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E2IUA7 (GLUTS_KALDA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 attributes

Sequence length767 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Oxidosqualene cyclase that generates glutinol, a triterpenoid product. Glutinol is probably required to coat the leaf exterior as a defense compound against pathogens or herbivores. Ref.1

Catalytic activity

(3S)-2,3-epoxy-2,3-dihydrosqualene = glutinol. Ref.1

Tissue specificity

Expressed only in the epidermal cells on both sides of the leaf and not in internal leaf tissues. Ref.1

Sequence similarities

Belongs to the terpene cyclase/mutase family.

Contains 2 PFTB repeats.

Ontologies

Keywords
   DomainRepeat
   Molecular functionIsomerase
Gene Ontology (GO)
   Biological_processtriterpenoid biosynthetic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functionintramolecular transferase activity

Inferred from direct assay Ref.1. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 767767Glutinol synthase
PRO_0000418482

Regions

Repeat148 – 18942PFTB 1
Repeat640 – 68142PFTB 2

Sequences

Sequence LengthMass (Da)Tools
E2IUA7 [UniParc].

Last modified November 30, 2010. Version 1.
Checksum: C19EE928D94D71D0

FASTA76788,148
        10         20         30         40         50         60 
MWKLKIADGG SNPYIFTTNN FVGRQIWEFD PQATDPQQLA KVEAARLDFY HNRYKLKPNS 

        70         80         90        100        110        120 
DLLWRMQFLE EKDFRQNIPQ VKVEDGEEVS YEAVTAALRR GVHLYSALQA SDGHWPAENA 

       130        140        150        160        170        180 
GPMFFMPPMV MCLYITGHLN AIFTEEHRSE TLRYIYYHQN EDGGWGFHIE GHSTMFGTVL 

       190        200        210        220        230        240 
NYICMRLLGE GPEGGQDNAV SRGRKWILDH GGATSIPSWG KTWLSIMGLC DWSGCNPMPP 

       250        260        270        280        290        300 
EFWLLPSYLP MHPGKMWCYC RMVYMPMSYL YGKRFTARIT PLILQLREEI HIQPYDQIDW 

       310        320        330        340        350        360 
KKVRHVCCKE DMYYPHPLLQ DLLWDTLYLT TEPLLTRWPL NKLIRQRALQ KTMKHIHYED 

       370        380        390        400        410        420 
ENSRYITIGT VEKVLCMLAC WVEDPNGDYF KKHLARVPDY FWVAEDGMKI QSFGSQHWDT 

       430        440        450        460        470        480 
VFSAQALLAS DMADEIGTTL AKAHYCIKES QVKDNPSGDF RSMYRHISKG SWTFSDQDHG 

       490        500        510        520        530        540 
WQLSDCTAEG LKCCLLFSLM QPEVVGEAMP PERLFDSVNI LLYLQSKNGG MPGWEPAGAS 

       550        560        570        580        590        600 
EWLELLNPTE FFENIVIEHE YVECTSSAVQ ALVLFKKLHP GHRRKEVERF ITNGAKYIED 

       610        620        630        640        650        660 
IQMPDGAWYG NWGVCFTYGA WFALGGLAAA GKTYNNCAAV RKGVDFLLRI QLEDGGWGES 

       670        680        690        700        710        720 
YQSCPDKKYV PLEDNRSNLV HTSWALMGLL CSGQADRDPN PLHRAAKLLI NSQLEDGDFP 

       730        740        750        760 
QQEITGVFKM NCMLHFAAYR SIFPVWALAE YKRFCNLSSE AISKPSK 

« Hide

References

[1]"Cloning and characterization of oxidosqualene cyclases from Kalanchoe daigremontiana: enzymes catalyzing up to 10 rearrangement steps yielding friedelin and other triterpenoids."
Wang Z., Yeats T., Han H., Jetter R.
J. Biol. Chem. 285:29703-29712(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
HM623869 mRNA. Translation: ADK35124.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-17973.

Family and domain databases

Gene3D1.50.10.20. 2 hits.
InterProIPR001330. Prenyltrans.
IPR018333. Squalene_cyclase.
IPR008930. Terpenoid_cyclase/PrenylTrfase.
[Graphical view]
PfamPF00432. Prenyltrans. 1 hit.
[Graphical view]
SUPFAMSSF48239. SSF48239. 2 hits.
TIGRFAMsTIGR01787. squalene_cyclas. 1 hit.
ProtoNetSearch...

Entry information

Entry nameGLUTS_KALDA
AccessionPrimary (citable) accession number: E2IUA7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 14 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