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Protein

Non-haem bromoperoxidase BPO-A2

Gene

bpoA2

Organism
Streptomyces aureofaciens
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

May be a chlorinating enzyme involved in 7-chlorotetracycline biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei99By similarity1
Active sitei229By similarity1
Active sitei258By similarity1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Antibiotic biosynthesis

Enzyme and pathway databases

BRENDAi1.11.1.18. 5978.

Protein family/group databases

ESTHERistrau-brpa2. Haloperoxidase.
PeroxiBasei5908. STaHalNPrx02.

Names & Taxonomyi

Protein namesi
Recommended name:
Non-haem bromoperoxidase BPO-A2 (EC:1.11.1.-)
Alternative name(s):
BPO2
Bromide peroxidase
Gene namesi
Name:bpoA2
Encoded oniPlasmid pOP26210 Publication
OrganismiStreptomyces aureofaciens
Taxonomic identifieri1894 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002070672 – 278Non-haem bromoperoxidase BPO-A2Add BLAST277

Interactioni

Subunit structurei

Homotrimer.

Structurei

Secondary structure

1278
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 9Combined sources7
Beta strandi12 – 21Combined sources10
Beta strandi23 – 30Combined sources8
Helixi37 – 40Combined sources4
Helixi41 – 49Combined sources9
Beta strandi53 – 57Combined sources5
Helixi74 – 88Combined sources15
Beta strandi92 – 98Combined sources7
Helixi99 – 101Combined sources3
Helixi102 – 112Combined sources11
Beta strandi117 – 124Combined sources8
Helixi143 – 155Combined sources13
Helixi157 – 168Combined sources12
Helixi171 – 174Combined sources4
Turni176 – 178Combined sources3
Helixi181 – 193Combined sources13
Helixi196 – 201Combined sources6
Helixi202 – 205Combined sources4
Turni211 – 213Combined sources3
Helixi214 – 216Combined sources3
Beta strandi221 – 226Combined sources6
Beta strandi230 – 232Combined sources3
Helixi234 – 236Combined sources3
Helixi238 – 244Combined sources7
Beta strandi248 – 253Combined sources6
Helixi260 – 263Combined sources4
Helixi265 – 277Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BROX-ray2.05A/B2-278[»]
1BRTX-ray1.50A2-278[»]
3VDXX-ray3.00A/B/C1-278[»]
4D9JX-ray3.92A/B/C/D/E/F/G/H/I/J/K/L1-278[»]
4IQ4X-ray3.50A/B/C/D/E/F1-278[»]
4ITVX-ray3.60A/B/C/D/E/F/G/H/I/J/K/L1-278[»]
4IVJX-ray7.35A/B/C1-278[»]
4QESX-ray4.19A/B/C1-278[»]
4QF0X-ray6.49A/B/C/D/E/F1-278[»]
4QFFX-ray7.81A/B/C/D/E/F/G/H/I/J/K/L1-278[»]
ProteinModelPortaliP29715.
SMRiP29715.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29715.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini26 – 264AB hydrolase-1Sequence analysisAdd BLAST239

Sequence similaritiesi

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P29715-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPFITVGQEN STSIDLYYED HGTGQPVVLI HGFPLSGHSW ERQSAALLDA
60 70 80 90 100
GYRVITYDRR GFGQSSQPTT GYDYDTFAAD LNTVLETLDL QDAVLVGFSM
110 120 130 140 150
GTGEVARYVS SYGTARIAKV AFLASLEPFL LKTDDNPDGA APQEFFDGIV
160 170 180 190 200
AAVKADRYAF YTGFFNDFYN LDENLGTRIS EEAVRNSWNT AASGGFFAAA
210 220 230 240 250
AAPTTWYTDF RADIPRIDVP ALILHGTGDR TLPIENTARV FHKALPSAEY
260 270
VEVEGAPHGL LWTHAEEVNT ALLAFLAK
Length:278
Mass (Da):30,385
Last modified:January 23, 2007 - v3
Checksum:i955B5A7E20E71FE9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84990 Unassigned DNA. Translation: AAB84315.1.
PIRiS27614.
RefSeqiWP_030279028.1. NZ_LBHA01000101.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M84990 Unassigned DNA. Translation: AAB84315.1.
PIRiS27614.
RefSeqiWP_030279028.1. NZ_LBHA01000101.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BROX-ray2.05A/B2-278[»]
1BRTX-ray1.50A2-278[»]
3VDXX-ray3.00A/B/C1-278[»]
4D9JX-ray3.92A/B/C/D/E/F/G/H/I/J/K/L1-278[»]
4IQ4X-ray3.50A/B/C/D/E/F1-278[»]
4ITVX-ray3.60A/B/C/D/E/F/G/H/I/J/K/L1-278[»]
4IVJX-ray7.35A/B/C1-278[»]
4QESX-ray4.19A/B/C1-278[»]
4QF0X-ray6.49A/B/C/D/E/F1-278[»]
4QFFX-ray7.81A/B/C/D/E/F/G/H/I/J/K/L1-278[»]
ProteinModelPortaliP29715.
SMRiP29715.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

ESTHERistrau-brpa2. Haloperoxidase.
PeroxiBasei5908. STaHalNPrx02.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi1.11.1.18. 5978.

Miscellaneous databases

EvolutionaryTraceiP29715.

Family and domain databases

Gene3Di3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiBPOA2_STRAU
AccessioniPrimary (citable) accession number: P29715
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 88 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing, Plasmid

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.