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Q9AR04 (AMS1_ARTAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Amorpha-4,11-diene synthase
EC=4.2.3.24
Gene names
Name:AMS1
Synonyms:KCS12
OrganismArtemisia annua (Sweet wormwood)
Taxonomic identifier35608 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › eudicotyledons › core eudicotyledons › asterids › campanulids › Asterales › Asteraceae › Asteroideae › Anthemideae › Artemisiinae › Artemisia

Protein attributes

Sequence length546 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in the biosynthesis of the antimalarial endoperoxide artemisinin. Catalyzes the formation of both olefinic and oxygenated sesquiterpenes, with amorpha-4,11-diene being the major product. Ref.1 Ref.3 Ref.4

Catalytic activity

(2E,6E)-farnesyl diphosphate = amorpha-4,11-diene + diphosphate.

Cofactor

Binds 3 magnesium or manganese ions per subunit By similarity.

Subcellular location

Cytoplasm Probable.

Induction

By exposure to reactive oxygen species. Ref.4

Domain

The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg2+.

Sequence similarities

Belongs to the terpene synthase family.

Biophysicochemical properties

Kinetic parameters:

KM=9 µM for farnesyl diphosphate (at pH 7.5) Ref.1

KM=70 µM for magnesium ions

KM=13 µM for manganese ions

pH dependence:

Optimum pH is 7.5-9.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMagnesium
Manganese
Metal-binding
   Molecular functionLyase
Gene Ontology (GO)
   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionamorpha-4,11-diene synthase activity

Inferred from electronic annotation. Source: EC

magnesium ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 546546Amorpha-4,11-diene synthase
PRO_0000248160

Regions

Motif299 – 3035DDXXD motif

Sites

Metal binding2991Magnesium or manganese 1 By similarity
Metal binding2991Magnesium or manganese 2 By similarity
Metal binding3031Magnesium or manganese 1 By similarity
Metal binding3031Magnesium or manganese 2 By similarity
Metal binding4431Magnesium or manganese 3 By similarity
Metal binding4471Magnesium or manganese 3 By similarity
Metal binding4511Magnesium or manganese 3 By similarity

Experimental info

Sequence conflict241F → S in ABB51572. Ref.5
Sequence conflict281E → Q in AAF98444. Ref.4
Sequence conflict811R → Q in AAK15697. Ref.2
Sequence conflict811R → Q in AAK15696. Ref.2
Sequence conflict991N → D in AAK15697. Ref.2
Sequence conflict991N → D in AAK15696. Ref.2
Sequence conflict1291N → D in AAK15697. Ref.2
Sequence conflict1291N → D in AAK15696. Ref.2
Sequence conflict1581I → T in ABB51572. Ref.5
Sequence conflict1591I → M in AAK15697. Ref.2
Sequence conflict1591I → M in AAK15696. Ref.2
Sequence conflict1731I → M in CAB94691. Ref.3
Sequence conflict2771Y → F Ref.2
Sequence conflict2771Y → F Ref.3
Sequence conflict3791K → N in ABB51572. Ref.5
Sequence conflict4121G → D in ABB51572. Ref.5
Sequence conflict4431N → D in ABB51572. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9AR04 [UniParc].

Last modified September 5, 2006. Version 2.
Checksum: 381386A7ED81FEF9

FASTA54663,933
        10         20         30         40         50         60 
MSLTEEKPIR PIANFPPSIW GDQFLIYEKQ VEQGVEQIVN DLKKEVRQLL KEALDIPMKH 

        70         80         90        100        110        120 
ANLLKLIDEI QRLGIPYHFE REIDHALQCI YETYGDNWNG DRSSLWFRLM RKQGYYVTCD 

       130        140        150        160        170        180 
VFNNYKDKNG AFKQSLANDV EGLLELYEAT SMRVPGEIIL EDALGFTRSR LSIMTKDAFS 

