RESID:AA0022
L-selenocysteine
Alternate names:
2-azanyl-3-selanylpropanoic acid;
3-selenylalanine;
SeCys;
selenium cysteine
Systematic name:
(2R)-2-amino-3-selanylpropanoic acid
Cross-references: CAS:10236-58-5; ChEBI:30000; PDBHET:CSE
Dates:
Created: 31-Mar-1995
Structure revised: 31-Mar-1995
Text changed: 31-May-2013
Formula: C 3 H 5 N 1 O 1 Se 1
Formula weight: #chem 150.05 #phys 150.953635
Correction formula: C 0 H 0 N 0 O 0 Se 0 #link SEC
Correction weight: #chem 0.00 #phys 0.000000
Based on AA0022
Correction formula: C 0 H 0 N 0 O 0 S -1 Se 1 #link CYS
Correction weight: #chem 46.91 #phys 47.944450
Based on AA0005
Reference 1:
Authors: Huber, R.E.; Criddle, R.S.
Journal: Arch. Biochem. Biophys. 122, 164-173, 1967
Title: Comparison of the chemical properties of selenocysteine and selenocystine with their sulfur analogs.
Cross-references: DOI:10.1016/0003-9861(67)90136-1; PMID:6076213
Reference 2:
Authors: Turner, D.C.; Stadtman, T.C.
Journal: Arch. Biochem. Biophys. 154, 366-381, 1973
Title: Purification of protein components of the clostridial glycine reductase system and characterization of protein A as a selenoprotein.
Cross-references: DOI:10.1016/0003-9861(73)90069-6; PMID:4734725
Reference 3:
Authors: Cone, J.E.; Del Río, R.M.; Davis, J.N.; Stadtman, T.C.
Journal: Proc. Natl. Acad. Sci. U.S.A. 73, 2659-2663, 1976
Title: Chemical characterization of the selenoprotein component of clostridial glycine reductase: identification of selenocysteine as the organoselenium moiety.
Cross-references: DOI:10.1073/pnas.73.8.2659; PMID:1066676
Reference 4:
Authors: Condell, R.A.; Tappel, A.L.
Journal: Biochim. Biophys. Acta 709, 304-309, 1982
Title: Amino acid sequence around the active-site selenocysteine of rat liver glutathione peroxidase.
Cross-references: DOI:10.1016/0167-4838(82)90472-1; PMID:6217842
Reference 5:
Authors: Günzler, W.A.; Steffens, G.J.; Grossmann, A.; Kim, S.-M.A.; Otting, F.; Wendel, A.; Flohé, L.
Journal: Hoppe-Seyler's Z. Physiol. Chem. 365, 195-212, 1984
Title: The amino-acid sequence of bovine glutathione peroxidase.
Cross-references: DOI:10.1515/bchm2.1984.365.1.195; PMID:6714945
Note: the initials of "S.M. Kim" in the PubMed citation are corrected
Reference 6:
Authors: Chambers, I.; Frampton, J.; Goldfarb, P.; Affara, N.; McBain, W.; Harrison, P.R.
Journal: EMBO J. 5, 1221-1227, 1986
Title: The structure of the mouse glutathione peroxidase gene: the selenocysteine in the active site is encoded by the 'termination' codon, TGA.
Cross-references: PMID:3015592
Note: gene sequence
Reference 7:
Authors: Zinoni, F.; Birkmann, A.; Stadtman, T.C.; Böck, A.
Journal: Proc. Natl. Acad. Sci. U.S.A. 83, 4650-4654, 1986
Title: Nucleotide sequence and expression of the selenocysteine-containing polypeptide of formate dehydrogenase (formate-hydrogen-lyase-linked) from Escherichia coli.
Cross-references: PMID:2941757
Note: gene sequence
Reference 8:
Authors: Sliwkowski, M.X.; Stadtman, T.C.
Journal: Proc. Natl. Acad. Sci. U.S.A. 85, 368-371, 1988
Title: Selenoprotein A of the clostridial glycine reductase complex: purification and amino acid sequence of the selenocysteine-containing peptide.
Cross-references: DOI:10.1073/pnas.85.2.368; PMID:2963330
Reference 9:
Authors: Hill, K.E.; Lloyd, R.S.; Yang, J.G.; Read, R.; Burk, R.F.
Journal: J. Biol. Chem. 266, 10050-10053, 1991
Title: The cDNA for rat selenoprotein P contains 10 TGA codons in the open reading frame.
Cross-references: PMID:2037562
Reference 10:
Authors: Dixon, H.B.F.
Journal: Eur. J. Biochem. 264, 607-609, 1999
Title: IUPAC-IUBMB Joint Commission on Biochemical Nomenclature (JCBN) and Nomenclature Committee of IUBMB (NC-IUBMB), newsletter 1999.
Cross-references: PMID:10523135
Note: http://www.chem.qmul.ac.uk/iubmb/newsletter/1999/item3.html ; the omission of the author in the PubMed citation is corrected
Reference 11:
Authors: Jormakka, M.; Törnroth, S.; Byrne, B.; Iwata, S.
Journal: Science 295, 1863-1868, 2002
Title: Molecular basis of proton motive force generation: structure of formate dehydrogenase-N.
Cross-references: DOI:10.1126/science.1068186; PMID:11884747
Note: X-ray diffraction, 1.6 angstroms
Reference 12:
Authors: Jormakka, M.; Tornroth, S.; Byrne, B.; Iwata, S.
Submission: submitted to the Protein Data Bank, January 2002
Description: Formate dehydrogenase N from E. coli.
Cross-references: PDB:1KQF
Note: X-ray diffraction, 1.60 angstroms
Reference 13:
Authors: Itoh, Y.; Bröcker, M.J.; Sekine, S.; Hammond, G.; Suetsugu, S.; Söll, D.; Yokoyama, S.
Journal: Science 340, 75-78, 2013
Title: Decameric SelA.tRNA(Sec) ring structure reveals mechanism of bacterial selenocysteine formation.
Cross-references: DOI:10.1126/science.1229521; PMID:23559248
Note: in bacteria selenocysteine is produced by serine acylation to tRNA(Sec) followed by reaction with selenophosphate to form selenocysteinyl-tRNA(Sec)
Comment: Selenocysteine is translated for the UGA codon in some genetic systems. It has not yet been demonstrated to arise alternatively from a post-translational modification.
Comment: Although the single letter symbol U is recommended by IUBMB, many software applications fail to recognize it, and some sequence databases may use the single letter symbol C.
Generating Enzyme:
serine--tRNA ligase (EC 6.1.1.11); L-seryl-tRNA(Sec) selenium transferase, SelA (EC 2.9.1.1); O-phosphoseryl-tRNA(Sec) kinase (EC 2.7.1.164); O-phospho-L-seryl-tRNA(Sec):L-selenocysteinyl-tRNA synthase, SepSecS (EC 2.9.1.2)
Sequence code: U #link SEC
Abbreviation: Sec
Cross-references: GO:0001514; PSI-MOD:00031
Sequence code: C #link CYS
Cross-references: PSI-MOD:00686
Source: natural
Keywords: pretranslational modification; selenium; selenocysteine
UniProt Features
NON_STD Selenocysteine
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