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Database: UniProt
Entry: A0A2N6U0L9_9MICO
LinkDB: A0A2N6U0L9_9MICO
Original site: A0A2N6U0L9_9MICO 
ID   A0A2N6U0L9_9MICO        Unreviewed;       453 AA.
AC   A0A2N6U0L9;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
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=CJ197_10370 {ECO:0000313|EMBL:PMC75104.1};
OS   Brachybacterium sp. UMB0905.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Brachybacterium.
OX   NCBI_TaxID=2069310 {ECO:0000313|EMBL:PMC75104.1, ECO:0000313|Proteomes:UP000235560};
RN   [1] {ECO:0000313|EMBL:PMC75104.1, ECO:0000313|Proteomes:UP000235560}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UMB0905 {ECO:0000313|EMBL:PMC75104.1,
RC   ECO:0000313|Proteomes:UP000235560};
RA   Thomas-White K., Kumar N., Forster S., Putonti C., Lawley T., Wolfe A.J.;
RT   "Bacterial strain isolated from the female urinary microbiota.";
RL   Submitted (SEP-2017) 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:PMC75104.1}.
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DR   EMBL; PNHL01000009; PMC75104.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N6U0L9; -.
DR   InParanoid; A0A2N6U0L9; -.
DR   OrthoDB; 9787096at2; -.
DR   UniPathway; UPA00906; UER00896.
DR   Proteomes; UP000235560; 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:UP000235560};
KW   Selenium {ECO:0000256|ARBA:ARBA00023266, ECO:0000256|HAMAP-Rule:MF_00423};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00423, ECO:0000313|EMBL:PMC75104.1}.
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   453 AA;  47210 MW;  D912D4B9510878C7 CRC64;
     MIVDDPRRRI PRTDQLLAHP LVVAATRTLS EKVVRGIVRA AQDRARSGHI TPEQVEAEVL
     AAVDSRSASS LRPVLNATGV IVHTNLGRAP LSDPARQALA DAAGYTDVEF DLATGARGRR
     GAGARAALLA ACPAAEDALV VNNGAGALLL ACTALVGTGE VIVSRGELIE IGAGFRLPDL
     IQSAGTHLRE VGTTNRTHLQ DYRDAIGADT RAILTIHTSN YRVIGFTAAQ GPAELAPLAR
     EHDLPLIADL GSGLLAPDPV LREEPDATTA LEAGADLVIA SGDKLLGGPQ AGVLLGKAEV
     IARLSRHPLA RAVRADKLTL AAIEATLTGP EPPVLAALHT RAEDLRQRTE AFAERLRQQA
     PGLEVEVLEH DGRTGGGGGA EVPLPGWALH LPAALTGVLR TPSDPELVPV VATTREDVCV
     VDLRCIPAAA EDQLLAALCG AAAEIERMGE GRR
//
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