ID   SELA_GEOSL              Reviewed;         462 AA.
AC   P61736;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   07-JUN-2004, sequence version 1.
DT   25-MAY-2022, entry version 101.
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=GSU3369;
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA   Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(2003).
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; AE017180; AAR36759.1; -; Genomic_DNA.
DR   RefSeq; NP_954409.1; NC_002939.5.
DR   RefSeq; WP_010943980.1; NC_002939.5.
DR   AlphaFoldDB; P61736; -.
DR   SMR; P61736; -.
DR   STRING; 243231.GSU3369; -.
DR   PRIDE; P61736; -.
DR   EnsemblBacteria; AAR36759; AAR36759; GSU3369.
DR   KEGG; gsu:GSU3369; -.
DR   PATRIC; fig|243231.5.peg.3391; -.
DR   eggNOG; COG1921; Bacteria.
DR   HOGENOM; CLU_038142_1_0_7; -.
DR   InParanoid; P61736; -.
DR   OMA; GATNRTH; -.
DR   UniPathway; UPA00906; UER00896.
DR   Proteomes; UP000000577; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004125; F:L-seryl-tRNASec selenium transferase activity; IBA:GO_Central.
DR   GO; GO:0001514; P:selenocysteine incorporation; IEA:UniProtKB-UniRule.
DR   GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IBA:GO_Central.
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; Reference proteome;
KW   Selenium; Transferase.
FT   CHAIN           1..462
FT                   /note="L-seryl-tRNA(Sec) selenium transferase"
FT                   /id="PRO_0000189603"
FT   MOD_RES         292
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00423"
SQ   SEQUENCE   462 AA;  49936 MW;  F0E2EDA4898954E2 CRC64;
     MTIFSRIPKV DRILEQDEVR RLLADHPRPT VLAAVRTALD ALRAEARAGS LREQDLADGA
     VAGRVGREVA RSTACSLRRV VNGTGVVIHT NLGRSPLAER VRQRVDDTAY GYSNLEFDLE
     RGERGSRYSH VEKLLCELTG AEAALVVNNN AAAVLLALSA LAGGKEVIVS RGELVEIGGS
     FRIPDVMQQG GAVLREVGTT NRTHSRDYRQ AVTSETGLLL KVHSSNFAVV GFTAEVTAPE
     MVAIGRELGL PVMADIGSGC LIDLSRFGIR GEPTVQEFVS VGVDVVTFSG DKLLGGPQAG
     IIVGRKAYVD PLKKHPLLRA IRIDKLTLAA LEGTLRLYRD ERQALAEVPT LRMLTASAEE
     LRLRARQFMR RLRRGVPSSV RLASLDGVSQ VGGGAYPLLE LPTTLIAVDV DGVSPQEMEA
     RLRRMTVPVV GRINRGRFLL DARTLLDDDA PAVISALREL AS