ID   SELA_MOOTH              Reviewed;         470 AA.
AC   O33277;
DT   14-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 89.
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};
OS   Moorella thermoacetica (Clostridium thermoaceticum).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Moorella group; Moorella.
OX   NCBI_TaxID=1525;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=ATCC 35608 / DSM 521 / JCM 9319;
RX   PubMed=9688279; DOI=10.1046/j.1432-1327.1998.2540655.x;
RA   Tormay P., Wilting R., Lottspeich F., Mehta P.K., Christen P., Boeck A.;
RT   "Bacterial selenocysteine synthase -- structural and functional
RT   properties.";
RL   Eur. J. Biochem. 254:655-661(1998).
CC   -!- FUNCTION: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec)
CC       required for selenoprotein biosynthesis. {ECO:0000255|HAMAP-
CC       Rule:MF_00423, ECO:0000269|PubMed:9688279}.
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; Y14814; CAA75096.1; -; Genomic_DNA.
DR   RefSeq; WP_011393981.1; NZ_VNHL01000001.1.
DR   AlphaFoldDB; O33277; -.
DR   SMR; O33277; -.
DR   PATRIC; fig|1525.10.peg.649; -.
DR   OMA; GATNRTH; -.
DR   OrthoDB; 1124266at2; -.
DR   UniPathway; UPA00906; UER00896.
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   InterPro; IPR025862; SelA_trans_N_dom.
DR   Pfam; PF12390; Se-cys_synth_N; 1.
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; Selenium;
KW   Transferase.
FT   CHAIN           1..470
FT                   /note="L-seryl-tRNA(Sec) selenium transferase"
FT                   /id="PRO_0000189609"
FT   MOD_RES         292
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00423"
SQ   SEQUENCE   470 AA;  50590 MW;  0A5972B6A6B3D237 CRC64;
     MESRNLLRQL PAVDQLLQHP RLKDLSRENY KMVLALTRQV LDDWRLKIKN GATTIPDPGQ
     LAREIENRYH EAGRSSLRPV INATGVVLHT NLGRAILSPA ARAAALTAAG RYTNLEYDLE
     KGQRGNRYSH VTGLLKELTG AEEALVVNNN AAAVLLALST LAAGRETIIS RGQLVEIGGS
     FRIPEVMGQS GTRLVEVGTT NKTYIHDYER AVGPDTALLL KVHPSNYRIQ GFTREVTTAE
     LVELGRRVGV PVMEDLGSGF LIDLEAYGIT GEPTVQAEIN QGVDVVTFSG DKLLGGPQAG
     IIVGRRDLVA AMAGHPLTRA LRIDKMNLAA LEATLRAYRN PDRAVKEIPT LAALVALPED
     LRLRAEELQK LLTSVLGSRA RVGLMPTTSQ AGGGSLPVTE LPSWAITIRP EQGGAAGLVT
     ALRRTDPPVL ARVQDDLLLL DVRTLLPGEG EELARALVQA LEGAVHGGES