SELD_SULDN
ID SELD_SULDN Reviewed; 343 AA.
AC Q30RE1;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=Suden_1162;
OS Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS denitrificans (strain ATCC 33889 / DSM 1251)).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Thiovulaceae; Sulfurimonas.
OX NCBI_TaxID=326298;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33889 / DSM 1251;
RX PubMed=18065616; DOI=10.1128/aem.01844-07;
RA Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT denitrificans.";
RL Appl. Environ. Microbiol. 74:1145-1156(2008).
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}.
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DR EMBL; CP000153; ABB44440.1; -; Genomic_DNA.
DR AlphaFoldDB; Q30RE1; -.
DR SMR; Q30RE1; -.
DR STRING; 326298.Suden_1162; -.
DR EnsemblBacteria; ABB44440; ABB44440; Suden_1162.
DR KEGG; tdn:Suden_1162; -.
DR eggNOG; COG0709; Bacteria.
DR HOGENOM; CLU_032859_0_1_7; -.
DR OMA; RWNKINM; -.
DR Proteomes; UP000002714; Chromosome.
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; 3.30.1330.10; -; 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..343
FT /note="Selenide, water dikinase"
FT /id="PRO_1000130522"
FT ACT_SITE 15
FT /evidence="ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00625"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_00625"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT BINDING 137..139
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 225
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT SITE 18
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
SQ SEQUENCE 343 AA; 36870 MW; 598FB1917AFACD97 CRC64;
MEEIKLTEYS HGAGCGCKIS PMLLDEILKT DISSTLYPQL LVGNEHKDDA AAYDLGNGTS
VLSTTDFFMP IVDDAFTFGR IAATNALSDI YAMGGKPLMA ISIFGWPIEK LSSEVARQVI
DGGRAACEDA GIPLAGGHSI DSPEPIFGLA VTGIVDNKNL MKNSSATDDC YIFITKSIGI
GILTTAQKQK KIEDGDIDVA IEAMATLNRA GAIFATLDSV LTMTDVTGFG LLGHLSEVCE
ASGISANIWF EKVPLLQNVE KYRAQGCIPG GSRKNFMSYG HKISQISDRQ REILCDAQTS
GGLLVFVKKS GLDEFYKSAK EFGLNLEPIG ETTPRRKHVI EVL
