ID   SELA_DESPS              Reviewed;         466 AA.
AC   Q6AMK5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=L-seryl-tRNA(Sec) selenium transferase {ECO:0000255|HAMAP-Rule:MF_00423};
DE            EC=2.9.1.1 {ECO:0000255|HAMAP-Rule:MF_00423};
DE   AltName: Full=Selenocysteine synthase {ECO:0000255|HAMAP-Rule:MF_00423};
DE            Short=Sec synthase {ECO:0000255|HAMAP-Rule:MF_00423};
DE   AltName: Full=Selenocysteinyl-tRNA(Sec) synthase {ECO:0000255|HAMAP-Rule:MF_00423};
GN   Name=selA {ECO:0000255|HAMAP-Rule:MF_00423}; OrderedLocusNames=DP1691;
OS   Desulfotalea psychrophila (strain LSv54 / DSM 12343).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfobacterales;
OC   Desulfocapsaceae; Desulfotalea.
OX   NCBI_TaxID=177439;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12343 / LSv54;
RX   PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x;
RA   Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M.,
RA   Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H.,
RA   Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.;
RT   "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from
RT   permanently cold Arctic sediments.";
RL   Environ. Microbiol. 6:887-902(2004).
CC   -!- FUNCTION: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec)
CC       required for selenoprotein biosynthesis. {ECO:0000255|HAMAP-
CC       Rule:MF_00423}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + L-seryl-tRNA(Sec) + selenophosphate = L-
CC         selenocysteinyl-tRNA(Sec) + phosphate; Xref=Rhea:RHEA:22728,
CC         Rhea:RHEA-COMP:9742, Rhea:RHEA-COMP:9743, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16144, ChEBI:CHEBI:43474, ChEBI:CHEBI:78533,
CC         ChEBI:CHEBI:78573; EC=2.9.1.1; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00423};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00423};
CC   -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC       biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec)
CC       (bacterial route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00423}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00423}.
CC   -!- SIMILARITY: Belongs to the SelA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00423}.
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DR   EMBL; CR522870; CAG36420.1; -; Genomic_DNA.
DR   RefSeq; WP_011188932.1; NC_006138.1.
DR   AlphaFoldDB; Q6AMK5; -.
DR   SMR; Q6AMK5; -.
DR   STRING; 177439.DP1691; -.
DR   PRIDE; Q6AMK5; -.
DR   EnsemblBacteria; CAG36420; CAG36420; DP1691.
DR   KEGG; dps:DP1691; -.
DR   eggNOG; COG1921; Bacteria.
DR   HOGENOM; CLU_038142_1_0_7; -.
DR   OMA; GATNRTH; -.
DR   OrthoDB; 1124266at2; -.
DR   UniPathway; UPA00906; UER00896.
DR   Proteomes; UP000000602; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004125; F:L-seryl-tRNASec selenium transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0001514; P:selenocysteine incorporation; IEA:UniProtKB-UniRule.
DR   GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.40.640.10; -; 1.
DR   HAMAP; MF_00423; SelA; 1.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR018319; SelA-like.
DR   InterPro; IPR004534; SelA_trans.
DR   Pfam; PF03841; SelA; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR00474; selA; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Protein biosynthesis; Pyridoxal phosphate; Reference proteome;
KW   Selenium; Transferase.
FT   CHAIN           1..466
FT                   /note="L-seryl-tRNA(Sec) selenium transferase"
FT                   /id="PRO_1000050362"
FT   MOD_RES         293
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00423"
SQ   SEQUENCE   466 AA;  51599 MW;  D8FA57BD392ED42E CRC64;
     MPKNNLLRTL PKVDESIAQL RSTGVAYSSD FVLKKSVQTC IARERQGILA GKITEKRAED
     SWHACFLKEL KERQAPNLRR MINGTGVVIH TNLGRSLLSS QVAERLAQTA SYYSNLEFDL
     ATGKRGSRYS LVEDTICELT GAEAALVVNN NAAAVFLALD ALCRGTEVIV SRGQLVEIGG
     SFRIPDVMAR SGADLVEVGA TNRTHLYDYE DAISEQTSML LRVHTSNFRI IGFTSEVPAE
     EMVGLARKKN LLTMEDLGSG SLIDLTSYGF PKEPTVQELV KAGVDVVTFS GDKLLGGPQA
     GIIVGSKSVV ERIKKSPMNR AFRVDKFTLA ALEVVLRSYY DSRQALQEIP TLRMLTTGKD
     VLLKRARRIS RRLSAKLKEK CTLRIVPTMS RVGGGAFPEH DLASWAVAFR PEHIRLSEIE
     KRLRKLNTPI IGRLENEKFL LDVRTIQDDE VGLLCSLLLE FFLEAS