ID A0A1X9MBM9_9BACI Unreviewed; 319 AA.
AC A0A1X9MBM9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 08-OCT-2025, entry version 29.
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 ECO:0000313|EMBL:ARK30845.1};
GN ORFNames=BkAM31D_13905 {ECO:0000313|EMBL:ARK30845.1};
OS Halalkalibacter krulwichiae.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Halalkalibacter.
OX NCBI_TaxID=199441 {ECO:0000313|EMBL:ARK30845.1, ECO:0000313|Proteomes:UP000193006};
RN [1] {ECO:0000313|EMBL:ARK30845.1, ECO:0000313|Proteomes:UP000193006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM31D {ECO:0000313|EMBL:ARK30845.1,
RC ECO:0000313|Proteomes:UP000193006};
RA Krulwich T.A., Anastor L., Ehrlich R., Ehrlich G.D., Janto B.;
RT "Bacillus krulwichiae AM31D Genome sequencing and assembly.";
RL Submitted (APR-2017) 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; CP020814; ARK30845.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X9MBM9; -.
DR STRING; 199441.BkAM31D_13905; -.
DR KEGG; bkw:BkAM31D_13905; -.
DR Proteomes; UP000193006; 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: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:UP000193006};
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 140..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 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 319 AA; 33942 MW; AAD0363BBE5A105A CRC64;
MRHLPKQTHD PNLLVGLDTS DDAGAYRLTD DLAMIQTVDY FTPVVDDAYM FGQIAAANAL
SDVYAMGGKP KTVMNIVGFP IKKLPPEILA DILRGAADKT KEAGAIIVGG HSIDDQEPKF
GLSVTGLAHP DRIFKNVGAK PGDILILTKP IGVGILTTGI KREAVTSEQE KAVTETMALL
NKQAAEKLEG LHPNAVTDVT GFGLLGHSYE MAKGSDVTFE LVLDQIPLLE GTRELAEKGI
VPGGSKANER WLDGCVDYAE TITDVEKAIL CDAITSGGLL ISLPANEAED YVHSMNQDGA
HASIIGKVVT KQNKSISVK
//
