SELD_DICDI
ID SELD_DICDI Reviewed; 364 AA.
AC Q94497; Q54SK1;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Selenide, water dikinase;
DE EC=2.7.9.3 {ECO:0000250|UniProtKB:P49903};
DE AltName: Full=Selenium donor protein;
DE AltName: Full=Selenophosphate synthase;
GN Name=selD; ORFNames=DDB_G0282367;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-335.
RC STRAIN=AX4;
RA Shaulsky G., Loomis W.F.;
RT "The selD gene of Dictyostelium.";
RL Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Synthesizes selenophosphate from selenide and ATP.
CC {ECO:0000250|UniProtKB:P49903}.
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:0000250|UniProtKB:P49903};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P49903};
CC Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000250|UniProtKB:P49903};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P49903}.
CC -!- SIMILARITY: Belongs to the selenophosphate synthase 1 family. Class II
CC subfamily. {ECO:0000305}.
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; AAFI02000047; EAL66043.2; -; Genomic_DNA.
DR EMBL; U68248; AAB17998.1; -; mRNA.
DR RefSeq; XP_640038.2; XM_634946.2.
DR STRING; 44689.DDB0214887; -.
DR PaxDb; Q94497; -.
DR PRIDE; Q94497; -.
DR EnsemblProtists; EAL66043; EAL66043; DDB_G0282367.
DR GeneID; 8623564; -.
DR KEGG; ddi:DDB_G0282367; -.
DR dictyBase; DDB_G0282367; selD.
DR eggNOG; KOG3939; Eukaryota.
DR HOGENOM; CLU_032859_1_0_1; -.
DR InParanoid; Q94497; -.
DR OMA; DNEPKYG; -.
DR PhylomeDB; Q94497; -.
DR Reactome; R-DDI-2408557; Selenocysteine synthesis.
DR PRO; PR:Q94497; -.
DR Proteomes; UP000002195; Chromosome 3.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 GO; GO:0016259; P:selenocysteine metabolic process; IDA:dictyBase.
DR CDD; cd02195; SelD; 1.
DR Gene3D; 3.30.1330.10; -; 1.
DR Gene3D; 3.90.650.10; -; 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; 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 2: Evidence at transcript level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Selenium; Selenocysteine; Transferase.
FT CHAIN 1..364
FT /note="Selenide, water dikinase"
FT /id="PRO_0000127655"
FT ACT_SITE 25
FT /evidence="ECO:0000255"
FT BINDING 28
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:0000250|UniProtKB:P49903"
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:0000250|UniProtKB:P49903"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P49903"
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:0000250|UniProtKB:P49903"
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:0000250|UniProtKB:P49903"
FT BINDING 89
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P49903"
FT BINDING 141..143
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250|UniProtKB:P49903"
FT BINDING 244
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P49903"
FT SITE 28
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P16456"
FT NON_STD 25
FT /note="Selenocysteine"
FT /evidence="ECO:0000305"
FT CONFLICT 25
FT /note="U -> G (in Ref. 2; AAB17998)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="E -> G (in Ref. 2; AAB17998)"
FT /evidence="ECO:0000305"
FT CONFLICT 66
FT /note="D -> DVSLKLFKNKNKLIKLYIYIYLIYIYIFFIIFLKKK (in Ref.
FT 2; AAB17998)"
FT /evidence="ECO:0000305"
FT CONFLICT 124
FT /note="I -> K (in Ref. 2; AAB17998)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="K -> N (in Ref. 2; AAB17998)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="V -> F (in Ref. 2; AAB17998)"
FT /evidence="ECO:0000305"
FT CONFLICT 198..200
FT /note="ERW -> KRG (in Ref. 2; AAB17998)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="E -> K (in Ref. 2; AAB17998)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="R -> K (in Ref. 2; AAB17998)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="R -> K (in Ref. 2; AAB17998)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="K -> N (in Ref. 2; AAB17998)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 364 AA; 40552 MW; 09DD8AA7105A8615 CRC64;
MSISIKDKKE ELLCRLTDFT KLKGUGCKVP QAELLSLLDG IGEGIGYDCS ISQTKFPDIV
MIQTTDFFFP LVDDPYFQGK IACANVLSDL YSFGIEDCDN MLMLLACSTD MTAEQRQWSS
KLMIQGFNDQ AICAGSKVSG GQTVKNPWPI VGGVATSILK TNEFIKPVNA VPGDVLVLTK
PLGTQVCVNF HQWLSKPERW EKINTITNAE ECEQVFNYAT LSMARLNRVG ARLMKKYNAH
AATDVTGFGI LGHSTNLAQN QLLPIRFEIH TLPIIKHMKK LEDHLNHPFK LLKGTSAETS
GGLLISMSRE NAEAFCKEIY EIEKQPAWII GDVIDQSSNY DRSKNTSIIL ENPKIIEVEP
NTNF
