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Database: UniProt
Entry: A0A138A0H6_9ACTN
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ID   A0A138A0H6_9ACTN        Unreviewed;       431 AA.
AC   A0A138A0H6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
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=AXK60_19470 {ECO:0000313|EMBL:KXP03935.1};
OS   Tsukamurella pseudospumae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Tsukamurellaceae;
OC   Tsukamurella.
OX   NCBI_TaxID=239498 {ECO:0000313|EMBL:KXP03935.1, ECO:0000313|Proteomes:UP000070258};
RN   [1] {ECO:0000313|Proteomes:UP000070258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 15929 {ECO:0000313|Proteomes:UP000070258};
RA   Wen L., He K., Yang H.;
RL   Submitted (FEB-2016) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXP03935.1}.
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DR   EMBL; LSRF01000058; KXP03935.1; -; Genomic_DNA.
DR   RefSeq; WP_068575043.1; NZ_LSRF01000058.1.
DR   AlphaFoldDB; A0A138A0H6; -.
DR   STRING; 239498.AXK60_19470; -.
DR   OrthoDB; 9787096at2; -.
DR   UniPathway; UPA00906; UER00896.
DR   Proteomes; UP000070258; Unassembled WGS sequence.
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}.
FT   DOMAIN          5..44
FT                   /note="L-seryl-tRNA selenium transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12390"
FT   MOD_RES         280
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00423,
FT                   ECO:0000256|PIRSR:PIRSR618319-50"
SQ   SEQUENCE   431 AA;  43713 MW;  ADAEE69F1DC6C698 CRC64;
     MTDPRRRIPR TDRLLAEPVL VAAAARLGER RVRAAITQAQ DAARRGDLAP EEVAAAVDRE
     LAATAPSSLR PVLNVTGVVV HTNLGRAPLS AAAVAALVDA AGYVDVELDL ATGARSKRGV
     AARGALLAAC PAAEEALVVN NGAAALVLAT TALAAGREVV ISRGELIEIG AGFRLPDLIA
     STGARLREVG TTNRTHAGDY ADAIGPDTGC VLKVHPSNFR VEGFTAEVGL SELREVCGDV
     PLVMDLGSGL LAADPALPGE PDAASALAAG ADLVTASGDK LLGGPQAGIL LGRADLVQRL
     ARHPLARAVR ADKLVLAALE ATVGGPQAPV IAYLHADPDG LRRRAERLAG RVGGTVVPHD
     GRVGGGGAPG VPLPGWAVRL PEALAAPLRT GDPAVLPRVT DGACLIDLRC VPEDSDAAVA
     DAVQRALACT S
//
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