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Q9X839 (CYC2_STRCO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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:
Germacradienol/geosmin synthase

Including the following 2 domains:

  1. Germacradienol/germacrene D synthase
    EC=4.2.3.22
    EC=4.2.3.75
    Alternative name(s):
    Sesquiterpene cyclase
    Sesquiterpene synthase
  2. Geosmin synthase
    EC=4.1.99.16
Gene names
Name:cyc2
Ordered Locus Names:SCO6073
ORF Names:SC9B1.20
OrganismStreptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]
Taxonomic identifier100226 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesStreptomycineaeStreptomycetaceaeStreptomycesStreptomyces albidoflavus group

Protein attributes

Sequence length726 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tow-domain protein where the N-terminal domain catalyzes the cyclization of farnesyl diphosphate (FPP) to a 85:15 mixture of the sesquiterpene alcohol germacradienol and the sesquiterpene hydrocarbon germacrene D. The C-terminal domain partially converts the germacradienol formed into geosmin, the characteristic odoriferous ('earthy aroma') constituent of Streptomyces species. Ref.2 Ref.3 Ref.4 Ref.5

Catalytic activity

(2E,6E)-farnesyl diphosphate + H2O = (1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + diphosphate. Ref.2

(1E,4S,5E,7R)-germacra-1(10),5-dien-11-ol + H2O = (-)-geosmin + acetone. Ref.2

(2E,6E)-farnesyl diphosphate = (-)-germacrene D + diphosphate. Ref.2

Cofactor

Magnesium. Fe2+ or Cu2+ ions are very less efficient as cofactors. Ref.2 Ref.5

Pathway

Secondary metabolite biosynthesis; geosmin biosynthesis.

Sesquiterpene biosynthesis; germacradienol biosynthesis; germacradienol from farnesyl diphosphate: step 1/1.

Sesquiterpene biosynthesis; germacrene D biosynthesis; germacrene D from farnesyl diphosphate: step 1/1.

Domain

Consists of 2 homologous sesquiterpene synthase domains. The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg2+. Ref.2 Ref.3

Miscellaneous

The earthy odorant geosmin is also responsible for the 'off-flavor' of contaminated drinking water, wines, and other foodstuffs.

Sequence similarities

Belongs to the terpene synthase family.

Caution

It is uncertain whether the initial Met is cleaved or not.

Biophysicochemical properties

Kinetic parameters:

KM=62 nM for FPP Ref.2

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2
Chain2 – 726725Germacradienol/geosmin synthase
PRO_0000247895

Regions

Region2 – 354353Germacradienol/germacrene D synthase
Region355 – 726372Geosmin synthase
Motif86 – 916DDXXD motif 1; degenerate
Motif455 – 4595DDXXD motif 2; degenerate

Sites

Metal binding861Magnesium Potential
Metal binding911Magnesium Potential
Metal binding2671Magnesium Potential
Metal binding2711Magnesium Potential
Metal binding2761Magnesium Potential
Metal binding4551Magnesium Potential
Metal binding5981Magnesium Potential
Metal binding6021Magnesium Potential
Metal binding6061Magnesium Potential

Sequences

Sequence LengthMass (Da)Tools
Q9X839 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: CB332AC7840EB81E

FASTA72681,474
        10         20         30         40         50         60 
MTQQPFQLPH FYLPHPARLN PHLDEARAHS TTWAREMGML EGSGVWEQSD LEAHDYGLLC 

        70         80         90        100        110        120 
AYTHPDCDGP ALSLITDWYV WVFFFDDHFL EKYKRSQDRL AGKAHLDRLP LFMPLDDAAG 

       130        140        150        160        170        180 
MPEPRNPVEA GLADLWTRTV PAMSADWRRR FAVATEHLLN ESMWELSNIN EGRVANPVEY 

       190        200        210        220        230        240 
IEMRRKVGGA PWSAGLVEYA TAEVPAAVAG TRPLRVLMET FSDAVHLRND LFSYQREVED 

       250        260        270        280        290        300 
EGELSNGVLV LETFFGCTTQ EAADLVNDVL TSRLHQFEHT AFTEVPAVAL EKGLTPLEVA 

       310        320        330        340        350        360 
AVGAYTKGLQ DWQSGGHEWH MRSSRYMNKG ERPLAGWQAL TGPGTSAADV GALLADAVAQ 

