ID A0A1G7YY67_9BACI Unreviewed; 320 AA.
AC A0A1G7YY67;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 08-OCT-2025, entry version 25.
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 ORFNames=SAMN05192534_101324 {ECO:0000313|EMBL:SDH01502.1};
OS Alteribacillus persepolensis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Alteribacillus.
OX NCBI_TaxID=568899 {ECO:0000313|EMBL:SDH01502.1, ECO:0000313|Proteomes:UP000199163};
RN [1] {ECO:0000313|EMBL:SDH01502.1, ECO:0000313|Proteomes:UP000199163}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21632 {ECO:0000313|EMBL:SDH01502.1,
RC ECO:0000313|Proteomes:UP000199163};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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;
CC Evidence={ECO:0000256|HAMAP-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}.
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DR EMBL; FNDK01000001; SDH01502.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7YY67; -.
DR STRING; 568899.SAMN05192534_101324; -.
DR Proteomes; UP000199163; Unassembled WGS sequence.
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: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:UP000199163};
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..128
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 140..317
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 110..112
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 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625"
SQ SEQUENCE 320 AA; 34032 MW; 219331684677D432 CRC64;
MRHLPERETN PNLLVGMDTS DDGGVYKLTD DIALVQSVDY FTPVVDDPYM FGQIAAANAL
SDIYAMGGKP TTVLNIVGFP IKELPDYLLA GMMKGAADKV EESGATIVGG HSIDDQEPKF
GLAATGIVHP EKVWANKGAE PGDVLVLTKP LGVGILTTAI KRQKATAAQE EAVTKTMAKL
NKAAAETLMD YQPHAVTDVT GFGLIGHSFE MAEASNVTFT FDTASIPLLD GARSLAEQGI
VPGGSKSNEN YLSDHIRRAD HVSSLTQTIL CDAITSGGLL AAMPEDEAKQ YVEAMHKQNE
ADTSIIGYVE KRGSHAISLQ
//
