ID A6VLH1_ACTSZ Unreviewed; 476 AA.
AC A6VLH1;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 98.
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 OrderedLocusNames=Asuc_0441 {ECO:0000313|EMBL:ABR73818.1};
OS Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 /
OS 130Z).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Actinobacillus.
OX NCBI_TaxID=339671 {ECO:0000313|EMBL:ABR73818.1, ECO:0000313|Proteomes:UP000001114};
RN [1] {ECO:0000313|Proteomes:UP000001114}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z
RC {ECO:0000313|Proteomes:UP000001114};
RX PubMed=21118570; DOI=10.1186/1471-2164-11-680;
RA McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A.,
RA Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L.,
RA Burkhart K.B., Harkins V., Vieille C.;
RT "A genomic perspective on the potential of Actinobacillus succinogenes for
RT industrial succinate production.";
RL BMC Genomics 11:680-680(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}.
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DR EMBL; CP000746; ABR73818.1; -; Genomic_DNA.
DR AlphaFoldDB; A6VLH1; -.
DR STRING; 339671.Asuc_0441; -.
DR KEGG; asu:Asuc_0441; -.
DR eggNOG; COG1921; Bacteria.
DR HOGENOM; CLU_038142_1_0_6; -.
DR UniPathway; UPA00906; UER00896.
DR Proteomes; UP000001114; 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:UP000001114};
KW Selenium {ECO:0000256|ARBA:ARBA00023266, ECO:0000256|HAMAP-Rule:MF_00423};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00423, ECO:0000313|EMBL:ABR73818.1}.
FT DOMAIN 19..58
FT /note="L-seryl-tRNA selenium transferase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF12390"
FT MOD_RES 308
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00423,
FT ECO:0000256|PIRSR:PIRSR618319-50"
SQ SEQUENCE 476 AA; 52618 MW; E3B3E916803E1ECE CRC64;
MYNAISILSK KGQKMTALFQ QLPSVNKLIN APQGQRLMIK FGHMAVVRVC RALLRQSREF
IRENRQLPDF LLQDNAVFAE IERRLQQQTQ VRIKSVHNLT GTVLHTNLGR ALWAESAQQA
ALTAMHDNVA LEYDLDAGKR GHRDNYISEL IRQLTGAEAA CVVNNNAAAV LLILAAFARG
KEVVISRGEL IEIGGAFRIP DIMAQAGCKL VEVGTTNRTH LQDYRNAINE NTAFLMKVHS
SNYQICGFTG EVSEQELAAL GKEFGIPVIS DLGSGALTDL SQYNLPKEPT VQEKLAQGVD
LISFSGDKLL GGPQAGIIAG KKELILQLQS HPLKRVLRCD KVILAGLEAT LRLYLQPEKL
AEKLTSLYLL TQPIEQLQQQ AVQLKTKLEN MLKNEFSLQI EASSAQIGSG SQPMARIPSV
AVTVAEKNSQ KLTALLTRFK QLSSPIIARV ENNKIWLDLR SLASFEKLLI TLDELK
//
