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Database: UniProt
Entry: A0A161YI73_9CLOT
LinkDB: A0A161YI73_9CLOT
Original site: A0A161YI73_9CLOT 
ID   A0A161YI73_9CLOT        Unreviewed;       463 AA.
AC   A0A161YI73;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 33.
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   ECO:0000313|EMBL:KZL90022.1};
GN   ORFNames=CLMAG_45060 {ECO:0000313|EMBL:KZL90022.1};
OS   Clostridium magnum DSM 2767.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1121326 {ECO:0000313|EMBL:KZL90022.1, ECO:0000313|Proteomes:UP000076603};
RN   [1] {ECO:0000313|EMBL:KZL90022.1, ECO:0000313|Proteomes:UP000076603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2767 {ECO:0000313|EMBL:KZL90022.1,
RC   ECO:0000313|Proteomes:UP000076603};
RA   Poehlein A., Uhlig R., Fischer R., Bahl H., Daniel R.;
RT   "Genome sequence of Clostridium magnum DSM 2767.";
RL   Submitted (APR-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:KZL90022.1}.
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DR   EMBL; LWAE01000006; KZL90022.1; -; Genomic_DNA.
DR   RefSeq; WP_066627298.1; NZ_LWAE01000006.1.
DR   AlphaFoldDB; A0A161YI73; -.
DR   STRING; 1121326.CLMAG_45060; -.
DR   PATRIC; fig|1121326.3.peg.4569; -.
DR   OrthoDB; 9787096at2; -.
DR   UniPathway; UPA00906; UER00896.
DR   Proteomes; UP000076603; 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:UP000076603};
KW   Selenium {ECO:0000256|ARBA:ARBA00023266, ECO:0000256|HAMAP-Rule:MF_00423};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00423}.
FT   DOMAIN          7..46
FT                   /note="L-seryl-tRNA selenium transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12390"
FT   MOD_RES         293
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00423,
FT                   ECO:0000256|PIRSR:PIRSR618319-50"
SQ   SEQUENCE   463 AA;  52179 MW;  46EED177AE111763 CRC64;
     MEKKKLLRKL PKIDELLKEE EIKSELENTA RALVIDALRT SIDNYRVLIL NDSIENFKKE
     DILKDFKNII EENKGSNFKK VINAAGVVIH TNLGRSLLAK KALENVINVS DNYNNLEYDL
     KKGQRGSRYS HVEELIRKVT GAEAAVVVNN NAAAVMLVLN TLCKDKEAVV SRGQLVEIGG
     SFRVPDVMTF SGAKLVEVGT TNRTHLYDYE NNINEFTGVL LKVHTSNFKI LGFTEDVSLE
     ELVELGAKSN IPVVEDIGSG TLVDFSKYGF TYEPTVQESI KKGVDVVTFS GDKMLGGPQA
     GIIAGKKEYI NKMKKNQLTR ALRIDKMTLA ALEGTLKYYL DEKEAVENIP TLYAILSDKS
     EHKKRAQRLK RKLQSKVKGF QFIIAEDYSM VGGGSMPVEK IETYVIRVKN DKFSPKELEK
     ELRENKIPII IRVANDEVIM DLRTMFDKDF DDVVDAFIIL SER
//
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