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Database: UniProt
Entry: A0A0Q9KPX6_9MICO
LinkDB: A0A0Q9KPX6_9MICO
Original site: A0A0Q9KPX6_9MICO 
ID   A0A0Q9KPX6_9MICO        Unreviewed;       446 AA.
AC   A0A0Q9KPX6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
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=ASG73_02600 {ECO:0000313|EMBL:KRE39247.1};
OS   Janibacter sp. Soil728.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Janibacter.
OX   NCBI_TaxID=1736393 {ECO:0000313|EMBL:KRE39247.1, ECO:0000313|Proteomes:UP000051572};
RN   [1] {ECO:0000313|EMBL:KRE39247.1, ECO:0000313|Proteomes:UP000051572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil728 {ECO:0000313|EMBL:KRE39247.1,
RC   ECO:0000313|Proteomes:UP000051572};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRE39247.1, ECO:0000313|Proteomes:UP000051572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Soil728 {ECO:0000313|EMBL:KRE39247.1,
RC   ECO:0000313|Proteomes:UP000051572};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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}.
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:KRE39247.1}.
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DR   EMBL; LMRZ01000001; KRE39247.1; -; Genomic_DNA.
DR   RefSeq; WP_055990310.1; NZ_LMRZ01000001.1.
DR   AlphaFoldDB; A0A0Q9KPX6; -.
DR   STRING; 1736393.ASG73_02600; -.
DR   OrthoDB; 9787096at2; -.
DR   UniPathway; UPA00906; UER00896.
DR   Proteomes; UP000051572; 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   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}.
FT   DOMAIN          6..45
FT                   /note="L-seryl-tRNA selenium transferase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF12390"
FT   MOD_RES         284
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00423,
FT                   ECO:0000256|PIRSR:PIRSR618319-50"
SQ   SEQUENCE   446 AA;  45971 MW;  5CD97B4CD7551282 CRC64;
     MSEDPRRAIP RTDDVLGQAP FVTAAARLGR SVVRTAVVAA QQRARDEEIA PDRVVEAALA
     ALPTRTSSLT PVLNATGVVV HTNIGRAPLS PSAIEAVVDA AGYVDVEMDL ATGARSRRGA
     GALAALLEAV PDASGALAVN NGAAALVLAT TALAAGREVV VSRGEMVEIG DGFRLPDLIA
     STGARLREVG TTNRTHLRDY ADAIGPETGC VLKVHPSNFR VDGFVTSVGL EELRGLTRPD
     GSSVPVVADI GSGLLAPDPL LPDEPDARTW LRAGATIITA SGDKLLGGPQ AGLVLGDAEV
     VDQLRRHPLQ RAVRVDKLTL AALEATLRGP ASPVTASLHA SADDLRLRVD ALGTAVGREV
     VPVEGRVGGG GAPGVPLPGW AVEIPIDAVE RLRQPAGDLP VVLARVDRGR GLVDLRCIPA
     DRDGDVEAAL RAVLGHDDAL HPLPSP
//
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