Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P33912 (BPA1_STRAU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 67. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Non-haem bromoperoxidase BPO-A1

EC=1.11.1.-
Alternative name(s):
BPO1
Bromide peroxidase
Encoded onPlasmid
OrganismStreptomyces aureofaciens
Taxonomic identifier1894 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

Protein attributes

Sequence length275 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Homodimer.

Sequence similarities

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

Ontologies

Keywords
   Biological processAntibiotic biosynthesis
   Molecular functionOxidoreductase
Peroxidase
   Technical term3D-structure
Direct protein sequencing
Plasmid
Gene Ontology (GO)
   Biological_processantibiotic biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionperoxidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 275274Non-haem bromoperoxidase BPO-A1
PRO_0000207066

Sites

Active site951 By similarity
Active site2241 By similarity
Active site2531 By similarity

Experimental info

Sequence conflict41C → S AA sequence Ref.2
Sequence conflict171W → D AA sequence Ref.2

Secondary structure

........................................... 275
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P33912 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: AA2F6A958C58406E

FASTA27530,475
        10         20         30         40         50         60 
MPICTTRDGV EIFYKDWGQG RPVVFIHGWP LNGDAWQDQL KAVVDAGYRG IAHDRRGHGH 

        70         80         90        100        110        120 
STPVWDGYDF DTFADDLNDL LTDLDLRDVT LVAHSMGGGE LARYVGRHGT GRLRSAVLLS 

       130        140        150        160        170        180 
AIPPVMIKSD KNPDGVPDEV FDALKNGVLT ERSQFWKDTA EGFFSANRPG NKVTQGNKDA 

       190        200        210        220        230        240 
FWYMAMAQTI EGGVRCVDAF GYTDFTEDLK KFDIPTLVVH GDDDQVVPID ATGRKSAQII 

       250        260        270 
PNAELKVYEG SSHGIAMVPG DKEKFNRDLL EFLNK 

« Hide

References

[1]"Cloning of a second non-haem bromoperoxidase gene from Streptomyces aureofaciens ATCC 10762: sequence analysis, expression in Streptomyces lividans and enzyme purification."
Pelletier I., Pfeifer O., Altenbuchner J., van Pee K.-P.
Microbiology 140:509-516(1994) [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.
Strain: ATCC 10762 / CCM 3239 / DSM 40127 / JCM 4008 / LMG 5968.
[3]"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).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U01096 Genomic DNA. Translation: AAC43253.1.
PIRS59929.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A8QX-ray1.75A2-275[»]
ProteinModelPortalP33912.
SMRP33912. Positions 2-275.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS33.992.
PeroxiBase5911. STaHalNPrx01.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.1820. 1 hit.
InterProIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
[Graphical view]
PRINTSPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMSSF53474. SSF53474. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP33912.

Entry information

Entry nameBPA1_STRAU
AccessionPrimary (citable) accession number: P33912
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 67 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references