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Protein

Non-heme chloroperoxidase CPO-A1

Gene

bpoA1

Organism
Streptomyces aureofaciens
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May be a chlorinating enzyme involved in 7-chlorotetracycline biosynthesis. Able to brominate as well.1 Publication

Enzyme regulationi

Brominating activity not inhibited by azide, peroxidase activity stimulated by bromide.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei95 – 951Charge relay systemCurated
Active sitei224 – 2241Charge relay systemCurated
Active sitei253 – 2531Charge relay systemCurated

GO - Molecular functioni

  1. peroxidase activity Source: UniProtKB-KW

GO - Biological processi

  1. antibiotic biosynthetic process Source: UniProtKB-KW
Complete GO annotation...

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-heme chloroperoxidase CPO-A11 Publication (EC:1.11.1.-)
Short name:
CPO-A1
Alternative name(s):
BPO11 Publication
Bromide peroxidase
Non-haem bromoperoxidase BPO-A11 Publication
Gene namesi
Name:bpoA1
OrganismiStreptomyces aureofaciens
Taxonomic identifieri1894 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 275274Non-heme chloroperoxidase CPO-A1PRO_0000207066Add
BLAST

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MPICTTRDGV EIFYKDWGQG RPVVFIHGWP LNGDAWQDQL KAVVDAGYRG
60 70 80 90 100
IAHDRRGHGH STPVWDGYDF DTFADDLNDL LTDLDLRDVT LVAHSMGGGE
110 120 130 140 150
LARYVGRHGT GRLRSAVLLS AIPPVMIKSD KNPDGVPDEV FDALKNGVLT
160 170 180 190 200
ERSQFWKDTA EGFFSANRPG NKVTQGNKDA FWYMAMAQTI EGGVRCVDAF
210 220 230 240 250
GYTDFTEDLK KFDIPTLVVH GDDDQVVPID ATGRKSAQII PNAELKVYEG
260 270
SSHGIAMVPG DKEKFNRDLL EFLNK
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:
EMBLi
GenBanki
DDBJi
Links Updated
U01096 Genomic DNA. Translation: AAC43253.1.
PIRiS59929.
RefSeqiWP_030556552.1. NZ_JOER01000052.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01096 Genomic DNA. Translation: AAC43253.1.
PIRiS59929.
RefSeqiWP_030556552.1. NZ_JOER01000052.1.

3D structure databases

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

Protein family/group databases

MEROPSiS33.992.
PeroxiBasei5911. STaHalNPrx01.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP33912.

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.
ProtoNetiSearch...

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, FUNCTION, ENZYME REGULATION, SUBUNIT.
    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) OF 2-275, PROBABLE CATALYTIC ACTIVITY.

Entry informationi

Entry nameiCPOA1_STRAU
AccessioniPrimary (citable) accession number: P33912
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: November 26, 2014
This is version 69 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

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

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 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.