ID D4M964_9BACT Unreviewed; 477 AA.
AC D4M964;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 65.
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=SY1_12870 {ECO:0000313|EMBL:CBL28409.1};
OS Fretibacterium fastidiosum.
OC Bacteria; Synergistota; Synergistia; Synergistales; Aminobacteriaceae;
OC Fretibacterium.
OX NCBI_TaxID=651822 {ECO:0000313|EMBL:CBL28409.1, ECO:0000313|Proteomes:UP000008957};
RN [1] {ECO:0000313|EMBL:CBL28409.1, ECO:0000313|Proteomes:UP000008957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGP1 {ECO:0000313|EMBL:CBL28409.1,
RC ECO:0000313|Proteomes:UP000008957};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Wade W., Vartoukian S.;
RT "The genome sequence of Synergistetes sp. SGP1.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBL28409.1, ECO:0000313|Proteomes:UP000008957}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SGP1 {ECO:0000313|EMBL:CBL28409.1,
RC ECO:0000313|Proteomes:UP000008957};
RA Pajon A.;
RL Submitted (MAR-2010) 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}.
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DR EMBL; FP929056; CBL28409.1; -; Genomic_DNA.
DR AlphaFoldDB; D4M964; -.
DR KEGG; sbr:SY1_12870; -.
DR PATRIC; fig|651822.3.peg.520; -.
DR HOGENOM; CLU_038142_1_0_0; -.
DR UniPathway; UPA00906; UER00896.
DR Proteomes; UP000008957; Chromosome.
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:UP000008957};
KW Selenium {ECO:0000256|ARBA:ARBA00023266, ECO:0000256|HAMAP-Rule:MF_00423};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00423, ECO:0000313|EMBL:CBL28409.1}.
FT DOMAIN 10..49
FT /note="L-seryl-tRNA selenium transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12390"
FT MOD_RES 296
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00423,
FT ECO:0000256|PIRSR:PIRSR618319-50"
SQ SEQUENCE 477 AA; 51039 MW; A411EA9585A51836 CRC64;
MTVEDIKQKL RAIPGMDVLL AQDWARPWIE RAGRETVKRV INGELTAVRR RMLTGQEEDV
SPERIREACL GALTEAERPN LRRVVNATGV VIHTNLGRSL MAAEAVRAME RAARGYSNLE
YNLAQGVRGQ RNVHVEGLVC DLTGAEAALV VNNNAGAVLL CLIALARGRE VVVSRGELVE
IGGSFRVPDI MEFSGAKLVE VGTTNRTHIE DYRAGLGENT AMLLKVHPSN FRIEGFTAAP
ERKDLAALAH ERGVVFMEDA GSGLLVDGEL LGLRGEMDVR TSLQQGVDLI TFSGDKMLGG
PQIGVIAGRR AVVNGLRKHP ILRTLRVDKI TLSAFEATLR LYRRGALDDI PTPAMIRIPA
ETLRERAEGL AAALKGRVAA QVEVVSVEDA VGGGSYPEKP LAGWGVAVSG HPAGGAGRLQ
ALLREGERPV IAGARDDALV LHVRTLQPGD EEVVVNALAA LQPEAGPLAG KGECACE
//
