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Database: UniProt
Entry: A0YH50_9GAMM
LinkDB: A0YH50_9GAMM
Original site: A0YH50_9GAMM 
ID   A0YH50_9GAMM            Unreviewed;       494 AA.
AC   A0YH50;
DT   23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT   23-JAN-2007, sequence version 1.
DT   24-JAN-2024, entry version 79.
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=GP2143_12019 {ECO:0000313|EMBL:EAW29818.1};
OS   marine gamma proteobacterium HTCC2143.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC   Spongiibacteraceae; BD1-7 clade.
OX   NCBI_TaxID=247633 {ECO:0000313|EMBL:EAW29818.1, ECO:0000313|Proteomes:UP000004931};
RN   [1] {ECO:0000313|EMBL:EAW29818.1, ECO:0000313|Proteomes:UP000004931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTCC2143 {ECO:0000313|EMBL:EAW29818.1,
RC   ECO:0000313|Proteomes:UP000004931};
RX   PubMed=20601481; DOI=10.1128/JB.00683-10;
RA   Oh H.M., Kang I., Ferriera S., Giovannoni S.J., Cho J.C.;
RT   "Genome sequence of the oligotrophic marine Gammaproteobacterium HTCC2143,
RT   isolated from the Oregon Coast.";
RL   J. Bacteriol. 192:4530-4531(2010).
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:EAW29818.1}.
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DR   EMBL; AAVT01000014; EAW29818.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0YH50; -.
DR   STRING; 247633.GP2143_12019; -.
DR   eggNOG; COG1921; Bacteria.
DR   UniPathway; UPA00906; UER00896.
DR   Proteomes; UP000004931; 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:UP000004931};
KW   Selenium {ECO:0000256|ARBA:ARBA00023266, ECO:0000256|HAMAP-Rule:MF_00423};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00423, ECO:0000313|EMBL:EAW29818.1}.
FT   DOMAIN          23..62
FT                   /note="L-seryl-tRNA selenium transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12390"
FT   MOD_RES         312
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00423,
FT                   ECO:0000256|PIRSR:PIRSR618319-50"
SQ   SEQUENCE   494 AA;  53524 MW;  25E118D01C0FF7F0 CRC64;
     MILPITLTSE YAHPMTHSPN TFFSKLPSVD SILSDPTIKI VAEKYGHTAV TKSVRIALQA
     GRNNHDTFSP SISRQELAQL IVNATVLDLE KINRYSLTPV FNLSGTVLHT NLGRASLPNE
     AVEAMIAAAK SPTNLEYDLA TGKRGSRDSH VESLLCELTG AEAATVVNNN AAAVLIALNS
     LALRKEVIVS RGELIEIGGA FRIPEIMTRA GAKLREVGTT NRTHRRDYEE AISPRTGLLM
     KVHTSNYRVE GFTAAVDEKA LAVLGREHGV PLMIDLGSGT LTELTDYGLP HEPMAGESVA
     SGANLVTFSG DKLLGGPQAG LIVGDRALIE KIKRNPMTRA LRVDKVRLAA LEAVLRLYLM
     PDKLGQRLPV LRTLTRPIAD ILQTAETIAA GLREYLPKDL DITIVEGVSA IGSGSLPGEE
     LITKVVMLCP TGNKKDNAKR VRLLDKGFRS LATPVIGRVS NGNLMLDMRC LDDTDDFIKQ
     LDQLSHLIDS KTRQ
//
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