ID A0A263BRG3_9BACI Unreviewed; 351 AA.
AC A0A263BRG3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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:OZM56299.1};
GN ORFNames=CIB95_12860 {ECO:0000313|EMBL:OZM56299.1};
OS Lottiidibacillus patelloidae.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lottiidibacillus.
OX NCBI_TaxID=2670334 {ECO:0000313|EMBL:OZM56299.1, ECO:0000313|Proteomes:UP000217083};
RN [1] {ECO:0000313|Proteomes:UP000217083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA5d-4 {ECO:0000313|Proteomes:UP000217083};
RA Huang Z.;
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OZM56299.1, ECO:0000313|Proteomes:UP000217083}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA5d-4 {ECO:0000313|EMBL:OZM56299.1,
RC ECO:0000313|Proteomes:UP000217083};
RA Liu R., Dong C., Shao Z.;
RT "Bacillus patelloidae sp. nov., isolated from the intestinal tract of a
RT marine limpet.";
RL Submitted (SEP-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=ATP + H2O + hydrogenselenide = AMP + 2 H(+) + phosphate +
CC selenophosphate; 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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OZM56299.1}.
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; NPIA01000007; OZM56299.1; -; Genomic_DNA.
DR Proteomes; UP000217083; Unassembled WGS sequence.
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:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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|HAMAP-Rule:MF_00625};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00625};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00625};
KW Reference proteome {ECO:0000313|Proteomes:UP000217083};
KW Selenium {ECO:0000256|ARBA:ARBA00023266, ECO:0000256|HAMAP-Rule:MF_00625};
KW Selenocysteine {ECO:0000313|EMBL:OZM56299.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00625}.
FT DOMAIN 51..158
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 170..348
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 18
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625"
FT BINDING 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 49..51
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 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625"
FT BINDING 69
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 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625"
FT BINDING 92
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 140..142
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 228
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625"
FT SITE 21
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625"
FT NON_STD 18
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:OZM56299.1"
SQ SEQUENCE 351 AA; 37578 MW; 72C6665EDE7877BF CRC64;
MSEQEKIRLT ALSTKAGUGC KIGPEDLSQV LRHLPEREHD PNLLVGLDTS DDAGVYKVTD
DIALIQTVDY FTPIVDDPYT FGQIAAANAL SDVYAMGGKP KTVLNIVGFP IKALGPEVLA
EILKGAADKT KEAGAIIVGG HSIDDQEPKF GLSVTGYVHP DKFYKNVGSK PGDVLVLTKP
IGVGVLTTGI KRNEVTEEQE KAVTIAMATL NKRAAELLEE FSPTAVTDVT GFGLLGHSTE
MAKGSKVSFD IKLSDVPVLD GTYELIQKGI VPGGTKANHS WLKDDVEYDE SLTFEDEMLL
CDAVTSGGLL ISMPADQAEQ YVEKCKNNGI EAASIIGTVS AKKEKSIYAK R
//
