ID A6TQL0_ALKMQ Unreviewed; 319 AA. AC A6TQL0; DT 21-AUG-2007, integrated into UniProtKB/TrEMBL. DT 21-AUG-2007, sequence version 1. DT 10-JUN-2026, entry version 104. 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=Amet_2321 {ECO:0000313|EMBL:ABR48478.1}; OS Alkaliphilus metalliredigens (strain QYMF). OC Bacteria; Bacillati; Bacillota; Clostridia; Peptostreptococcales; OC Natronincolaceae; Alkaliphilus. OX NCBI_TaxID=293826 {ECO:0000313|EMBL:ABR48478.1, ECO:0000313|Proteomes:UP000001572}; RN [1] {ECO:0000313|Proteomes:UP000001572} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=QYMF {ECO:0000313|Proteomes:UP000001572}; RX PubMed=27811105; DOI=10.1128/genomea.01226-16; RA Hwang C., 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 Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., RA Land M.L., Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J., RA Richardson P., Fields M.W.; RT "Complete genome sequence of Alkaliphilus metalliredigens strain QYMF, an RT alkaliphilic and metal-reducing bacterium isolated from borax-contaminated RT leachate ponds."; RL Genome Announc. 4:0-0(2016). 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; CP000724; ABR48478.1; -; Genomic_DNA. DR AlphaFoldDB; A6TQL0; -. DR STRING; 293826.Amet_2321; -. DR KEGG; amt:Amet_2321; -. DR eggNOG; COG0709; Bacteria. DR HOGENOM; CLU_032859_0_1_9; -. DR Proteomes; UP000001572; 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 {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:UP000001572}; 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 21..127 FT /note="PurM-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF00586" FT DOMAIN 139..318 FT /note="PurM-like C-terminal" FT /evidence="ECO:0000259|Pfam:PF02769" FT BINDING 19..21 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 22 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625" FT BINDING 39 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 62 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625" FT BINDING 62 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 109..111 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 197 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625" SQ SEQUENCE 319 AA; 34786 MW; A040604081395B77 CRC64; MLCHIPRIKD EKLIVGLETS DDAAVYQIDE ERALVQTLDF FTPVVDDPYT YGQIAAANSL SDVYAMGGQP LTAMNIVCFP SCLSPDVLKE ILKGGADKIM EANCLLVGGH TVEDNEPKYG LSVTGMVSPH EIWTNAGAKV GEYLILTKPI GTGVLNTAIK VDMVDESQYE DAVKVMVTLN KYGMEALKDF NISACTDITG FGLLGHAYEM AKGSHVSLEI YSDQVPFIAG VKEFARMGII PGGMYANKKH IEKDVNVNGD VEEVIMDLLY DPQTSGGLLV SIAEEQVEEA IEKLTELNLT EFAVIGKVVE KDEFTIYIK //