ID   SELD_ECO57              Reviewed;         347 AA.
AC   P66794; Q8FGY3; Q8XDW6;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   02-SEP-2026, entry version 123.
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};
GN   OrderedLocusNames=Z2797, ECs2470;
OS   Escherichia coli O157:H7.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA   Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA   Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA   Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA   Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA   Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA   Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA   Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT   genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Synthesizes selenophosphate from selenide and ATP.
CC       {ECO:0000255|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:0000255|HAMAP-Rule:MF_00625};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         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   ---------------------------------------------------------------------------
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; AE005174; AAG56750.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB35893.1; -; Genomic_DNA.
DR   PIR; B85786; B85786.
DR   PIR; F90937; F90937.
DR   RefSeq; NP_310497.1; NC_002695.2.
DR   RefSeq; WP_001298241.1; NZ_AP018488.1.
DR   AlphaFoldDB; P66794; -.
DR   SMR; P66794; -.
DR   STRING; 155864.Z2797; -.
DR   GeneID; 914210; -.
DR   GeneID; 93775981; -.
DR   KEGG; ece:Z2797; -.
DR   KEGG; ecs:ECs_2470; -.
DR   PATRIC; fig|386585.9.peg.2585; -.
DR   eggNOG; COG0709; Bacteria.
DR   HOGENOM; CLU_032859_0_1_6; -.
DR   OMA; LARDWMC; -.
DR   Proteomes; UP000000558; 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:L-selenocysteine biosynthetic process; IEA:InterPro.
DR   CDD; cd02195; SelD; 1.
DR   FunFam; 3.30.1330.10:FF:000003; Selenide, water dikinase; 1.
DR   FunFam; 3.90.650.10:FF:000004; Selenide, water dikinase; 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; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW   Reference proteome; Selenium; Transferase.
FT   CHAIN           1..347
FT                   /note="Selenide, water dikinase"
FT                   /id="PRO_0000127622"
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"
SQ   SEQUENCE   347 AA;  36673 MW;  58F544785D01361E CRC64;
     MSENSIRLTQ YSHGAGCGCK ISPKVLETIL HSEQAKFVDP NLLVGNETRD DAAVYDLGNG
     TSVISTTDFF MPIVDNPFDF GRIAATNAIS DIFAMGGKPI MAIAILGWPI NKLSPEIARE
     VTEGGRYACR QAGIALAGGH SIDAPEPIFG LAVTGIVPTE RVKKNSTAQA GCKLFLTKPL
     GIGVLTTAEK KSLLKPEHQG LATEVMCRMN IAGASFANIE GVKAMTDVTG FGLLGHLSEM
     CQGAGVQARV DYDAIPKLPG VEEYIKLGAV PGGTERNFAS YGHLMGEMPR EVRDLLCDPQ
     TSGGLLLAVM PEAENEVKAT AAEFGIELTA IGELVPARGG RAMVEIR
//