SPS2_TRYB2
ID SPS2_TRYB2 Reviewed; 393 AA.
AC Q38A34;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Selenide, water dikinase {ECO:0000305};
DE EC=2.7.9.3 {ECO:0000269|PubMed:18812192};
DE AltName: Full=Selenophosphate synthetase 2 {ECO:0000303|PubMed:21723329};
DE AltName: Full=TbSPS2 {ECO:0000303|PubMed:21723329};
DE AltName: Full=TbselD {ECO:0000303|PubMed:18812192};
GN Name=SPS2 {ECO:0000303|PubMed:21723329};
GN Synonyms=SelD {ECO:0000303|PubMed:18812192};
GN ORFNames=Tb10.6k15.0990 {ECO:0000312|EMBL:EAN78336.1};
OS Trypanosoma brucei brucei (strain 927/4 GUTat10.1).
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Trypanosoma.
OX NCBI_TaxID=185431 {ECO:0000312|Proteomes:UP000008524};
RN [1] {ECO:0000312|Proteomes:UP000008524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=927/4 GUTat10.1 {ECO:0000312|Proteomes:UP000008524};
RX PubMed=16020726; DOI=10.1126/science.1112642;
RA Berriman M., Ghedin E., Hertz-Fowler C., Blandin G., Renauld H.,
RA Bartholomeu D.C., Lennard N.J., Caler E., Hamlin N.E., Haas B., Bohme U.,
RA Hannick L., Aslett M.A., Shallom J., Marcello L., Hou L., Wickstead B.,
RA Alsmark U.C.M., Arrowsmith C., Atkin R.J., Barron A.J., Bringaud F.,
RA Brooks K., Carrington M., Cherevach I., Chillingworth T.J., Churcher C.,
RA Clark L.N., Corton C.H., Cronin A., Davies R.M., Doggett J., Djikeng A.,
RA Feldblyum T., Field M.C., Fraser A., Goodhead I., Hance Z., Harper D.,
RA Harris B.R., Hauser H., Hostetler J., Ivens A., Jagels K., Johnson D.,
RA Johnson J., Jones K., Kerhornou A.X., Koo H., Larke N., Landfear S.,
RA Larkin C., Leech V., Line A., Lord A., Macleod A., Mooney P.J., Moule S.,
RA Martin D.M., Morgan G.W., Mungall K., Norbertczak H., Ormond D., Pai G.,
RA Peacock C.S., Peterson J., Quail M.A., Rabbinowitsch E., Rajandream M.A.,
RA Reitter C., Salzberg S.L., Sanders M., Schobel S., Sharp S., Simmonds M.,
RA Simpson A.J., Tallon L., Turner C.M., Tait A., Tivey A.R., Van Aken S.,
RA Walker D., Wanless D., Wang S., White B., White O., Whitehead S.,
RA Woodward J., Wortman J., Adams M.D., Embley T.M., Gull K., Ullu E.,
RA Barry J.D., Fairlamb A.H., Opperdoes F., Barrell B.G., Donelson J.E.,
RA Hall N., Fraser C.M., Melville S.E., El-Sayed N.M.A.;
RT "The genome of the African trypanosome Trypanosoma brucei.";
RL Science 309:416-422(2005).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, ACTIVE SITE, AND MUTAGENESIS OF
RP CYS-42.
RX PubMed=18812192; DOI=10.1016/j.molbiopara.2008.08.009;
RA Sculaccio S.A., Rodrigues E.M., Cordeiro A.T., Magalhaes A., Braga A.L.,
RA Alberto E.E., Thiemann O.H.;
RT "Selenocysteine incorporation in Kinetoplastid: selenophosphate synthetase
RT (SELD) from Leishmania major and Trypanosoma brucei.";
RL Mol. Biochem. Parasitol. 162:165-171(2008).
RN [3] {ECO:0000305}
RP DISRUPTION PHENOTYPE.
RX PubMed=21723329; DOI=10.1016/j.molbiopara.2011.04.007;
RA Costa F.C., Oliva M.A., de Jesus T.C., Schenkman S., Thiemann O.H.;
RT "Oxidative stress protection of Trypanosomes requires selenophosphate
RT synthase.";
RL Mol. Biochem. Parasitol. 180:47-50(2011).
CC -!- FUNCTION: Synthesizes selenophosphate from selenide and ATP.
CC {ECO:0000269|PubMed:18812192}.
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:0000269|PubMed:18812192};
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:0000269|PubMed:18812192}.
CC -!- DISRUPTION PHENOTYPE: RNAi-mediated knock down in procyclic and blood
CC stream forms (strain 29-13) impairs growth following prolonged exposure
CC to oxidative stress. {ECO:0000269|PubMed:21723329}.
CC -!- SIMILARITY: Belongs to the selenophosphate synthase 1 family. Class I
CC subfamily. {ECO:0000305}.
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DR EMBL; CM000208; EAN78336.1; -; Genomic_DNA.
DR RefSeq; XP_823164.1; XM_818071.1.
DR AlphaFoldDB; Q38A34; -.
DR SMR; Q38A34; -.
DR STRING; 5691.EAN78336; -.
DR PaxDb; Q38A34; -.
DR GeneID; 3662208; -.
DR KEGG; tbr:Tb10.6k15.0990; -.
DR VEuPathDB; TriTrypDB:Tb927.10.9410; -.
DR eggNOG; KOG3939; Eukaryota.
DR InParanoid; Q38A34; -.
DR OMA; DNEPKYG; -.
DR BRENDA; 2.7.9.3; 6519.
DR Proteomes; UP000008524; Chromosome 10.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:GeneDB.
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; IDA:GeneDB.
DR GO; GO:0072721; P:cellular response to dithiothreitol; IMP:GeneDB.
DR GO; GO:1904577; P:cellular response to tunicamycin; IMP:GeneDB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016260; P:selenocysteine biosynthetic process; IDA:GeneDB.
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 1: Evidence at protein level;
KW ATP-binding; Kinase; Magnesium; Metal-binding; Nucleotide-binding;
KW Reference proteome; Selenium; Transferase.
FT CHAIN 1..393
FT /note="Selenide, water dikinase"
FT /id="PRO_0000451405"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 42
FT /evidence="ECO:0000305|PubMed:18812192"
FT BINDING 45
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 68..70
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 70
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P49903"
FT BINDING 93
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 116
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 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P49903"
FT BINDING 167..170
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 273
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P49903"
FT SITE 45
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250|UniProtKB:P16456"
FT MUTAGEN 42
FT /note="C->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:18812192"
SQ SEQUENCE 393 AA; 42984 MW; 23283111B52CFE30 CRC64;
MSEKEGKVIP ETNGMKRPRF DPVKLGLPEE FTLTDYTRLK GCSCKVPQPE LLALLQSVST
TPGRRDVGMD CSIVKLQHKD ETGKPLYMVS TTDFFFPSVE DPYLQGQIGA ANVLSDLYST
GIDRCDTVLM LLAASTDMDK TEREVCTQEM MKGFVDHVRL AGSDVTGGQT VMNPWPLIGG
IATSVVAESQ MIRPTGLQPG DILVLTKPLG CQIAVNLKQW LRRPSPIFEE QIQGKMDSEE
IEELYNAAAD GMKRLNRMAA ALMHSHGAHG ATDVTGFGIL GHAKNLGSAQ KADVCLVLDS
LPMYRGAVKA SKLMGDKYRL FEGYAAETSG GLLVAFGTRE EAEGYIRELY ETDGEPAWVV
GRVVRREGSA PYALLQKDYK IIEVGAKVND KII
