Reviewed, UniProtKB/Swiss-Prot P0A821 (SELA_ECOLI)

Names and origin

Protein names

Recommended name:
    L-seryl-tRNA(Sec) selenium transferase
    EC=2.9.1.1
Alternative name(s):
    Selenocysteine synthase
      Short name=Sec synthase
    Selenocysteinyl-tRNA(Sec) synthase

Gene names

Name:	selA
Synonyms:	fdhA
Ordered Locus Names:	b3591, JW3564

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	463 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec) required for selenoprotein biosynthesis. Requires selenophosphate as the selenium-donor molecule. Ref.1 Ref.5
Catalytic activity	L-seryl-tRNA(Sec) + selenophosphate = L-selenocysteinyl-tRNA(Sec) + phosphate. Ref.5
Cofactor	Pyridoxal phosphate. Ref.1
Pathway	Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) (bacterial route): step 1/1. HAMAP MF_00423
Subunit structure	Homodecamer; pentamer of dimers. Binds only one seryl-tRNA(Sec) per dimer. Ref.6
Subcellular location	Cytoplasm. HAMAP MF_00423
Sequence similarities	Belongs to the selA family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Cellular component	Cytoplasm
Ligand	Pyridoxal phosphate Selenium
Molecular function	Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	selenocysteine incorporation Inferred from electronic annotation. Source: HAMAP
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	L-seryl-tRNASec selenium transferase activity Inferred from electronic annotation. Source: HAMAP protein binding Inferred from physical interaction. Source: IntAct selenium binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
mtlD	P09424	1	EBI-1118693,EBI-554652

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 463	463	L-seryl-tRNA(Sec) selenium transferase HAMAP MF_00423		PRO_0000189599
Amino acid modifications
	Modified residue	295	1	N6-(pyridoxal phosphate)lysine
Experimental info
	Mutagenesis	224	1	K → N: Still binds PLP. Ref.7
	Mutagenesis	295	1	K → N: Loss of activity and PLP binding. Ref.7
	Mutagenesis	328	1	K → N: Loss of PLP binding. Ref.7
	Sequence conflict	7	1	S → F in AAA24624. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P0A821-1 [UniParc]. Last modified June 7, 2005. Version 1. Checksum: CD724FF681D882DF	FASTA	463	50,607
	10 20 30 40 50 60 MTTETRSLYS QLPAIDRLLR DSSFLSLRDT YGHTRVVELL RQMLDEAREV IRGSQTLPAW 70 80 90 100 110 120 CENWAQEVDA RLTKEAQSAL RPVINLTGTV LHTNLGRALQ AEAAVEAVAQ AMRSPVTLEY 130 140 150 160 170 180 DLDDAGRGHR DRALAQLLCR ITGAEDACIV NNNAAAVLLM LAATASGKEV VVSRGELVEI 190 200 210 220 230 240 GGAFRIPDVM RQAGCTLHEV GTTNRTHAND YRQAVNENTA LLMKVHTSNY SIQGFTKAID 250 260 270 280 290 300 EAELVALGKE LDVPVVTDLG SGSLVDLSQY GLPKEPMPQE LIAAGVSLVS FSGDKLLGGP 310 320 330 340 350 360 QAGIIVGKKE MIARLQSHPL KRALRADKMT LAALEATLRL YLHPEALSEK LPTLRLLTRS 370 380 390 400 410 420 AEVIQIQAQR LQAPLAAHYG AEFAVQVMPC LSQIGSGSLP VDRLPSAALT FTPHDGRGSH 430 440 450 460 LESLAARWRE LPVPVIGRIY DGRLWLDLRC LEDEQRFLEM LLK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Selenocysteine synthase from Escherichia coli. Nucleotide sequence of the gene (selA) and purification of the protein." Forchhammer K., Leinfelder W., Boesmiller K., Veprek B., Boeck A. J. Biol. Chem. 266:6318-6323(1991) [PubMed: 2007584] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COFACTOR.
[2]	"Analysis of the Escherichia coli genome. V. DNA sequence of the region from 76.0 to 81.5 minutes." Sofia H.J., Burland V., Daniels D.L., Plunkett G. III, Blattner F.R. Nucleic Acids Res. 22:2576-2586(1994) [PubMed: 8041620] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Selenocysteine synthase from Escherichia coli. Analysis of the reaction sequence." Forchhammer K., Boeck A. J. Biol. Chem. 266:6324-6328(1991) [PubMed: 2007585] [Abstract] Cited for: FUNCTION, CATALYTIC ACTIVITY, REACTION MECHANISM.
[6]	"Structure of selenocysteine synthase from Escherichia coli and location of tRNA in the seryl-tRNA(sec)-enzyme complex." Engelhardt H., Forchhammer K., Mueller S., Goldie K.N., Boeck A. Mol. Microbiol. 6:3461-3467(1992) [PubMed: 1474891] [Abstract] Cited for: SUBUNIT.
[7]	"Bacterial selenocysteine synthase -- structural and functional properties." Tormay P., Wilting R., Lottspeich F., Mehta P.K., Christen P., Boeck A. Eur. J. Biochem. 254:655-661(1998) [PubMed: 9688279] [Abstract] Cited for: PLP BINDING SITE, SUBSTRATE SPECIFICITY, MUTAGENESIS OF LYS-224; LYS-295 AND LYS-328.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M64177 Genomic DNA. Translation: AAA24624.1. U00039 Genomic DNA. Translation: AAB18568.1. U00096 Genomic DNA. Translation: AAC76615.1. AP009048 Genomic DNA. Translation: BAE77702.1.
PIR	A65159.
RefSeq	AP_004201.1. NP_418048.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P0A821. 2 interactions.
2-D gel databases
ECO2DBASE	G050.7. 6TH EDITION.
Genome annotation databases
GeneID	948124.
GenomeReviews	Gene locus JW3564 in contig AP009048_GR. Gene locus b3591 in contig U00096_GR.
KEGG	ecj:JW3564. eco:b3591.
Organism-specific databases
EchoBASE	EB0934.
EcoGene	EG10941. selA.
CMR	Search...
Phylogenomic databases
HOGENOM	P0A821.
OMA	P0A821. ALWLDLR.
Enzyme and pathway databases
BioCyc	EcoCyc:EG10941-MON. MetaCyc:EG10941-MON.
Family and domain databases
HAMAP	MF_00423. [Tree]
InterPro	IPR018319. Pyridoxal-P-dep_Trfase. IPR004534. SelA_trans. [Graphical view]
Pfam	PF03841. SelA. 1 hit. [Graphical view]
TIGRFAMs	TIGR00474. selA. 1 hit.
ProtoNet	Search...

Entry information

Entry name

SELA_ECOLI

Accession

Primary (citable) accession number: P0A821
Secondary accession number(s): P23328 , P58225, P78119, Q2M7Q4

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	June 7, 2005
Last modified:	June 16, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)