UniProtKB - P81701 (PRXV_ASCNO)
Protein
Vanadium-dependent bromoperoxidase
Gene
N/A
Organism
Ascophyllum nodosum (Knotted wrack) (Brown seaweed)
Status
Functioni
Catalyzes the halogenation of organic substrates in the presence of hydrogen peroxide.2 Publications
Catalytic activityi
- RH + Br(-) + H(2)O(2) = RBr + 2 H(2)O.Curated EC:1.11.1.18
Cofactori
vanadate1 PublicationNote: Binds 1 vanadate ion per subunit.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 341 | Vanadate1 Publication | 1 | |
Binding sitei | 349 | Vanadate1 Publication | 1 | |
Active sitei | 411 | 1 | ||
Active sitei | 418 | 1 | ||
Binding sitei | 480 | Vanadate1 Publication | 1 | |
Binding sitei | 486 | Vanadate1 Publication | 1 |
GO - Molecular functioni
- bromide peroxidase activity Source: UniProtKB-EC
- metal ion binding Source: UniProtKB-KW
Keywordsi
Molecular function | Oxidoreductase, Peroxidase |
Ligand | Metal-binding, Vanadium |
Enzyme and pathway databases
BRENDAi | 1.11.1.18, 8891 |
Protein family/group databases
PeroxiBasei | 5895, AnoVBPo |
Names & Taxonomyi
Protein namesi | Recommended name: Vanadium-dependent bromoperoxidase (EC:1.11.1.18)Short name: V-BPO Alternative name(s): Vanadium haloperoxidase |
Organismi | Ascophyllum nodosum (Knotted wrack) (Brown seaweed) |
Taxonomic identifieri | 52969 [NCBI] |
Taxonomic lineagei | Eukaryota › Sar › Stramenopiles › Ochrophyta › PX clade › Phaeophyceae › Fucales › Fucaceae › Ascophyllum |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000207068 | 1 – 557 | Vanadium-dependent bromoperoxidaseAdd BLAST | 557 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1 | Pyrrolidone carboxylic acid1 Publication | 1 | |
Disulfide bondi | 3 | Interchain (with C-41) | ||
Disulfide bondi | 41 | Interchain (with C-3) | ||
Disulfide bondi | 77 ↔ 86 | |||
Disulfide bondi | 441 ↔ 462 | |||
Disulfide bondi | 544 ↔ 555 |
Keywords - PTMi
Disulfide bond, Pyrrolidone carboxylic acidInteractioni
Subunit structurei
Homodimer; disulfide-linked.
1 PublicationStructurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P81701 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P81701 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 416 – 418 | Vanadate binding | 3 |
Sequence similaritiesi
Belongs to the bacterial non-heme bromo- and chloro-peroxidases family.Curated
Family and domain databases
Gene3Di | 1.10.606.10, 1 hit |
InterProi | View protein in InterPro IPR016119, Br/Cl_peroxidase_C IPR036938, P_Acid_Pase_2/haloperoxi_sf |
SUPFAMi | SSF48317, SSF48317, 1 hit |
i Sequence
Sequence statusi: Complete.
P81701-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
QTCSTSDDAD DPTPPNERDD EAFASRVAAA KRELEGTGTV CQINNGETDL
60 70 80 90 100
AAKFHKSLPH DDLGQVDADA FAALEDCILN GDLSICEDVP VGNSEGDPVG
110 120 130 140 150
RLVNPTAAFA IDISGPAFSA TTIPPVPTLP SPELAAQLAE VYWMALARDV
160 170 180 190 200
PFMQYGTDDI TVTAAANLAG MEGFPNLDAV SIGSDGTVDP LSQLFRATFV
210 220 230 240 250
GVETGPFISQ LLVNSFTIDS ITVEPKQETF APDVNYMVDF DEWLNIQNGG
260 270 280 290 300
PPAGPELLDD ELRFVRNARD LARVTFTDNI NTEAYRGALI LLGLDAFNRA
310 320 330 340 350
GVNGPFIDID RQAGFVNFGI SHYFRLIGAA ELAQRSSWYQ KWQVHRFARP
360 370 380 390 400
EALGGTLHLT IKGELNADFD LSLLENAELL KRVAAINAAQ NPNNEVTYLL
410 420 430 440 450
PQAIQEGSPT HPSYPSGHAT QNGAFATVLK ALIGLDRGGD CYPDPVYPDD
460 470 480 490 500
DGLKLIDFRG SCLTFEGEIN KLAVNVAFGR QMLGIHYRFD GIQGLLLGET
510 520 530 540 550
ITVRTLHQEL MTFAEESTFE FRLFTGEVIK LFQDGTFTID GFKCPGLVYT
GVENCVS
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 321 | S → D AA sequence (PubMed:8564812).Curated | 1 | |
Sequence conflicti | 341 | K → N AA sequence (PubMed:8564812).Curated | 1 | |
Sequence conflicti | 403 – 404 | AI → VY AA sequence (PubMed:8564812).Curated | 2 | |
Sequence conflicti | 407 – 408 | GS → T AA sequence (PubMed:8564812).Curated | 2 | |
Sequence conflicti | 409 | P → S AA sequence (PubMed:8564812).Curated | 1 | |
Sequence conflicti | 441 – 444 | CYPD → AIR AA sequence (PubMed:8564812).Curated | 4 | |
Sequence conflicti | 470 | N → K AA sequence (PubMed:8564812).Curated | 1 |
Similar proteinsi
Cross-referencesi
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1QI9 | X-ray | 2.05 | A/B | 2-556 | [»] | |
SMRi | P81701 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein family/group databases
PeroxiBasei | 5895, AnoVBPo |
Enzyme and pathway databases
BRENDAi | 1.11.1.18, 8891 |
Miscellaneous databases
EvolutionaryTracei | P81701 |
Family and domain databases
Gene3Di | 1.10.606.10, 1 hit |
InterProi | View protein in InterPro IPR016119, Br/Cl_peroxidase_C IPR036938, P_Acid_Pase_2/haloperoxi_sf |
SUPFAMi | SSF48317, SSF48317, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | PRXV_ASCNO | |
Accessioni | P81701Primary (citable) accession number: P81701 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 21, 2001 |
Last sequence update: | June 1, 2000 | |
Last modified: | April 7, 2021 | |
This is version 84 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencingDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families