SELD_CAEEL
ID SELD_CAEEL Reviewed; 378 AA.
AC O62461;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 19-DEC-2001, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Probable selenide, water dikinase;
DE EC=2.7.9.3 {ECO:0000250|UniProtKB:P49903};
DE AltName: Full=Selenium donor protein;
DE AltName: Full=Selenophosphate synthase 1;
GN Name=seld-1; ORFNames=Y45F10A.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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 I
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; AL021488; CAA16367.2; -; Genomic_DNA.
DR PIR; T26910; T26910.
DR RefSeq; NP_502604.1; NM_070203.1.
DR AlphaFoldDB; O62461; -.
DR SMR; O62461; -.
DR BioGRID; 54526; 1.
DR STRING; 6239.Y45F10A.4; -.
DR EPD; O62461; -.
DR PaxDb; O62461; -.
DR PeptideAtlas; O62461; -.
DR EnsemblMetazoa; Y45F10A.4.1; Y45F10A.4.1; WBGene00012867.
DR EnsemblMetazoa; Y45F10A.4.2; Y45F10A.4.2; WBGene00012867.
DR GeneID; 189912; -.
DR CTD; 189912; -.
DR WormBase; Y45F10A.4; CE28704; WBGene00012867; seld-1.
DR eggNOG; KOG3939; Eukaryota.
DR GeneTree; ENSGT00390000000950; -.
DR HOGENOM; CLU_032859_1_0_1; -.
DR InParanoid; O62461; -.
DR OMA; RWNKINM; -.
DR OrthoDB; 1166567at2759; -.
DR PhylomeDB; O62461; -.
DR BRENDA; 2.7.9.3; 1045.
DR Reactome; R-CEL-2408557; Selenocysteine synthesis.
DR PRO; PR:O62461; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00012867; Expressed in germ line (C elegans) and 4 other tissues.
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 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 3: Inferred from homology;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Selenium; Transferase.
FT CHAIN 1..378
FT /note="Probable selenide, water dikinase"
FT /id="PRO_0000127654"
FT ACT_SITE 33
FT /evidence="ECO:0000255"
FT BINDING 36
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 63..65
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 65
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P49903"
FT BINDING 83
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 106
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 106
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P49903"
FT BINDING 158..160
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 260
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P49903"
FT SITE 36
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P16456"
SQ SEQUENCE 378 AA; 41555 MW; 66E0A5E10B1653E5 CRC64;
MNRIERILEG FDPVSNGLDE DFVLTKLTGM KGCGCKVPRN VLLQLLQTFK TDLVINNDEV
DIGLDSCVIP LRHPGLRLVQ TTDFFYPLID DPYIMGRVTC ANVLSDLYAM GVSECDNMLM
LLAVAIDLNE KQRDIVVPLF IQGFKDAADE AGTKIRGGQT VRCPWLLLGG VATSVAHESE
IIKVDQAVPG DVLILTKPIG GQVAVNSYEW IKKKNGKIEE LNLEIPKIEK AFKQVCEQMS
RLNRNAAKLL HKYDAHSSTD VTGFGLLGHA ENLARVQKQP MEFIIEKLPI IEYMDEIADK
MIAKGGEGFK LYQGTSAETS GGLLIAMSEE NAKKYIAELS SLDNAPAWII GKVTAKTTDS
SIARILPDAV RISVPSHI
