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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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei99 – 991By similarity
Active sitei229 – 2291By similarity
Active sitei258 – 2581By similarity

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 278277Non-haem bromoperoxidase BPO-A2PRO_0000207067Add
BLAST

Interactioni

Subunit structurei

Homotrimer.

Structurei

Secondary structure

1
278
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 97Combined sources
Beta strandi12 – 2110Combined sources
Beta strandi23 – 308Combined sources
Helixi37 – 404Combined sources
Helixi41 – 499Combined sources
Beta strandi53 – 575Combined sources
Helixi74 – 8815Combined sources
Beta strandi92 – 987Combined sources
Helixi99 – 1013Combined sources
Helixi102 – 11211Combined sources
Beta strandi117 – 1248Combined sources
Helixi143 – 15513Combined sources
Helixi157 – 16812Combined sources
Helixi171 – 1744Combined sources
Turni176 – 1783Combined sources
Helixi181 – 19313Combined sources
Helixi196 – 2016Combined sources
Helixi202 – 2054Combined sources
Turni211 – 2133Combined sources
Helixi214 – 2163Combined sources
Beta strandi221 – 2266Combined sources
Beta strandi230 – 2323Combined sources
Helixi234 – 2363Combined sources
Helixi238 – 2447Combined sources
Beta strandi248 – 2536Combined sources
Helixi260 – 2634Combined sources
Helixi265 – 27713Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-278.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29715.

Family & Domainsi

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
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. Positions 2-278.
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...

Publicationsi

  1. "Molecular cloning and sequencing of a non-haem bromoperoxidase gene from Streptomyces aureofaciens ATCC 10762."
    Pfeifer O., Pelletier I., Altenbuchner J., van Pee K.-H.
    J. Gen. Microbiol. 138:1123-1131(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ATCC 10762 / CCM 3239 / DSM 40127 / JCM 4008 / LMG 5968.
  2. "Purification, characterization and comparison of two non-haem bromoperoxidases from Streptomyces aureofaciens ATCC 10762."
    Weng M., Pfeifer O., Krauss S., Lingens F., van Pee K.-H.
    J. Gen. Microbiol. 137:2539-2546(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-21.
  3. "The metal-ion-free oxidoreductase from Streptomyces aureofaciens has an alpha/beta hydrolase fold."
    Hecht H.-J., Sobek H., Haag T., Pfeifer O., van Pee K.-H.
    Nat. Struct. Biol. 1:532-537(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
    Strain: ATCC 10762 / CCM 3239 / DSM 40127 / JCM 4008 / LMG 5968.
  4. "Structural investigation of the cofactor-free chloroperoxidases."
    Hofmann B., Tolzer S., Pelletier I., Altenbuchner J., van Pee K.-H., Hecht H.-J.
    J. Mol. Biol. 279:889-900(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS).
    Strain: ATCC 10762 / CCM 3239 / DSM 40127 / JCM 4008 / LMG 5968.

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: October 14, 2015
This is version 85 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.