ID F3YTQ6_DESAF Unreviewed; 477 AA.
AC F3YTQ6;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 69.
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=Desaf_0074 {ECO:0000313|EMBL:EGJ48437.1};
OS Desulfocurvibacter africanus subsp. africanus str. Walvis Bay.
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfocurvibacter.
OX NCBI_TaxID=690850 {ECO:0000313|EMBL:EGJ48437.1, ECO:0000313|Proteomes:UP000007844};
RN [1] {ECO:0000313|EMBL:EGJ48437.1, ECO:0000313|Proteomes:UP000007844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Walvis Bay {ECO:0000313|EMBL:EGJ48437.1,
RC ECO:0000313|Proteomes:UP000007844};
RX PubMed=21642452; DOI=10.1128/JB.05223-11;
RA Brown S.D., Wall J.D., Kucken A.M., Gilmour C.C., Podar M., Brandt C.C.,
RA Teshima H., Detter J.C., Han C.S., Land M.L., Lucas S., Han J.,
RA Pennacchio L., Nolan M., Pitluck S., Woyke T., Goodwin L., Palumbo A.V.,
RA Elias D.A.;
RT "Genome sequence of the mercury-methylating and pleomorphic Desulfovibrio
RT africanus Strain Walvis Bay.";
RL J. Bacteriol. 193:4037-4038(2011).
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; CP003221; EGJ48437.1; -; Genomic_DNA.
DR RefSeq; WP_014258313.1; NC_016629.1.
DR AlphaFoldDB; F3YTQ6; -.
DR STRING; 690850.Desaf_0074; -.
DR KEGG; daf:Desaf_0074; -.
DR eggNOG; COG1921; Bacteria.
DR HOGENOM; CLU_038142_1_0_7; -.
DR UniPathway; UPA00906; UER00896.
DR Proteomes; UP000007844; 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:UP000007844};
KW Selenium {ECO:0000256|ARBA:ARBA00023266, ECO:0000256|HAMAP-Rule:MF_00423};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00423, ECO:0000313|EMBL:EGJ48437.1}.
FT DOMAIN 5..44
FT /note="L-seryl-tRNA selenium transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12390"
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 477 AA; 52617 MW; 6AFBDAF53366FC2E CRC64;
MPNLFRLLPP VDQALHRLAG EPELAAMPRP LLRDLVNKFL DLCREEIKAG VIASEEQLVS
DTFFRRMTCF VRSQSRPHFR RVLNATGVVI HTNLGRSLLA ESAIEAVTEA CRNYSNLEFN
LDTGKRGSRY SHVEELLCRL TGAEAALVVN NNASAVLLCL ETLAKGRETI VSRGQLVEIG
GSFRIPDVMA RSGSILVEVG ATNRTHPRDY ENAINENTAL LLRVHTSNYR MIGFTRETTA
EELVEIGRRR NIPVMEDLGS GCFFDLRPMG FQFEPMVQDV VASGADVVTF SGDKVLGGPQ
AGIIVGRREY IEKIKRNPIN RAMRIDKMTL AALEATLRLY LDPELARREI PTIAMITAEP
DELKKKAQAL ARLLKRDLSG RLDIATRPGV SRVGGGSFPE RDLPTTVVTV KPTSGGAQAL
ETLKDNLRTA EPPLIGYIEE DAFCLDPRTL RNDEFRLVSA SLAQALDMAG DGSACHN
//
