ID Q6APM6_DESPS Unreviewed; 308 AA. AC Q6APM6; DT 13-SEP-2004, integrated into UniProtKB/TrEMBL. DT 13-SEP-2004, sequence version 1. DT 10-JUN-2026, entry version 130. DE RecName: Full=Selenide, water dikinase {ECO:0000256|HAMAP-Rule:MF_00625}; DE EC=2.7.9.3 {ECO:0000256|HAMAP-Rule:MF_00625}; DE AltName: Full=Selenium donor protein {ECO:0000256|HAMAP-Rule:MF_00625}; DE AltName: Full=Selenophosphate synthase {ECO:0000256|HAMAP-Rule:MF_00625}; GN Name=selD {ECO:0000256|HAMAP-Rule:MF_00625}; GN OrderedLocusNames=DP0969 {ECO:0000313|EMBL:CAG35698.1}; OS Desulfotalea psychrophila (strain LSv54 / DSM 12343). OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfobulbia; OC Desulfobulbales; Desulfocapsaceae; Desulfotalea. OX NCBI_TaxID=177439 {ECO:0000313|EMBL:CAG35698.1, ECO:0000313|Proteomes:UP000000602}; RN [1] {ECO:0000313|Proteomes:UP000000602} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 12343 / LSv54 {ECO:0000313|Proteomes:UP000000602}; RX PubMed=15305914; DOI=10.1111/j.1462-2920.2004.00665.x; RA Rabus R., Ruepp A., Frickey T., Rattei T., Fartmann B., Stark M., Bauer M., RA Zibat A., Lombardot T., Becker I., Amann J., Gellner K., Teeling H., RA Leuschner W.D., Gloeckner F.-O., Lupas A.N., Amann R., Klenk H.-P.; RT "The genome of Desulfotalea psychrophila, a sulfate-reducing bacterium from RT permanently cold Arctic sediments."; RL Environ. Microbiol. 6:887-902(2004). CC -!- FUNCTION: Synthesizes selenophosphate from selenide and ATP. CC {ECO:0000256|HAMAP-Rule:MF_00625}. CC -!- CATALYTIC ACTIVITY: CC Reaction=hydrogenselenide + ATP + H2O = selenophosphate + AMP + CC phosphate + 2 H(+); Xref=Rhea:RHEA:18737, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16144, ChEBI:CHEBI:29317, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456215; EC=2.7.9.3; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00625}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00625}; CC Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000256|HAMAP-Rule:MF_00625}; CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00625}. CC -!- SIMILARITY: Belongs to the selenophosphate synthase 1 family. Class I CC subfamily. {ECO:0000256|ARBA:ARBA00008026, ECO:0000256|HAMAP- CC Rule:MF_00625}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00625}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CR522870; CAG35698.1; -; Genomic_DNA. DR AlphaFoldDB; Q6APM6; -. DR STRING; 177439.DP0969; -. DR KEGG; dps:DP0969; -. DR eggNOG; COG0709; Bacteria. DR HOGENOM; CLU_032859_0_1_7; -. DR Proteomes; UP000000602; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0004756; F:selenide, water dikinase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016260; P:L-selenocysteine biosynthetic process; IEA:InterPro. DR CDD; cd02195; SelD; 1. DR Gene3D; 3.90.650.10; PurM-like C-terminal domain; 1. DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 1. DR HAMAP; MF_00625; SelD; 1. DR InterPro; IPR010918; PurM-like_C_dom. DR InterPro; IPR036676; PurM-like_C_sf. DR InterPro; IPR016188; PurM-like_N. DR InterPro; IPR036921; PurM-like_N_sf. DR InterPro; IPR023061; SelD_I. DR InterPro; IPR004536; SPS/SelD. DR NCBIfam; NF002098; PRK00943.1; 1. DR NCBIfam; TIGR00476; selD; 1. DR PANTHER; PTHR10256:SF0; INACTIVE SELENIDE, WATER DIKINASE-LIKE PROTEIN-RELATED; 1. DR PANTHER; PTHR10256; SELENIDE, WATER DIKINASE; 1. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR PIRSF; PIRSF036407; Selenphspht_syn; 1. DR SUPFAM; SSF56042; PurM C-terminal domain-like; 1. DR SUPFAM; SSF55326; PurM N-terminal domain-like; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00625}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00625}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00625}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00625}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00625}; Reference proteome {ECO:0000313|Proteomes:UP000000602}; KW Selenium {ECO:0000256|ARBA:ARBA00023266, ECO:0000256|HAMAP-Rule:MF_00625}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00625}. FT DOMAIN 9..116 FT /note="PurM-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF00586" FT DOMAIN 129..303 FT /note="PurM-like C-terminal" FT /evidence="ECO:0000259|Pfam:PF02769" FT BINDING 7..9 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625" FT BINDING 10 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625" FT BINDING 27 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625" FT BINDING 50 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625" FT BINDING 50 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625" FT BINDING 98..100 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625" FT BINDING 186 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625" SQ SEQUENCE 308 AA; 33166 MW; 7F6F64BDBCC3BAEE CRC64; MLVGMATADD AGVYKVSDEL ALIQTLDFFT PIVDDPYDFG RIAAANALSD VYAMGGVPQT AMNIVAYPMK TLGREPLREM LAGGSAMLRE ANTVLLGGHS VEDEELKYGL SVTGFVHPDK ILANQGLRTG DVLILTKAIG TGILNTAIKA RLASKETIEE LTELMVTLNK KPAEIMREFN ISACTDITGF GLLGHIAEMI DGSDKSITIQ SQNVPILNQA HHFASMGLVP IGAHNNRAFR KEMMQIPKAF DPVLRDILFD PQTSGGLLIG CAEEDGPSLV RRLQDAGVKD AQIIGFVTEN RANIIQIS //