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Database: UniProt
Entry: A0A1A0MDJ2_9MYCO
LinkDB: A0A1A0MDJ2_9MYCO
Original site: A0A1A0MDJ2_9MYCO 
ID   A0A1A0MDJ2_9MYCO        Unreviewed;       435 AA.
AC   A0A1A0MDJ2;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=A9W99_07780 {ECO:0000313|EMBL:OBA83569.1};
OS   Mycobacterium sp. 1164966.3.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=1856861 {ECO:0000313|EMBL:OBA83569.1, ECO:0000313|Proteomes:UP000092060};
RN   [1] {ECO:0000313|Proteomes:UP000092060}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1164966.3 {ECO:0000313|Proteomes:UP000092060};
RA   Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Garcia-Basteiro A.,
RA   Lopez-Varela E., Palencia S.;
RL   Submitted (JUN-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:OBA83569.1}.
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DR   EMBL; LZSG01000008; OBA83569.1; -; Genomic_DNA.
DR   RefSeq; WP_067374083.1; NZ_LZSG01000008.1.
DR   AlphaFoldDB; A0A1A0MDJ2; -.
DR   STRING; 1856861.A9W99_07780; -.
DR   OrthoDB; 9787096at2; -.
DR   UniPathway; UPA00906; UER00896.
DR   Proteomes; UP000092060; 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}; Reference proteome {ECO:0000313|Proteomes:UP000092060};
KW   Selenium {ECO:0000256|ARBA:ARBA00023266, ECO:0000256|HAMAP-Rule:MF_00423};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00423, ECO:0000313|EMBL:OBA83569.1}.
FT   DOMAIN          7..46
FT                   /note="L-seryl-tRNA selenium transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12390"
FT   MOD_RES         284
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00423,
FT                   ECO:0000256|PIRSR:PIRSR618319-50"
SQ   SEQUENCE   435 AA;  45077 MW;  D0443B13B1D0E48E CRC64;
     MTQVDPRRLI PRTDQLLALP AVQRARVRLG EHVVRAVVRE VQAQARRGDL APDRVQDGVL
     ASLAARTTTS LRPVLNATGV VVHTNLGRAP LAAGAVEALV EASGYVDVEL DLATGTRSQR
     GVAAREALLI ACPAAEDALV VNNGAAALVL ATTALSAGKE VVVSRGELIE IGAGFRLPDL
     IASTGARLRE VGTTNRTHLK DYAEAIGPQT GCVLKVHQSN FRVEGFTATV TLPELRLLTA
     ERDVPLVADL GSGLLAPDPL LPDEPDAATA LSEGADVVTA SGDKLLGGPQ AGVVLGRADV
     VARMARHPLA RAVRADKLTL AALEATVRSG ISPVTRYLHA DSERLRVRAE RLAAAVGASV
     VAHDGRVGGG GAPGVPLPGW AVRLPESAAA LLRAGDPAVL PRVHDGACLL DLRCIPESDD
     DRLLAAVRKA LGADP
//
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