ID A0A5Q2W1U0_9CELL Unreviewed; 484 AA.
AC A0A5Q2W1U0;
DT 26-FEB-2020, integrated into UniProtKB/TrEMBL.
DT 26-FEB-2020, sequence version 1.
DT 05-FEB-2025, entry version 16.
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 {ECO:0000256|HAMAP-Rule:MF_00423};
GN ORFNames=GCE65_14190 {ECO:0000313|EMBL:QGH70514.1};
OS Pseudactinotalea sp. HY158.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC Cellulomonadaceae; Pseudactinotalea.
OX NCBI_TaxID=2654547 {ECO:0000313|EMBL:QGH70514.1, ECO:0000313|Proteomes:UP000374843};
RN [1] {ECO:0000313|EMBL:QGH70514.1, ECO:0000313|Proteomes:UP000374843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HY158 {ECO:0000313|EMBL:QGH70514.1,
RC ECO:0000313|Proteomes:UP000374843};
RA Meng J.;
RL Submitted (NOV-2019) 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=L-seryl-tRNA(Sec) + selenophosphate + H(+) = 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|ARBA:ARBA00044507,
CC ECO:0000256|HAMAP-Rule:MF_00423}.
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DR EMBL; CP045920; QGH70514.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A5Q2W1U0; -.
DR KEGG; psei:GCE65_14190; -.
DR UniPathway; UPA00906; UER00896.
DR Proteomes; UP000374843; 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:0001717; P:conversion of seryl-tRNAsec to selenocys-tRNAsec; 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}; Reference proteome {ECO:0000313|Proteomes:UP000374843};
KW Selenium {ECO:0000256|ARBA:ARBA00023266, ECO:0000256|HAMAP-Rule:MF_00423};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00423, ECO:0000313|EMBL:QGH70514.1}.
FT DOMAIN 14..53
FT /note="L-seryl-tRNA selenium transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12390"
FT REGION 459..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 294
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00423,
FT ECO:0000256|PIRSR:PIRSR618319-50"
SQ SEQUENCE 484 AA; 49262 MW; 8202677C91EA50FB CRC64;
MLPGCEGGTV PDPRRGIPRT DALLALPAAR AAADRLGPNR VRTAVRASQE AARRGELAPE
AVEADTLARI AGLESREASS LRPVLNATGV VVHTNLGRAP LSDAARAAVA AASGYTDLEL
DLRTGRRSRR GEGARAALLA ACPAAGDALV VNNGAAALLL AVTALAAGRD VIISRGELVE
IGGGFRLPEL LTATGARLRE VGTTNRTHAR DYSGALGAET GCLLKVHPSN FTQAGFVTDV
PLTELRGIAS EGGVPLVADL GSGLLHPEPV LPGEPDVTSA LAAGADLVIV SGDKLLGGPQ
AGILLGRVDL IDRLARHPLA RALRADKLTL AALEATVIAL TAMPGPAAAT PVMSAVRADP
QRLRDRAEAL AAALPASLAA TVVPHDGRVG GGGAPGVALQ GWAVRLPERL ARTLRANDPA
VLARTHDGAC LLDLRCIPEA DDDVLQRVVR AALAAPEVLP APAPDLPTGP STELPHVPAG
GEAR
//