       190        200        210        220        230        240 
TNPALFTEIQ RALKQPLWKR LPRIEAAQYI PFYQQQDSHN KTLLKLAKLE FNLLQSLHKE 

       250        260        270        280        290        300 
ELSHVCKWWK AFDIKKNAPC LRDRIVECYF WGLGSGYEPQ YSRARVFFTK AVAVITLIDD 

       310        320        330        340        350        360 
TYDAYGTYEE LKIFTEAVER WSITCLDTLP EYMKPIYKLF MDTYTEMEEF LAKEGRTDLF 

       370        380        390        400        410        420 
NCGKEFVKEF VRNLMVEAKW ANEGHIPTTE EHDPVVIITG GANLLTTTCY LGMSDIFTKE 

       430        440        450        460        470        480 
SVEWAVSAPP LFRYSGILGR RLNDLMTHKA EQERKHSSSS LESYMKEYNV NEEYAQTLIY 

       490        500        510        520        530        540 
KEVEDVWKDI NREYLTTKNI PRPLLMAVIY LCQFLEVQYA GKDNFTRMGD EYKHLIKSLL 


VYPMSI

« Hide

References

[1]"Molecular cloning, expression, and characterization of a amorpha-4,11-diene synthase from, a key enzyme of artemisinin biosynthesis of Artemisia annua L."
Mercke P.E., Bengtsson M., Bouwmeester H.J., Posthumus M.A., Brodelius P.E.
Arch. Biochem. Biophys. 381:173-180(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
Tissue: Leaf.
[2]"Cloning of sesquiterpene cyclase gene from Artemisia annua."
Liu Y., Ye H.C., Li G.F.
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Leaf.
[3]"Amorpha-4,11-diene synthase of Artemisia annua: cDNA isolation and bacterial expression of a terpene synthase involved in artemisinin biosynthesis."
Chang Y.-J., Song S.-H., Park S.-H., Kim S.-U.
Arch. Biochem. Biophys. 383:178-184(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION.
[4]"Amorpha-4,11-diene synthase: cloning and functional expression of a key enzyme in the biosynthetic pathway of the novel antimalarial drug artemisinin."
Wallaart T.E., Bouwmeester H.J., Hille J., Poppinga L., Maijers N.C.A.
Planta 212:460-465(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INDUCTION.
[5]"Cloning and sequencing of amorpha-4,11-diene synthase cDNA of Artemisia annua L."
Huang Y., Feng L.L., Zeng Q.P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Leaf.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF138959 mRNA. Translation: AAF61439.1.
AF327527 Genomic DNA. Translation: AAK15697.1.
AF327526 mRNA. Translation: AAK15696.1.
AJ251751 mRNA. Translation: CAB94691.1.
AY006482 mRNA. Translation: AAF98444.1.
DQ241826 mRNA. Translation: ABB51572.1.

3D structure databases

ProteinModelPortalQ9AR04.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-12182.
BRENDA4.2.3.24. 7150.

Family and domain databases

Gene3D1.10.600.10. 1 hit.
1.50.30.10. 1 hit.
InterProIPR001906. Terpene_synth_N.
IPR005630. Terpene_synthase_metal-bd.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
IPR008949. Terpenoid_synth.
[Graphical view]
PfamPF01397. Terpene_synth. 1 hit.
PF03936. Terpene_synth_C. 1 hit.
[Graphical view]
SUPFAMSSF48239. Terp_cyc_toroid. 1 hit.
SSF48576. Terpenoid_synth. 1 hit.
ProtoNetSearch...

Entry information

Entry nameAMS1_ARTAN
AccessionPrimary (citable) accession number: Q9AR04
Secondary accession number(s): Q306S5 expand/collapse secondary AC list , Q9FVM5, Q9FY41, Q9LW98
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2006
Last sequence update: September 5, 2006
Last modified: May 29, 2013
This is version 53 of the entry and version 2 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

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