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SELD_SALTY
ID   SELD_SALTY              Reviewed;         347 AA.
AC   Q8ZPV5; Q9XC76;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Selenide, water dikinase {ECO:0000255|HAMAP-Rule:MF_00625};
DE            EC=2.7.9.3 {ECO:0000255|HAMAP-Rule:MF_00625};
DE   AltName: Full=Selenium donor protein {ECO:0000255|HAMAP-Rule:MF_00625};
DE   AltName: Full=Selenophosphate synthase {ECO:0000255|HAMAP-Rule:MF_00625};
GN   Name=selD {ECO:0000255|HAMAP-Rule:MF_00625}; OrderedLocusNames=STM1297;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-157.
RA   Hallenbeck P.C.;
RT   "Mutations that permit the expression of fdhF in a selD mutant of
RT   Salmonella typhimurium.";
RL   Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Synthesizes selenophosphate from selenide and ATP.
CC       {ECO:0000255|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:0000255|HAMAP-Rule:MF_00625};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00625};
CC       Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000255|HAMAP-Rule:MF_00625};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00625}.
CC   -!- SIMILARITY: Belongs to the selenophosphate synthase 1 family. Class I
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00625}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD43089.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE006468; AAL20222.1; -; Genomic_DNA.
DR   EMBL; AF147202; AAD43089.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_460263.1; NC_003197.2.
DR   RefSeq; WP_001294900.1; NC_003197.2.
DR   AlphaFoldDB; Q8ZPV5; -.
DR   SMR; Q8ZPV5; -.
DR   STRING; 99287.STM1297; -.
DR   PaxDb; Q8ZPV5; -.
DR   EnsemblBacteria; AAL20222; AAL20222; STM1297.
DR   GeneID; 1252815; -.
DR   KEGG; stm:STM1297; -.
DR   PATRIC; fig|99287.12.peg.1378; -.
DR   HOGENOM; CLU_032859_0_1_6; -.
DR   OMA; DNEPKYG; -.
DR   PhylomeDB; Q8ZPV5; -.
DR   BioCyc; SENT99287:STM1297-MON; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0016260; P:selenocysteine biosynthetic process; IBA:GO_Central.
DR   CDD; cd02195; SelD; 1.
DR   Gene3D; 3.30.1330.10; -; 1.
DR   Gene3D; 3.90.650.10; -; 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   PANTHER; PTHR10256; PTHR10256; 1.
DR   Pfam; PF00586; AIRS; 1.
DR   Pfam; PF02769; AIRS_C; 1.
DR   PIRSF; PIRSF036407; Selenphspht_syn; 1.
DR   SUPFAM; SSF55326; SSF55326; 1.
DR   SUPFAM; SSF56042; SSF56042; 1.
DR   TIGRFAMs; TIGR00476; selD; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Selenium; Transferase.
FT   CHAIN           1..347
FT                   /note="Selenide, water dikinase"
FT                   /id="PRO_0000127638"
FT   ACT_SITE        17
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT   BINDING         20
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:0000255|HAMAP-Rule:MF_00625"
FT   BINDING         48..50
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:0000255|HAMAP-Rule:MF_00625"
FT   BINDING         51
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT   BINDING         68
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:0000255|HAMAP-Rule:MF_00625"
FT   BINDING         91
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:0000255|HAMAP-Rule:MF_00625"
FT   BINDING         91
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT   BINDING         139..141
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT   BINDING         227
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT   SITE            20
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT   CONFLICT        81..82
FT                   /note="GR -> AG (in Ref. 2; AAD43089)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   347 AA;  36438 MW;  F63A20121E6E596A CRC64;
     MSEQAIRLTQ YSHGAGCGCK ISPKVLETIL HSEQAKFVDP NLLVGNETRD DAAVYDLGNG
     TSIISTTDFF MPIVDNPFDF GRIAATNAIS DIFAMGGKPI MAIAILGWPI NTLSPDIARE
     VTEGGRFACR QAGIALAGGH SIDAPEPIFG LAVTGVVPTE RVKKNSTAQA GCKLFLTKPL
     GIGVLTTAEK KSLLKPEHQG LATEVMCRMN VAGAAFANID GVKAMTDVTG FGLLGHLSEM
     CQGAGVQALL CYQDIPKLPG VEEYIALGAV PGGTERNFAS YGHLMGDMSR EVRSLLCDPQ
     TSGGLLLAVT PDAEDDVKAT AAEFGIDLTA IGELVEARGG RAMVEIR
 
 
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