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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)DescriptionActionsGraphical viewLength
Active sitei95Charge relay systemCurated1
Active sitei224Charge relay systemCurated1
Active sitei253Charge relay systemCurated1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase, Peroxidase

Keywords - Biological processi

Antibiotic biosynthesis

Protein family/group databases

ESTHERistrau-brpa1. Haloperoxidase.
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 lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00002070662 – 275Non-heme chloroperoxidase CPO-A1Add BLAST274

Interactioni

Subunit structurei

Homodimer.1 Publication

Structurei

Secondary structure

1275
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi3 – 5Combined sources3
Beta strandi11 – 17Combined sources7
Beta strandi19 – 26Combined sources8
Helixi33 – 36Combined sources4
Helixi37 – 45Combined sources9
Beta strandi49 – 53Combined sources5
Helixi70 – 83Combined sources14
Beta strandi88 – 94Combined sources7
Helixi97 – 108Combined sources12
Beta strandi113 – 120Combined sources8
Helixi138 – 163Combined sources26
Turni164 – 167Combined sources4
Helixi175 – 185Combined sources11
Helixi190 – 202Combined sources13
Helixi206 – 209Combined sources4
Beta strandi216 – 221Combined sources6
Beta strandi225 – 227Combined sources3
Helixi229 – 231Combined sources3
Helixi233 – 239Combined sources7
Beta strandi244 – 248Combined sources5
Turni253 – 257Combined sources5
Helixi261 – 273Combined sources13

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP33912.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini22 – 255AB hydrolase-1Sequence analysisAdd BLAST234

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.

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)DescriptionActionsGraphical viewLength
Sequence conflicti4C → S AA sequence (PubMed:1783900).Curated1
Sequence conflicti17W → D AA sequence (PubMed:1783900).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01096 Genomic DNA. Translation: AAC43253.1.
PIRiS59929.
RefSeqiWP_030556552.1. NZ_LBHA01000051.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01096 Genomic DNA. Translation: AAC43253.1.
PIRiS59929.
RefSeqiWP_030556552.1. NZ_LBHA01000051.1.

3D structure databases

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

Protein family/group databases

ESTHERistrau-brpa1. Haloperoxidase.
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]
PfamiPF00561. Abhydrolase_1. 1 hit.
[Graphical view]
PRINTSiPR00111. ABHYDROLASE.
PR00412. EPOXHYDRLASE.
SUPFAMiSSF53474. SSF53474. 1 hit.
ProtoNetiSearch...

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 2, 2016
This is version 77 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

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.