ID SELD_PHOPR Reviewed; 346 AA. AC Q6LP05; DT 04-JAN-2005, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 10-JUN-2026, entry version 108. DE RecName: Full=Selenide, water dikinase {ECO:0000255|HAMAP-Rule:MF_00625}; DE EC=2.7.9.3 {ECO:0000255|HAMAP-Rule:MF_00625}; DE AltName: Full=Selenium donor protein {ECO:0000255|HAMAP-Rule:MF_00625}; DE AltName: Full=Selenophosphate synthase {ECO:0000255|HAMAP-Rule:MF_00625}; GN Name=selD {ECO:0000255|HAMAP-Rule:MF_00625}; GN OrderedLocusNames=PBPRA2592; OS Photobacterium profundum (strain SS9). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Photobacterium. OX NCBI_TaxID=298386; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1253 / SS9; RX PubMed=15746425; DOI=10.1126/science.1103341; RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M., RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C., RA Bartlett D.H., Valle G.; RT "Life at depth: Photobacterium profundum genome sequence and expression RT analysis."; RL Science 307:1459-1461(2005). CC -!- FUNCTION: Synthesizes selenophosphate from selenide and ATP. CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00625}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00625}; CC Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000255|HAMAP-Rule:MF_00625}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00625}. CC -!- SIMILARITY: Belongs to the selenophosphate synthase 1 family. Class I CC subfamily. {ECO:0000255|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; CR378671; CAG20971.1; -; Genomic_DNA. DR AlphaFoldDB; Q6LP05; -. DR SMR; Q6LP05; -. DR STRING; 298386.PBPRA2592; -. DR KEGG; ppr:PBPRA2592; -. DR eggNOG; COG0709; Bacteria. DR HOGENOM; CLU_032859_0_1_6; -. DR Proteomes; UP000000593; Chromosome 1. 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 FunFam; 3.30.1330.10:FF:000003; Selenide, water dikinase; 1. DR FunFam; 3.90.650.10:FF:000004; Selenide, water dikinase; 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; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Reference proteome; Selenium; Transferase. FT CHAIN 1..346 FT /note="Selenide, water dikinase" FT /id="PRO_0000127630" FT ACT_SITE 15 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625" FT BINDING 18 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:0000255|HAMAP-Rule:MF_00625" FT BINDING 46..48 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:0000255|HAMAP-Rule:MF_00625" FT BINDING 49 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625" FT BINDING 66 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:0000255|HAMAP-Rule:MF_00625" FT BINDING 89 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:0000255|HAMAP-Rule:MF_00625" FT BINDING 89 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625" FT BINDING 137..139 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625" FT BINDING 225 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625" FT SITE 18 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625" SQ SEQUENCE 346 AA; 36846 MW; 30533C0F6D69FE6A CRC64; MENVRLTQYS HGAGCGCKIS PQVLDTILRT QLAPFSDPNL LVGNESKDDA AVYDLGNGTA AISTTDFFMP IVDDPFDFGR IAATNAISDI YAMGGKPIMA IAILGWPVNV LAPEIAQQVI EGGRSVCREA GISLAGGHSI DAPEPIFGLA VTGIVDTDRV KRNNRAENGC KLYLTKPLGI GVLTTAEKQS KLADEHKGLA RDWMCKLNIP GQDFANVEGV KAMTDVTGFG LMGHLSEICE GSQLKARVDF DSVPYLPGVF DYIAQGCVPG GTTRNFDSYG QKLGAMTEQQ KALLCDPQTS GGLLIAVTPD AETEQQLQAI AARHNIELQA IGEMMPLDGD TLIEIC //