ID SELD_PELPD Reviewed; 348 AA. AC A1APP9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 1. DT 10-JUN-2026, entry version 92. 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=Ppro_1707; OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1). OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfuromonadia; OC Desulfuromonadales; Desulfuromonadaceae; Pelobacter. OX NCBI_TaxID=338966; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D., RA Richardson P.; RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379."; RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000482; ABK99319.1; -; Genomic_DNA. DR RefSeq; WP_011735596.1; NC_008609.1. DR AlphaFoldDB; A1APP9; -. DR SMR; A1APP9; -. DR STRING; 338966.Ppro_1707; -. DR KEGG; ppd:Ppro_1707; -. DR eggNOG; COG0709; Bacteria. DR HOGENOM; CLU_032859_0_1_7; -. DR OrthoDB; 9767928at2; -. DR Proteomes; UP000006732; 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 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..348 FT /note="Selenide, water dikinase" FT /id="PRO_1000051600" FT ACT_SITE 17 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625" FT BINDING 20 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 47..49 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 50 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625" FT BINDING 67 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 90 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 90 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625" FT BINDING 138..140 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 226 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625" FT SITE 20 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625" SQ SEQUENCE 348 AA; 36778 MW; 544231A42EC3A7E7 CRC64; MTDTTIRLTQ TVKGAGCAAK LAPGDLDRAL CGLDLPVDPN LLVGLERADD AGVYRISDDL ALVQTIDFFP PMVDDPYSFG QIAAANALSD IYAMGGVPKT AMNVVAFPAK TMDISVLRSV IEGGLDKMRE AGVVLVGGHT VEDSELKYGL SVTGFIHPDR ILTKKNLQTG DCLILTKPLG TGIVSTAIKA GLAGSDLTER VIRNMTALNR DAALVMGDFT VHACTDITGF GFLGHLAEMV VDSGCGVRII AADVPHYPEA LEWADMGLIP GGAYNNRDFR GMFVDFGAAV SRRFRDLLFD PQTSGGLLIA VAPNEAEQLV AALKATGIEC AAVVGEVVEE PLERIVVE //