ID L0DUE6_THIND Unreviewed; 481 AA.
AC L0DUE6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=L-seryl-tRNA(Sec) selenium transferase {ECO:0000256|HAMAP-Rule:MF_00423};
DE EC=2.9.1.1 {ECO:0000256|HAMAP-Rule:MF_00423};
DE AltName: Full=Selenocysteine synthase {ECO:0000256|HAMAP-Rule:MF_00423};
DE Short=Sec synthase {ECO:0000256|HAMAP-Rule:MF_00423};
DE AltName: Full=Selenocysteinyl-tRNA(Sec) synthase {ECO:0000256|HAMAP-Rule:MF_00423};
GN Name=selA [H] {ECO:0000313|EMBL:AGA32627.1};
GN Synonyms=selA {ECO:0000256|HAMAP-Rule:MF_00423};
GN OrderedLocusNames=TVNIR_0939 {ECO:0000313|EMBL:AGA32627.1};
OS Thioalkalivibrio nitratireducens (strain DSM 14787 / UNIQEM 213 / ALEN2).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=1255043 {ECO:0000313|EMBL:AGA32627.1, ECO:0000313|Proteomes:UP000010809};
RN [1] {ECO:0000313|Proteomes:UP000010809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14787 / UNIQEM 213 / ALEN2
RC {ECO:0000313|Proteomes:UP000010809};
RA Tikhonova T.V., Pavlov A.R., Beletsky A.V., Mardanov A.V., Sorokin D.Y.,
RA Ravin N.V., Popov V.O.;
RT "Complete sequence of Thioalkalivibrio nitratireducens.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Converts seryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec)
CC required for selenoprotein biosynthesis. {ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_00423};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_00423, ECO:0000256|PIRSR:PIRSR618319-50};
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:0000256|HAMAP-Rule:MF_00423}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00423}.
CC -!- SIMILARITY: Belongs to the SelA family. {ECO:0000256|HAMAP-
CC Rule:MF_00423}.
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DR EMBL; CP003989; AGA32627.1; -; Genomic_DNA.
DR RefSeq; WP_015257768.1; NC_019902.2.
DR AlphaFoldDB; L0DUE6; -.
DR STRING; 1255043.TVNIR_0939; -.
DR KEGG; tni:TVNIR_0939; -.
DR PATRIC; fig|1255043.3.peg.945; -.
DR eggNOG; COG1921; Bacteria.
DR HOGENOM; CLU_038142_1_0_6; -.
DR OrthoDB; 9787096at2; -.
DR UniPathway; UPA00906; UER00896.
DR Proteomes; UP000010809; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004125; F:L-seryl-tRNA(Sec) selenium transferase activity; IEA:UniProtKB-UniRule.
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 InterPro; IPR025862; SelA_trans_N_dom.
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; PF12390; Se-cys_synth_N; 1.
DR Pfam; PF03841; SelA; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00423};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00423};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_00423};
KW Selenium {ECO:0000256|ARBA:ARBA00023266, ECO:0000256|HAMAP-Rule:MF_00423};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00423, ECO:0000313|EMBL:AGA32627.1}.
FT DOMAIN 21..58
FT /note="L-seryl-tRNA selenium transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12390"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 304
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00423,
FT ECO:0000256|PIRSR:PIRSR618319-50"
SQ SEQUENCE 481 AA; 52150 MW; 68C6A2711B668F86 CRC64;
MNPPAPPREP VDDANTATRP RPPSVDRLLA HPDAIDLQQR HGRQPVLLAL RARLDELRAR
DTRDPSDFEP PRLLAGVRSR LERDAAPRLQ RVFNLTGTVL HTNLGRAPLP AEAVNAAALA
AAGSCNLEFD LGRGRRGDRD DLINDLIREL TGAEAATVVN NNAAAVLLAL NTLALRKEVV
ISRGELVEIG GAFRIPEVMS RAGCRLVEVG ATNRTHARDF EAAIGPRTRL FMKAHTSNYA
IEGFTAAVAE NTLARIAHDH GLPFMIDLGS GTFVDLAQWG LPHEPTVQEA LRNGADVVTF
SGDKLLGGPQ AGLIVGRADL IARIKKNPLK RALRVDKMTL AALEAVLRIY RDPDRLTQRL
TTLRLLTRPQ AEIQVLAKRL QPLLATAFGE RFTVTLQACA SQIGSGALPV DRLPSAALVL
RPHRSGRGSG TALKRLEREL RDLPSPVIGR VHDGALWLDL RCLEDETGFA AQLAGAEAPR
P
//
