ID   SELA_DESBA              Reviewed;         465 AA.
AC   P56372;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=L-seryl-tRNA(Sec) selenium transferase;
DE            EC=2.9.1.1;
DE   AltName: Full=Selenocysteine synthase;
DE            Short=Sec synthase;
DE   AltName: Full=Selenocysteinyl-tRNA(Sec) synthase;
GN   Name=selA;
OS   Desulfomicrobium baculatum (Desulfovibrio baculatus).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfomicrobiaceae; Desulfomicrobium.
OX   NCBI_TaxID=899;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=DSM 1743;
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: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;
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000250};
CC   -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec)
CC       biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec)
CC       (bacterial route): step 1/1.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SelA family. {ECO:0000305}.
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DR   EMBL; Y14815; CAA75098.1; -; Genomic_DNA.
DR   AlphaFoldDB; P56372; -.
DR   SMR; P56372; -.
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..465
FT                   /note="L-seryl-tRNA(Sec) selenium transferase"
FT                   /id="PRO_0000189597"
FT   MOD_RES         294
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   465 AA;  50688 MW;  21E2497085BDC815 CRC64;
     MSSLFRHIPS VDRFLQDLEQ DRALADLPRQ MLKDLVAEFL DLCREEIRAG VVTDESALAF
     TTLAARAGAY VRTRSRPHFR RVVNATGVVI HTNLGRSILA EEAVLAVAEG CRHYSNLEMD
     LDTGQRGSRY SHVEKLLCRL TGAEAGLVVN NNAAAVLLVL DTLAKGREVV VSRGQLVEIG
     GSFRIPEVMK KSGAVLREVG ATNRTHLRDY AEAIGPDTAM LMKVHTSNYR IIGFHKEVDL
     PDLVALGRER GLSTFEDLGS GNLFDFSPYG FMPEPTVQQV LRSGVDVVTF SGDKLLGGPQ
     AGVIVGRREF IERIKKNQLN RALRIDKMTL AALEATLRLY LDPEQARRTV PTLAMITAAP
     KELHARAGRL RRRLSRDLAG LASVAVKPGF SRVGGGSFPE QDLSTTLVSV APTGMDVDSL
     RQGLLAEDIP VVGRVEDGAF CLDPRTLMDA EFALVAGAMK AVLAR