SELD_PSESM
ID SELD_PSESM Reviewed; 344 AA.
AC Q889F7;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=PSPTO_0793;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO54335.1; -; Genomic_DNA.
DR RefSeq; NP_790640.1; NC_004578.1.
DR RefSeq; WP_011103287.1; NC_004578.1.
DR AlphaFoldDB; Q889F7; -.
DR SMR; Q889F7; -.
DR STRING; 223283.PSPTO_0793; -.
DR PRIDE; Q889F7; -.
DR EnsemblBacteria; AAO54335; AAO54335; PSPTO_0793.
DR GeneID; 1182418; -.
DR KEGG; pst:PSPTO_0793; -.
DR PATRIC; fig|223283.9.peg.806; -.
DR eggNOG; COG0709; Bacteria.
DR HOGENOM; CLU_032859_0_1_6; -.
DR OMA; DNEPKYG; -.
DR OrthoDB; 882590at2; -.
DR PhylomeDB; Q889F7; -.
DR Proteomes; UP000002515; 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..344
FT /note="Selenide, water dikinase"
FT /id="PRO_0000127635"
FT ACT_SITE 16
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT BINDING 19
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 47..49
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
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT BINDING 67
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 90
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 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT BINDING 138..140
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 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT SITE 19
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
SQ SEQUENCE 344 AA; 36195 MW; AD50B972B7771F4B CRC64;
MNEPIRLTQY SHGAGCGCKI SPKVLDVILA GSGAQNLDPK LWVGNTSRDD AAVYALDDER
GVVSTTDFFM PIVDDPFDFG RIAATNAISD IYAMGGDPLM AIAILGWPVN VLPPEVAREV
IRGGRAVCDA AGIPLAGGHS IDAPEPIFGL AVTGVVQKKH MKRNDTAQAG CVLYLTKPLG
IGILTTAEKK ARLREEDMGL ARDWMCTLNT PGSRFGKLAG VAAMTDVTGF GLLGHLVEMA
DGAGLTARLD YAAVPRLPGV EHYIAEGCVP GGTLRNFESY GDKIAALSDA QRDLLCDPQT
SGGLLVAVSP EGEAEFLAVA AELGLQLNPI GTLLERQTHA VEVF
