ATGGLISVNK 

       430        440        450        460        470        480 
IAAEKGESVF PEVDLAVEEL EDILEKAEIS NRKQNIADGD PDPDPSFLLP QAFAEGSPFH 

       490        500        510        520        530        540 
PSYGSGHAVV AGACVTILKA FFDSNFQIDQ VFEVDKDEDK LVKSSFKGTL TVAGELNKLA 

       550        560        570        580        590 
DNIAIGRNMA GVHYFSDQFE SILLGEQVAI GILEEQSLTY GENFFFNLPK FDGTTIQI

« Hide

References

[1]"Reactivity of recombinant and mutant vanadium bromoperoxidase from the red alga Corallina officinalis."
Carter J.N., Beatty K.E., Simpson M.T., Butler A.
J. Inorg. Biochem. 91:59-69(2002) [PubMed: 12121762] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, MUTAGENESIS OF HIS-480.
[2]"Crystal structure of dodecameric vanadium-dependent bromoperoxidase from the red algae Corallina officinalis."
Isupov M.N., Dalby A.R., Brindley A.A., Izumi Y., Tanabe T., Murshudov G.N., Littlechild J.A.
J. Mol. Biol. 299:1035-1049(2000) [PubMed: 10843856] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH CALCIUM AND PHOSPHATE, COFACTOR.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF218810 mRNA. Translation: AAM46061.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QHBX-ray2.30A/B/C/D/E/F1-596[»]
ProteinModelPortalQ8LLW7.
SMRQ8LLW7. Positions 2-598.
ModBaseSearch...

Protein family/group databases

PeroxiBase5901. CoVBPo.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR016119. Br/Cl_peroxidase_C.
IPR000326. P_Acid_Pase_2/haloperoxidase.
[Graphical view]
Gene3DG3DSA:1.10.606.10. Br/Cl_peroxidase_C. 1 hit.
PfamPF01569. PAP2. 1 hit.
[Graphical view]
SUPFAMSSF48317. AcPase_VanPerase. 1 hit.
ProtoNetSearch...

Entry information

Entry namePRXV_COROI
AccessionPrimary (citable) accession number: Q8LLW7
Entry history
Integrated into UniProtKB/Swiss-Prot: November 30, 2010
Last sequence update: October 1, 2002
Last modified: June 28, 2011
This is version 36 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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