       370        380        390        400        410        420 
RARSYTYVPF QKVGPSVIPD IRMPYPLELS PALDGARRHL SEWCREMGIL SEGVWDEDKL 

       430        440        450        460        470        480 
ESCDLPLCAA GLDPDATQDQ LDLASGWLAF GTYGDDYYPL VYGHRRDLAA ARLTTTRLSD 

       490        500        510        520        530        540 
CMPLDGEPVP PPGNAMERSL IDLWVRTTAG MTPEERRPLK KAVDDMTEAW LWELSNQIQN 

       550        560        570        580        590        600 
RVPDPVDYLE MRRATFGSDL TLGLCRAGHG PAVPPEVYRS GPVRSLENAA IDYACLLNDV 

       610        620        630        640        650        660 
FSYQKEIEYE GEIHNAVLVV QNFFGVDYPA ALGVVQDLMN QRMRQFEHVV AHELPVVYDD 

       670        680        690        700        710        720 
FQLSEEARTV MRGYVTDLQN WMAGILNWHR NVPRYKAEYL AGRTHGFLPD RIPAPPVPRS 


SPALTH 

« Hide

References

« Hide 'large scale' references
[1]"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)."
Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. expand/collapse author list , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.
Nature 417:141-147(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-471 / A3(2) / M145.
[2]"Expression and mechanistic analysis of a germacradienol synthase from Streptomyces coelicolor implicated in geosmin biosynthesis."
Cane D.E., Watt R.M.
Proc. Natl. Acad. Sci. U.S.A. 100:1547-1551(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-10, FUNCTION, CATALYTIC ACTIVITY, DOMAIN, KINETIC PARAMETERS, COFACTOR.
Strain: ATCC BAA-471 / A3(2) / M145.
[3]"PCR-targeted Streptomyces gene replacement identifies a protein domain needed for biosynthesis of the sesquiterpene soil odor geosmin."
Gust B., Challis G.L., Fowler K., Kieser T., Chater K.F.
Proc. Natl. Acad. Sci. U.S.A. 100:1541-1546(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: DOMAIN, ROLE IN GEOSMIN BIOSYNTHESIS.
Strain: ATCC BAA-471 / A3(2) / M145.
[4]"Mechanism and stereochemistry of the germacradienol/germacrene D synthase of Streptomyces coelicolor A3(2)."
He X., Cane D.E.
J. Am. Chem. Soc. 126:2678-2679(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN GERMACRENE D PRODUCTION, REACTION STEREOCHEMISTRY.
Strain: ATCC BAA-471 / A3(2) / M145.
[5]"Geosmin biosynthesis. Streptomyces coelicolor germacradienol/germacrene D synthase converts farnesyl diphosphate to geosmin."
Jiang J., He X., Cane D.E.
J. Am. Chem. Soc. 128:8128-8129(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN DIRECT GEOSMIN PRODUCTION, COFACTOR, REACTION MECHANISM.
Strain: ATCC BAA-471 / A3(2) / M145.

Web resources

Protein Spotlight

The earth's perfume - Issue 35 of June 2003

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL939126 Genomic DNA. Translation: CAB41566.1.
PIRT35865.
RefSeqNP_630182.1. NC_003888.3.

3D structure databases

ProteinModelPortalQ9X839.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING100226.SCO6073.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB41566; CAB41566; CAB41566.
GeneID1101514.
KEGGsco:SCO6073.
PATRIC23742056. VBIStrCoe124346_6175.

Phylogenomic databases

eggNOGNOG15313.
HOGENOMHOG000253477.
KOK10187.
OMARLHQFEH.
OrthoDBEOG622PK5.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14022.
BRENDA4.2.3.22. 5998.
SABIO-RKQ9X839.
UniPathwayUPA00209.
UPA00283; UER00583.
UPA00285; UER00584.

Family and domain databases

Gene3D1.10.600.10. 2 hits.
InterProIPR005630. Terpene_synthase_metal-bd.
IPR008949. Terpenoid_synth.
[Graphical view]
PfamPF03936. Terpene_synth_C. 2 hits.
[Graphical view]
SUPFAMSSF48576. SSF48576. 2 hits.
ProtoNetSearch...

Entry information

Entry nameCYC2_STRCO
AccessionPrimary (citable) accession number: Q9X839
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 82 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

PATHWAY comments

Index of metabolic and biosynthesis pathways