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SELD_PSEAE
ID   SELD_PSEAE              Reviewed;         344 AA.
AC   Q9I383;
DT   25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=PA1642;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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; AE004091; AAG05031.1; -; Genomic_DNA.
DR   PIR; G83439; G83439.
DR   RefSeq; NP_250333.1; NC_002516.2.
DR   RefSeq; WP_003087546.1; NZ_QZGE01000003.1.
DR   AlphaFoldDB; Q9I383; -.
DR   SMR; Q9I383; -.
DR   STRING; 287.DR97_247; -.
DR   PaxDb; Q9I383; -.
DR   PRIDE; Q9I383; -.
DR   EnsemblBacteria; AAG05031; AAG05031; PA1642.
DR   GeneID; 877775; -.
DR   KEGG; pae:PA1642; -.
DR   PATRIC; fig|208964.12.peg.1702; -.
DR   PseudoCAP; PA1642; -.
DR   HOGENOM; CLU_032859_0_1_6; -.
DR   InParanoid; Q9I383; -.
DR   OMA; DNEPKYG; -.
DR   PhylomeDB; Q9I383; -.
DR   BioCyc; PAER208964:G1FZ6-1672-MON; -.
DR   Proteomes; UP000002438; 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; ISS:PseudoCAP.
DR   GO; GO:0004756; F:selenide, water dikinase activity; ISS:PseudoCAP.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0016260; P:selenocysteine biosynthetic process; ISS:PseudoCAP.
DR   GO; GO:0070329; P:tRNA seleno-modification; ISS:PseudoCAP.
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_0000127632"
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;  36354 MW;  2D8451117676D35B CRC64;
     MSEAIRLTQY SHGAGCGCKI SPKVLEVILA GSGAQNLDPK LWVGNASRDD AAVYALDEER
     GVVSTTDFFM PIVDDPFDFG RIAATNAISD IYAMGGDPLM AIAILGWPVN VLAAEVAREV
     IAGGRKVCEE AGIPLAGGHS IDAPEPIFGL AVTGVVEKRF MKRNDTAEAG CRLYLTKPLG
     IGILTTAEKK ARLRAEDVGV ARDWMCTLNR PGARFGRLAG VKAMTDVTGF GLLGHLVEMA
     DGSKLTARVE YAAVPRLASA EYYLEQGCVP GGTLRNFDSY GERIAPLPEV QKLLLCDPQT
     SGGLLVAVAP EGEAEFLAVA AELGLQLAPI GELVERQSLA VQVL
 
 
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