UniProt: A0A3Q9HQP8

Database: UniProt
Entry: A0A3Q9HQP8_9FIRM

LinkDB:  A0A3Q9HQP8_9FIRM 
Original site:  A0A3Q9HQP8_9FIRM

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (7)   
   InterPro (5)   
   Pfam (2)   
All databases (13)   

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ID   A0A3Q9HQP8_9FIRM        Unreviewed;       465 AA.
AC   A0A3Q9HQP8;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-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=BBF96_07340 {ECO:0000313|EMBL:AZR73213.1};
OS   Anoxybacter fermentans.
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Anoxybacter.
OX   NCBI_TaxID=1323375 {ECO:0000313|EMBL:AZR73213.1, ECO:0000313|Proteomes:UP000267250};
RN   [1] {ECO:0000313|EMBL:AZR73213.1, ECO:0000313|Proteomes:UP000267250}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DY22613 {ECO:0000313|EMBL:AZR73213.1,
RC   ECO:0000313|Proteomes:UP000267250};
RA   Zeng X., Shao Z.;
RT   "Genome and transcriptome analysis of iron-reducing fermentative bacteria
RT   Anoxybacter fermentans.";
RL   Submitted (JUL-2016) 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; CP016379; AZR73213.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3Q9HQP8; -.
DR   KEGG; aft:BBF96_07340; -.
DR   OrthoDB; 9787096at2; -.
DR   UniPathway; UPA00906; UER00896.
DR   Proteomes; UP000267250; 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:UP000267250};
KW   Selenium {ECO:0000256|ARBA:ARBA00023266, ECO:0000256|HAMAP-Rule:MF_00423};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   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         296
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00423,
FT                   ECO:0000256|PIRSR:PIRSR618319-50"
SQ   SEQUENCE   465 AA;  52081 MW;  C615D3EC119EF9F1 CRC64;
     MKQEYLRKIP AVNRLLQTTE IQNILTEYPH DLVVDLINQV LDKKRRDILE ETTDPEKLDL
     SIEGLAREAK EAILAYMAPR LKKVINATGT VLHTNLGRAV LSEKAADALA QIARTYSNLE
     YDLKEGKRGS RYTLVTDLLC RLTGAEDALV VNNNAAAVLL VLSTLAKGKE VIISRGELVE
     IGGSFRMHEV MKISGCTLVE VGSTNKTHLY DYENAITSET GLLVKVHTSN YQIVGFSKSV
     ENKELVELAH KYQIPVFEDL GSGVLINLEK YGIAHEPTVQ EAVSHGVDLV SFSGDKLLGG
     PQAGIIVGKK EYIQRLKRNH LLRALRVDKF TLAALEVTLK HYLREEEAMN EIPTLRMLKL
     TADVIKKRVE KFAQRLKETL NEVEIRVVEG RSMVGGGSLP LEEIPTWLVG VKFNRISTTD
     AEIQLRQGEV PVICRIQDDE LLFDLRTVFP DQEDEILEAL LKVNR
//

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