Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q4VNK0 (SMTA_BRAOT) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 19. 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 namesRecommended name:
Selenocysteine Se-methyltransferase

Short name=BoSMT
EC=2.1.1.n3
Gene names
Name:SMT
OrganismBrassica oleracea var. italica (Broccoli)
Taxonomic identifier36774 [NCBI]
Taxonomic lineageEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonscore eudicotyledonsrosidsmalvidsBrassicalesBrassicaceaeBrassiceaeBrassica

Protein attributes

Sequence length346 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the methylation of DL- and L-selenocysteine with S-methylmethionine as donor. Methylates also DL-homocysteine, DL- and L-cysteine in vitro. May be involved in selenium detoxification. Ref.1 Ref.2

Catalytic activity

S-methyl-L-methionine + L-selenocysteine = L-methionine + Se-methyl-L- selenocysteine. Ref.1 Ref.2

Cofactor

Zinc Potential.

Enzyme regulation

Inhibited by L-methionine. Ref.1

Tissue specificity

Expressed in roots, young leaves and florets, but not detected in plants not exposed to selenium. Ref.1

Induction

Up-regulated by selenate, but not by selenite. Down-regulated by sulfate. Ref.1

Sequence similarities

Contains 1 Hcy-binding domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.0. Ref.1

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 346346Selenocysteine Se-methyltransferase
PRO_0000409375

Regions

Domain13 – 330318Hcy-binding
Compositional bias332 – 34413Ser-rich

Sites

Metal binding2481Zinc Potential
Metal binding3151Zinc Potential
Metal binding3161Zinc Potential

Sequences

Sequence LengthMass (Da)Tools
Q4VNK0 [UniParc].

Last modified July 5, 2005. Version 1.
Checksum: 50E11284D078FC8D

FASTA34637,863
        10         20         30         40         50         60 
MVTGNTKAET FYSMKELLKE TGGYAIIDGG LATELERHGA DLNDPLWSAK CLLTSPHLIH 

        70         80         90        100        110        120 
TVHLDYLEAG ADIISSASYQ ATIQGFEAKG YSIEKSESLL RKSVEIACEA RSTYYDKCKD 

       130        140        150        160        170        180 
DDDKKILKKR PILVAASVGS YGAFLADGSE YSGIYGDLIT LETLKDFHRR RVQVLAESGA 

       190        200        210        220        230        240 
DIIAFETIPN KLEAQAFAEL LDEGVAKIPG WFSFNSKDGV NVVSGDSIKE CIAIAEACEK 

       250        260        270        280        290        300 
VVAVGINCTP PRFIEGLVLE IAKVTSKPIL VYPNSGERYD PERKEWVENT GVGNEDFVSY 

       310        320        330        340 
VEKWMDAGVS LLGGCCRTTP TTIRAIHKRL VSRRSLFSSS SSSSHH 

« Hide

References

[1]"Molecular and biochemical characterization of the selenocysteine Se-methyltransferase gene and Se-methylselenocysteine synthesis in broccoli."
Lyi S.M., Heller L.I., Rutzke M., Welch R.M., Kochian L.V., Li L.
Plant Physiol. 138:409-420(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION BY SELENATE AND SULFATE, ENZYME REGULATION, TISSUE SPECIFICITY.
Strain: cv. Green comet.
[2]"Biochemical and molecular characterization of the homocysteine S-methyltransferase from broccoli (Brassica oleracea var. italica)."
Lyi S.M., Zhou X., Kochian L.V., Li L.
Phytochemistry 68:1112-1119(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
Strain: cv. Green comet.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY817737 mRNA. Translation: AAX20123.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-15249.

Family and domain databases

Gene3D3.20.20.330. 1 hit.
InterProIPR003726. S_MeTrfase.
[Graphical view]
PfamPF02574. S-methyl_trans. 1 hit.
[Graphical view]
SUPFAMSSF82282. S_methyl_trans. 1 hit.
PROSITEPS50970. HCY. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameSMTA_BRAOT
AccessionPrimary (citable) accession number: Q4VNK0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 31, 2011
Last sequence update: July 5, 2005
Last modified: March 6, 2013
This is version 19 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