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Database: UniProt
Entry: C5S404_9PAST
LinkDB: C5S404_9PAST
Original site: C5S404_9PAST 
ID   C5S404_9PAST            Unreviewed;       462 AA.
AC   C5S404;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 75.
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=AM305_02055 {ECO:0000313|EMBL:EER46368.1};
OS   Actinobacillus minor NM305.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=637911 {ECO:0000313|EMBL:EER46368.1, ECO:0000313|Proteomes:UP000005532};
RN   [1] {ECO:0000313|EMBL:EER46368.1, ECO:0000313|Proteomes:UP000005532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NM305 {ECO:0000313|EMBL:EER46368.1,
RC   ECO:0000313|Proteomes:UP000005532};
RX   PubMed=19819087; DOI=10.1016/j.vetmic.2009.09.030;
RA   Arya G., Niven D.F.;
RT   "Production of haemolysins by strains of the Actinobacillus
RT   minor/"porcitonsillarum" complex.";
RL   Vet. Microbiol. 141:332-341(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:EER46368.1}.
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DR   EMBL; ACQL01000118; EER46368.1; -; Genomic_DNA.
DR   RefSeq; WP_005825319.1; NZ_ACQL01000118.1.
DR   AlphaFoldDB; C5S404; -.
DR   eggNOG; COG1921; Bacteria.
DR   OrthoDB; 9787096at2; -.
DR   UniPathway; UPA00906; UER00896.
DR   Proteomes; UP000005532; 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   Coiled coil {ECO:0000256|SAM:Coils};
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, ECO:0000313|EMBL:EER46368.1}.
FT   DOMAIN          5..44
FT                   /note="L-seryl-tRNA selenium transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12390"
FT   COILED          353..380
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         294
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00423,
FT                   ECO:0000256|PIRSR:PIRSR618319-50"
SQ   SEQUENCE   462 AA;  51361 MW;  A23226E32FF472FD CRC64;
     MQMLFRQIPS LDRLLKQPQA VEFIEKFGYS AVVKTLRLLL EQARTTIQQT QTLPSFLADE
     TALFTQLEHQ LTQSQKVELR TVFNMTGTVL HTNLGRGLWS EKAVEAATNA MRNNVALEFD
     IDAGKRSHRD LYISQLLQQL TGAEAACIVN NNAAAVLLML ATFAKDKEVI VSRGELVEIG
     GAFRIPDIMA QAGCKLVEVG TTNRTHLKDY HNAINENTAF LMKVHTSNYQ IQGFTASVSE
     EELVELGQAF QLPVISDLGS GSLTDMKLLN LPAEPMVQQK VAAGVDLVSF SCDKLLGGPQ
     AGIIVGKKAF IDQLQSHPLK RVLRCDKVIL SALEATLRHY LFPEHLCQDL PTLHLLTQSL
     DSLQEKAERL RNTLSKRLDS RYILQIEASQ AQIGSGALPT ERLPSLALTI TSEKQSDLLA
     LEKKFKSLPC PIIGRFSEQK FWLDLRSVAQ FDQLIEMLSL NP
//
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