ID SELA_AQUAE Reviewed; 452 AA. AC O67140; DT 14-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 133. 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}; GN OrderedLocusNames=aq_1031; OS Aquifex aeolicus (strain VF5). OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Aquifex. OX NCBI_TaxID=224324; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=VF5; RX PubMed=9537320; DOI=10.1038/32831; RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.; RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."; RL Nature 392:353-358(1998). 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 -!- INTERACTION: CC O67140; O67140: selA; NbExp=3; IntAct=EBI-16044058, EBI-16044058; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00423}. CC -!- SIMILARITY: Belongs to the SelA family. {ECO:0000255|HAMAP- CC Rule:MF_00423}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AE000657; AAC07094.1; -; Genomic_DNA. DR PIR; A70389; A70389. DR RefSeq; NP_213703.1; NC_000918.1. DR RefSeq; WP_010880641.1; NC_000918.1. DR PDB; 3W1H; X-ray; 3.89 A; A/B/C/D/E=1-452. DR PDB; 3W1I; X-ray; 3.19 A; A/B/C/D/E/F/G/H/I/J=62-452. DR PDB; 3W1J; X-ray; 3.25 A; A/B/C/D/E/F/G/H/I/J=62-452. DR PDB; 3W1K; X-ray; 7.50 A; A/B/C/D/E=1-452. DR PDB; 3WCN; X-ray; 3.35 A; A/B=1-452. DR PDB; 3WCO; X-ray; 2.40 A; A/B=62-452. DR PDBsum; 3W1H; -. DR PDBsum; 3W1I; -. DR PDBsum; 3W1J; -. DR PDBsum; 3W1K; -. DR PDBsum; 3WCN; -. DR PDBsum; 3WCO; -. DR AlphaFoldDB; O67140; -. DR SMR; O67140; -. DR DIP; DIP-61414N; -. DR STRING; 224324.aq_1031; -. DR EnsemblBacteria; AAC07094; AAC07094; aq_1031. DR KEGG; aae:aq_1031; -. DR PATRIC; fig|224324.8.peg.805; -. DR eggNOG; COG1921; Bacteria. DR HOGENOM; CLU_038142_1_0_0; -. DR InParanoid; O67140; -. DR OrthoDB; 9787096at2; -. DR BRENDA; 2.9.1.1; 396. DR UniPathway; UPA00906; UER00896. DR Proteomes; UP000000798; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0004125; F:L-seryl-tRNA(Sec) selenium transferase activity; IBA:GO_Central. DR GO; GO:0001514; P:selenocysteine incorporation; IEA:UniProtKB-UniRule. DR Gene3D; 3.90.1150.180; -; 1. DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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 NCBIfam; TIGR00474; selA; 1. DR PANTHER; PTHR32328; L-SERYL-TRNA(SEC) SELENIUM TRANSFERASE; 1. DR PANTHER; PTHR32328:SF0; L-SERYL-TRNA(SEC) SELENIUM TRANSFERASE; 1. DR Pfam; PF03841; SelA; 1. DR SUPFAM; SSF53383; PLP-dependent transferases; 1. PE 1: Evidence at protein level; KW 3D-structure; Cytoplasm; Protein biosynthesis; Pyridoxal phosphate; KW Reference proteome; Selenium; Transferase. FT CHAIN 1..452 FT /note="L-seryl-tRNA(Sec) selenium transferase" FT /id="PRO_0000189594" FT MOD_RES 285 FT /note="N6-(pyridoxal phosphate)lysine" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00423" FT HELIX 2..6 FT /evidence="ECO:0007829|PDB:3WCN" FT HELIX 11..17 FT /evidence="ECO:0007829|PDB:3WCN" FT HELIX 24..43 FT /evidence="ECO:0007829|PDB:3WCN" FT HELIX 53..64 FT /evidence="ECO:0007829|PDB:3WCN" FT STRAND 73..77 FT /evidence="ECO:0007829|PDB:3WCO" FT HELIX 82..84 FT /evidence="ECO:0007829|PDB:3WCO" FT HELIX 91..101 FT /evidence="ECO:0007829|PDB:3WCO" FT STRAND 102..105 FT /evidence="ECO:0007829|PDB:3WCO" FT TURN 111..114 FT /evidence="ECO:0007829|PDB:3WCO" FT HELIX 119..122 FT /evidence="ECO:0007829|PDB:3WCO" FT HELIX 124..131 FT /evidence="ECO:0007829|PDB:3WCO" FT STRAND 134..140 FT /evidence="ECO:0007829|PDB:3WCO" FT HELIX 142..154 FT /evidence="ECO:0007829|PDB:3WCO" FT STRAND 157..162 FT /evidence="ECO:0007829|PDB:3WCO" FT HELIX 163..166 FT /evidence="ECO:0007829|PDB:3WCO" FT STRAND 167..169 FT /evidence="ECO:0007829|PDB:3WCO" FT TURN 170..172 FT /evidence="ECO:0007829|PDB:3W1I" FT HELIX 174..180 FT /evidence="ECO:0007829|PDB:3WCO" FT TURN 181..183 FT /evidence="ECO:0007829|PDB:3WCO" FT STRAND 185..191 FT /evidence="ECO:0007829|PDB:3WCO" FT STRAND 192..194 FT /evidence="ECO:0007829|PDB:3W1J" FT HELIX 197..202 FT /evidence="ECO:0007829|PDB:3WCO" FT STRAND 208..214 FT /evidence="ECO:0007829|PDB:3WCO" FT STRAND 218..224 FT /evidence="ECO:0007829|PDB:3W1I" FT HELIX 230..240 FT /evidence="ECO:0007829|PDB:3WCO" FT STRAND 244..250 FT /evidence="ECO:0007829|PDB:3WCO" FT HELIX 256..259 FT /evidence="ECO:0007829|PDB:3WCO" FT HELIX 268..273 FT /evidence="ECO:0007829|PDB:3WCO" FT STRAND 277..282 FT /evidence="ECO:0007829|PDB:3WCO" FT STRAND 289..291 FT /evidence="ECO:0007829|PDB:3WCO" FT STRAND 293..297 FT /evidence="ECO:0007829|PDB:3WCO" FT HELIX 299..307 FT /evidence="ECO:0007829|PDB:3WCO" FT HELIX 310..313 FT /evidence="ECO:0007829|PDB:3WCO" FT HELIX 318..332 FT /evidence="ECO:0007829|PDB:3WCO" FT HELIX 336..338 FT /evidence="ECO:0007829|PDB:3WCO" FT HELIX 340..345 FT /evidence="ECO:0007829|PDB:3WCO" FT HELIX 349..362 FT /evidence="ECO:0007829|PDB:3WCO" FT TURN 363..365 FT /evidence="ECO:0007829|PDB:3WCO" FT STRAND 369..378 FT /evidence="ECO:0007829|PDB:3WCO" FT STRAND 381..384 FT /evidence="ECO:0007829|PDB:3W1I" FT STRAND 390..402 FT /evidence="ECO:0007829|PDB:3WCO" FT HELIX 404..413 FT /evidence="ECO:0007829|PDB:3WCO" FT STRAND 414..416 FT /evidence="ECO:0007829|PDB:3WCO" FT STRAND 418..423 FT /evidence="ECO:0007829|PDB:3WCO" FT STRAND 426..430 FT /evidence="ECO:0007829|PDB:3WCO" FT HELIX 431..433 FT /evidence="ECO:0007829|PDB:3W1I" FT HELIX 436..438 FT /evidence="ECO:0007829|PDB:3WCO" FT HELIX 439..449 FT /evidence="ECO:0007829|PDB:3WCO" SQ SEQUENCE 452 AA; 50848 MW; E511326E17E9F015 CRC64; MKSLLRQIPQ ISKVVEIFKK KYPEIYVVKA AREVAEKYRK EIIEGKRKDL NGFLEDVERK IKSLMKPNIK RVINATGVVI NTNLGRAPLS KDVINFISEI ANGYSNLEYN LEEGKRGSRI AHIEKYLNEL TGAESSFVVN NNAGAVFLVL NTLAEGKEVI ISRGELVEIG GSFRIPDIMK KSGAILREVG TTNKTKVSDY EGAINQNTAL LMKVHKSNFY MEGFVEEVKL EDLVKLGHKY GIPTYYDAGS GLLINLKEFG ISVDEPNFRD CISLGIDLVS GSGDKLLGGP QAGIIVGKKN LIEKIKKNPI ARALRIDKLT LSGLEMTLKL YFEKRYEDIP VIRMLTQDEK ALRQKAKRLE KLLKDIPGLK ISVIKDKAKP GGGSLPELEL PTYCVAIRHD RLSSQELSRR LRLAEPPIVC RIREDQLLFD MRTVFHEDLK TIKKTLQELL SI //