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SELD_METJA
ID   SELD_METJA              Reviewed;         349 AA.
AC   P60819;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 81.
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=MJ1591;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   PROBABLE SELENOCYSTEINE AT SEC-19.
RX   PubMed=9102456; DOI=10.1006/jmbi.1996.0812;
RA   Wilting R., Schorling S., Persson B.C., Boeck A.;
RT   "Selenoprotein synthesis in archaea: identification of an mRNA element of
RT   Methanococcus jannaschii probably directing selenocysteine insertion.";
RL   J. Mol. Biol. 266:637-641(1997).
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, ECO:0000305}.
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DR   EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   InParanoid; P60819; -.
DR   OMA; DNEPKYG; -.
DR   PhylomeDB; P60819; -.
DR   Proteomes; UP000000805; 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; Selenocysteine; Transferase.
FT   CHAIN           1..349
FT                   /note="Selenide, water dikinase"
FT                   /id="PRO_0000127645"
FT   ACT_SITE        19
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT   BINDING         22
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         50..52
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         53
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT   BINDING         69
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         92
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         92
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT   BINDING         140..142
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         246
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT   SITE            22
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT   NON_STD         19
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   349 AA;  38040 MW;  93B43EB552563680 CRC64;
     MERGNEKIKL TELVKLHGUA CKLPSTELEF LVKGIVTDDD LLDKNILVGL GDDASIIKRN
     GLVIAKTVDV FTPIVDDPYI QGKIAACNST SDIYAMGLLD IVGVLAIVGI PEKLPIHVVR
     EMLKGFQDFC RENKTTIVGG HTILNPWPLI GGAVTGVGRE EEVLTKAGVK VGDVLILTKP
     LGTQTAMALS RIPEEFKDLI SITEEERDYI INKAIEIMTT SNRYALKALR KAEERVGDKI
     ANALTDITGF GILGHSNEMA KNSNVLIEIN LLPCIKRTPE LSRLFGHALL DGYGAETAGG
     LLISAKEEYK DNLIDELEKA KCYAFEVGRV VKKGEGKAVL SKDVKVIEI
 
 
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