ID A0A3B7A8F1_9RHOO Unreviewed; 465 AA.
AC A0A3B7A8F1;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=HYN24_00260 {ECO:0000313|EMBL:AXS78605.1};
OS Dechloromonas sp. HYN0024.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=2231055 {ECO:0000313|EMBL:AXS78605.1, ECO:0000313|Proteomes:UP000257259};
RN [1] {ECO:0000313|EMBL:AXS78605.1, ECO:0000313|Proteomes:UP000257259}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HYN0024 {ECO:0000313|EMBL:AXS78605.1,
RC ECO:0000313|Proteomes:UP000257259};
RA Kim M., Yi H.;
RT "Genome sequencing of Dechloromonas sp. HYN0024.";
RL Submitted (JUN-2018) 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; CP031842; AXS78605.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B7A8F1; -.
DR KEGG; dey:HYN24_00260; -.
DR OrthoDB; 9787096at2; -.
DR UniPathway; UPA00906; UER00896.
DR Proteomes; UP000257259; 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:UP000257259};
KW Selenium {ECO:0000256|ARBA:ARBA00023266, ECO:0000256|HAMAP-Rule:MF_00423};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00423, ECO:0000313|EMBL:AXS78605.1}.
FT DOMAIN 6..41
FT /note="L-seryl-tRNA selenium transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12390"
FT MOD_RES 291
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00423,
FT ECO:0000256|PIRSR:PIRSR618319-50"
SQ SEQUENCE 465 AA; 49552 MW; 5B87EE47B28996DF CRC64;
MNEHKRLPAV DRVLQQIPDL IDVHGRQPVT ACVRAELAAA REGLKFGLPL PDDASLLAAI
RRRAEAAGQA RLRSVFNLTG TVLHTNLGRA QLAEEAIAAM VEAARSPCPL EYDLASGGRG
DRDDLVSGLL AELIAGGSPN IAATIVNNNA AAVLLTLNAL AQGKEAVVSR GELVEIGGAF
RIPDVMRRAQ VKLHEIGTTN RTHAKDFQEA INPKTALLMK IHTSNYAVTG FTATVDEKAI
ADIAHAAGLP FVIDLGSGTL CDFAAYGLPA EPTPQQALAA GADIVTFSGD KLLGGPQAGL
IVGRKDLIAK IKKNPLKRAL RVGKTTLAAL EATLRLYRDP DRLAERLPTL RLLTRPLAEI
NALAERLLPL VQATFGELAT VSVEPCCSQI GSGALPVERL PSAALVFRVN AKRAGKMLLS
IEAAFRGLPT PVIGYIRDDA YHLDLRCLEG KDETRFTAQL PQLKL
//
