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Q9L9D7 (COCE_RHOSM) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 73. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cocaine esterase
EC=3.1.1.-
Gene names
Name:cocE
OrganismRhodococcus sp. (strain MB1 Bresler)
Taxonomic identifier104109 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length574 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Hydrolyzes cocaine to benzoate and ecgonine methyl ester, endowing the bacteria with the ability to utilize cocaine as a sole source of carbon and energy for growth, as this bacterium lives in the rhizosphere of coca plants.

Catalytic activity

Cocaine + H2O = ecgonine methyl ester + benzoate. Ref.1

Pathway

Alkaloid degradation; cocaine degradation.

Subunit structure

Monomer. Ref.1

Subcellular location

Cytoplasm Probable.

Induction

Positively induced by cocaine.

Domain

It consists of three domains: domain 1 contains the active site; domains 2 and 3 are involved in substrate recognition. Domain 1 contains the GxSxxG motif found in most members of the alpha/beta hydrolase family.

Biotechnological use

Has potential as a highly-sensitive drug detector. It is also an attractive candidate for rapid cocaine detoxification in an emergency setting.

Miscellaneous

This enzyme hydrolyzes cocaine faster than any other known cocaine esterase.

Sequence similarities

Belongs to the alpha/beta hydrolase family. Carboxylesterase subfamily.

Biophysicochemical properties

Kinetic parameters:

KM=0.64 µM for cocaine Ref.3

Ontologies

Keywords
   Cellular componentCytoplasm
   Molecular functionHydrolase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological processproteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionaminopeptidase activity

Inferred from electronic annotation. Source: InterPro

dipeptidyl-peptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 574574Cocaine esterase
PRO_0000090000

Regions

Region1 – 1441441A
Region145 – 240962
Region241 – 3541141B
Region355 – 5742203

Sites

Active site1171
Active site2591
Active site2871
Site441Probably involved in activating the substrate carbonyl and the acyl enzyme for hydrolysis

Experimental info

Mutagenesis441Y → F: Loss of activity. Ref.3
Mutagenesis551Q → A or E: Decrease in activity. Ref.3
Mutagenesis1171S → A: Loss of activity. Ref.3
Mutagenesis1171S → C: Great decrease in activity. Ref.3
Mutagenesis1511W → A: Decrease in activity. Ref.3
Mutagenesis1661W → A: Decrease in activity. Ref.3
Mutagenesis2591D → N: Loss of activity. Ref.3
Mutagenesis2611F → A: Decrease in activity. Ref.3
Mutagenesis2871H → A: Loss of activity. Ref.3
Mutagenesis4071L → A: Decrease in activity. Ref.3
Mutagenesis4081F → A: Decrease in activity. Ref.3

Secondary structure

1 ................................................................................................. 574
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9L9D7 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 9E35724F586089B7

FASTA57462,132
        10         20         30         40         50         60 
MVDGNYSVAS NVMVPMRDGV RLAVDLYRPD ADGPVPVLLV RNPYDKFDVF AWSTQSTNWL 

        70         80         90        100        110        120 
EFVRDGYAVV IQDTRGLFAS EGEFVPHVDD EADAEDTLSW ILEQAWCDGN VGMFGVSYLG 

       130        140        150        160        170        180 
VTQWQAAVSG VGGLKAIAPS MASADLYRAP WYGPGGALSV EALLGWSALI GTGLITSRSD 

       190        200        210        220        230        240 
ARPEDAADFV QLAAILNDVA GAASVTPLAE QPLLGRLIPW VIDQVVDHPD NDESWQSISL 

       250        260        270        280        290        300 
FERLGGLATP ALITAGWYDG FVGESLRTFV AVKDNADARL VVGPWSHSNL TGRNADRKFG 

       310        320        330        340        350        360 
IAATYPIQEA TTMHKAFFDR HLRGETDALA GVPKVRLFVM GIDEWRDETD WPLPDTAYTP 

       370        380        390        400        410        420 
FYLGGSGAAN TSTGGGTLST SISGTESADT YLYDPADPVP SLGGTLLFHN GDNGPADQRP 

       430        440        450        460        470        480 
IHDRDDVLCY STEVLTDPVE VTGTVSARLF VSSSAVDTDF TAKLVDVFPD GRAIALCDGI 

       490        500        510        520        530        540 
VRMRYRETLV NPTLIEAGEI YEVAIDMLAT SNVFLPGHRI MVQVSSSNFP KYDRNSNTGG 

       550        560        570 
VIAREQLEEM CTAVNRIHRG PEHPSHIVLP IIKR

« Hide

References

[1]"Gene cloning and nucleotide sequencing and properties of a cocaine esterase from Rhodococcus sp. strain MB1."
Bresler M.M., Rosser S.J., Basran A., Bruce N.C.
Appl. Environ. Microbiol. 66:904-908(2000) [PubMed: 10698749] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-11, CATALYTIC ACTIVITY, SUBUNIT.
[2]"Crystal structure of a bacterial cocaine esterase."
Larsen N.A., Turner J.M., Stevens J., Rosser S.J., Basran A., Lerner R.A., Bruce N.C., Wilson I.A.
Nat. Struct. Biol. 9:17-21(2002) [PubMed: 11742345] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS).
[3]"Biochemical characterization and structural analysis of a highly proficient cocaine esterase."
Turner J.M., Larsen N.A., Basran A., Barbas C.F. III, Bruce N.C., Wilson I.A., Lerner R.A.
Biochemistry 41:12297-12307(2002) [PubMed: 12369817] [Abstract]
Cited for: MUTAGENESIS OF TYR-44; GLN-55; SER-117; TRP-151; TRP-166; ASP-259; PHE-261; HIS-287; LEU-407 AND PHE-408, X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF MUTANTS Y44F AND S117A, BIOPHYSICOCHEMICAL PROPERTIES.
+Additional computationally mapped references.

Web resources

Protein Spotlight

Rhodococcus: Nature's junkie - Issue 27 of October 2002

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF173165 Genomic DNA. Translation: AAF42807.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JU3X-ray1.58A1-574[»]
1JU4X-ray1.63A1-574[»]
1L7QX-ray1.76A1-574[»]
1L7RX-ray1.64A1-574[»]
3I2FX-ray2.50A1-574[»]
3I2GX-ray2.50A1-574[»]
3I2HX-ray1.65A1-574[»]
3I2IX-ray2.14A1-574[»]
3I2JX-ray2.01A1-574[»]
3I2KX-ray1.51A1-574[»]
3IDAX-ray1.60A1-574[»]
3PUHX-ray2.30A/B1-574[»]
3PUIX-ray1.53A1-574[»]
ProteinModelPortalQ9L9D7.
SMRQ9L9D7. Positions 5-574.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15371.
BRENDA3.1.1.1. 5397.

Family and domain databases

InterProIPR005674. CocE_NonD_hydro.
IPR008979. Galactose-bd-like.
IPR013736. Pept_S15/CocE/NonD_C.
IPR000383. X-Pro-like_dom.
[Graphical view]
PfamPF02129. Peptidase_S15. 1 hit.
PF08530. PepX_C. 1 hit.
[Graphical view]
SMARTSM00939. PepX_C. 1 hit.
[Graphical view]
SUPFAMSSF49785. Gal_bind_like. 1 hit.
TIGRFAMsTIGR00976. /NonD. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCOCE_RHOSM
AccessionPrimary (citable) accession number: Q9L9D7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 31, 2002
Last sequence update: October 1, 2000
Last modified: November 16, 2011
This is version 73 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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