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Q94FT4 (SALAT_PAPSO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 39. 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:
Salutaridinol 7-O-acetyltransferase

Short name=salAT
EC=2.3.1.150
Gene names
Name:SALAT
OrganismPapaver somniferum (Opium poppy)
Taxonomic identifier3469 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsRanunculalesPapaveraceaePapaveroideaePapaver

Protein attributes

Sequence length474 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the conversion of the phenanthrene alkaloid salutaridinol to salutaridinol-7-O-acetate, the immediate precursor of thebaine along the morphine biosynthetic pathway. Conversion of 7-O-acetylsalutaridinol into thebaine is spontaneous. Ref.1

Catalytic activity

Acetyl-CoA + salutaridinol = CoA + 7-O-acetylsalutaridinol. Ref.2

Pathway

Alkaloid biosynthesis; morphine biosynthesis.

Tissue specificity

Expressed in root, stem, leaf and capsule of the mature plant. Ref.1

Sequence similarities

Belongs to the plant acyltransferase family.

Biophysicochemical properties

Kinetic parameters:

KM=9 µM for salutaridinol Ref.1

KM=54 µM for acetyl-CoA

Vmax=25 pmol/sec/mg enzyme

pH dependence:

Optimum pH is 7-9.

Temperature dependence:

Optimum temperature is 47 degrees Celsius.

Ontologies

Keywords
   Biological processAlkaloid metabolism
   Molecular functionAcyltransferase
Transferase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processalkaloid metabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionsalutaridinol 7-O-acetyltransferase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 474474Salutaridinol 7-O-acetyltransferase
PRO_0000147366

Sites

Active site1631Proton acceptor Potential
Active site4161Proton acceptor Potential

Sequences

Sequence LengthMass (Da)Tools
Q94FT4 [UniParc].

Last modified December 1, 2001. Version 1.
Checksum: 3A467FEE8B6A155E

FASTA47452,632
        10         20         30         40         50         60 
MATMYSAAVE VISKETIKPT TPTPSQLKNF NLSLLDQCFP LYYYVPIILF YPATAANSTG 

        70         80         90        100        110        120 
SSNHHDDLDL LKSSLSKTLV HFYPMAGRMI DNILVDCHDQ GINFYKVKIR GKMCEFMSQP 

       130        140        150        160        170        180 
DVPLSQLLPS EVVSASVPKE ALVIVQVNMF DCGGTAICSS VSHKIADAAT MSTFIRSWAS 

       190        200        210        220        230        240 
TTKTSRSGGS TAAVTDQKLI PSFDSASLFP PSERLTSPSG MSEIPFSSTP EDTEDDKTVS 

       250        260        270        280        290        300 
KRFVFDFAKI TSVREKLQVL MHDNYKSRRQ TRVEVVTSLI WKSVMKSTPA GFLPVVHHAV 

       310        320        330        340        350        360 
NLRKKMDPPL QDVSFGNLSV TVSAFLPATT TTTTNAVNKT INSTSSESQV VLHELHDFIA 

       370        380        390        400        410        420 
QMRSEIDKVK GDKGSLEKVI QNFASGHDAS IKKINDVEVI NFWISSWCRM GLYEIDFGWG 

       430        440        450        460        470 
KPIWVTVDPN IKPNKNCFFM NDTKCGEGIE VWASFLEDDM AKFELHLSEI LELI 

« Hide

References

[1]"Molecular characterization of the salutaridinol 7-O-acetyltransferase involved in morphine biosynthesis in Opium poppy Papaver somniferum."
Grothe T., Lenz R., Kutchan T.M.
J. Biol. Chem. 276:30717-30723(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 14-30; 241-244; 257-272; 287-313; 340-362 AND 378-394, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY.
[2]"Acetyl coenzyme A:salutaridinol-7-O-acetyltransferase from Papaver somniferum plant cell cultures. The enzyme catalyzing the formation of thebaine in morphine biosynthesis."
Lenz R., Zenk M.H.
J. Biol. Chem. 270:31091-31096(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF339913 mRNA. Translation: AAK73661.1.

3D structure databases

ProteinModelPortalQ94FT4.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12301.
BRENDA2.3.1.150. 4515.
UniPathwayUPA00852.

Family and domain databases

Gene3D3.30.559.10. 2 hits.
InterProIPR023213. CAT-like_dom.
IPR003480. Transferase.
[Graphical view]
PfamPF02458. Transferase. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSALAT_PAPSO
AccessionPrimary (citable) accession number: Q94FT4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: December 1, 2001
Last modified: April 16, 2014
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways