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Database: UniProt
Entry: W6N8D8_CLOTY
LinkDB: W6N8D8_CLOTY
Original site: W6N8D8_CLOTY 
ID   W6N8D8_CLOTY            Unreviewed;       343 AA.
AC   W6N8D8;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=CTDIVETGP_2755 {ECO:0000313|EMBL:CDL92685.1};
OS   Clostridium tyrobutyricum DIVETGP.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1408889 {ECO:0000313|EMBL:CDL92685.1, ECO:0000313|Proteomes:UP000019482};
RN   [1] {ECO:0000313|EMBL:CDL92685.1, ECO:0000313|Proteomes:UP000019482}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DIVETGP {ECO:0000313|EMBL:CDL92685.1,
RC   ECO:0000313|Proteomes:UP000019482};
RA   Soggiu A., Piras C., Gaiarsa S., Sassera D., Roncada P., Bendixen E.,
RA   Brasca M., Bonizzi L.;
RT   "Draft Genome Sequence of Clostridium tyrobutyricum Strain DIVETGP,
RT   Isolated from Cow's Milk for Grana Padano Production.";
RL   Genome Announc. 3:213-215(2015).
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:CDL92685.1}.
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DR   EMBL; CBXI010000044; CDL92685.1; -; Genomic_DNA.
DR   RefSeq; WP_017752135.1; NZ_CBXI010000044.1.
DR   AlphaFoldDB; W6N8D8; -.
DR   GeneID; 29419407; -.
DR   OrthoDB; 9772934at2; -.
DR   Proteomes; UP000019482; 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|HAMAP-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:UP000019482};
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          48..154
FT                   /note="PurM-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00586"
FT   DOMAIN          166..343
FT                   /note="PurM-like C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02769"
FT   ACT_SITE        15
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00625"
FT   BINDING         18
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         46..48
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
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00625"
FT   BINDING         66
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         89
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00625"
FT   BINDING         89
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         136..138
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         224
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00625"
FT   SITE            18
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00625"
SQ   SEQUENCE   343 AA;  37393 MW;  5DB3A524500AD3B4 CRC64;
     MSDKNSCEFT CGGGCTAKLG AGFLKHVLES LPESRHDPNL LIGFQSSDDA AVYKITDDIA
     IIQTLDFFPP VVEDPYTFGK IAAANALSDI YAMGGNVKTA LNIVCFPEKL DSSILADILR
     GGAEKVYEAG GIVCGGHSIN DSECKYGLSV TGIVNPKNIL PNNNCKIGDK LILTKPLGVG
     IITTANRVGE ASTKAYEKAV KSMETLNKYA SEIIKRYEVN ACTDVTGFGF LGHLNEMTRE
     NYTMLIEADS IPYITEAYDY AKEFLITAGG QKNRNHLKDK VKMENIEFAL QEILFDPQTS
     GGFIISVNKD DAHNLLNELN NLHIKSNIVG EVTERTNYNI VVK
//
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