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P33912

- BPA1_STRAU

UniProt

P33912 - BPA1_STRAU

Protein

Non-haem bromoperoxidase BPO-A1

Gene
N/A
Organism
Streptomyces aureofaciens
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei95 – 951By similarity
    Active sitei224 – 2241By similarity
    Active sitei253 – 2531By similarity

    GO - Molecular functioni

    1. peroxidase activity Source: UniProtKB-KW

    GO - Biological processi

    1. antibiotic biosynthetic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Oxidoreductase, Peroxidase

    Keywords - Biological processi

    Antibiotic biosynthesis

    Protein family/group databases

    MEROPSiS33.992.
    PeroxiBasei5911. STaHalNPrx01.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Non-haem bromoperoxidase BPO-A1 (EC:1.11.1.-)
    Alternative name(s):
    BPO1
    Bromide peroxidase
    Encoded oniPlasmid0 Publication
    OrganismiStreptomyces aureofaciens
    Taxonomic identifieri1894 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 275274Non-haem bromoperoxidase BPO-A1PRO_0000207066Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    1
    275
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 53
    Beta strandi11 – 177
    Beta strandi19 – 268
    Helixi33 – 364
    Helixi37 – 459
    Beta strandi49 – 535
    Helixi70 – 8314
    Beta strandi88 – 947
    Helixi97 – 10812
    Beta strandi113 – 1208
    Helixi138 – 16326
    Turni164 – 1674
    Helixi175 – 18511
    Helixi190 – 20213
    Helixi206 – 2094
    Beta strandi216 – 2216
    Beta strandi225 – 2273
    Helixi229 – 2313
    Helixi233 – 2397
    Beta strandi244 – 2485
    Turni253 – 2575
    Helixi261 – 27313

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1A8QX-ray1.75A2-275[»]
    ProteinModelPortaliP33912.
    SMRiP33912. Positions 2-275.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP33912.

    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]
    PRINTSiPR00111. ABHYDROLASE.
    PR00412. EPOXHYDRLASE.
    SUPFAMiSSF53474. SSF53474. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    P33912-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPICTTRDGV EIFYKDWGQG RPVVFIHGWP LNGDAWQDQL KAVVDAGYRG    50
    IAHDRRGHGH STPVWDGYDF DTFADDLNDL LTDLDLRDVT LVAHSMGGGE 100
    LARYVGRHGT GRLRSAVLLS AIPPVMIKSD KNPDGVPDEV FDALKNGVLT 150
    ERSQFWKDTA EGFFSANRPG NKVTQGNKDA FWYMAMAQTI EGGVRCVDAF 200
    GYTDFTEDLK KFDIPTLVVH GDDDQVVPID ATGRKSAQII PNAELKVYEG 250
    SSHGIAMVPG DKEKFNRDLL EFLNK 275
    Length:275
    Mass (Da):30,475
    Last modified:January 23, 2007 - v3
    Checksum:iAA2F6A958C58406E
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti4 – 41C → S AA sequence (PubMed:1783900)Curated
    Sequence conflicti17 – 171W → D AA sequence (PubMed:1783900)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U01096 Genomic DNA. Translation: AAC43253.1.
    PIRiS59929.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U01096 Genomic DNA. Translation: AAC43253.1 .
    PIRi S59929.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1A8Q X-ray 1.75 A 2-275 [» ]
    ProteinModelPortali P33912.
    SMRi P33912. Positions 2-275.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi S33.992.
    PeroxiBasei 5911. STaHalNPrx01.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P33912.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    IPR000639. Epox_hydrolase-like.
    [Graphical view ]
    PRINTSi PR00111. ABHYDROLASE.
    PR00412. EPOXHYDRLASE.
    SUPFAMi SSF53474. SSF53474. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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).

    Entry informationi

    Entry nameiBPA1_STRAU
    AccessioniPrimary (citable) accession number: P33912
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 68 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

    External Data

    Dasty 3