SELD2_PEPAC
ID SELD2_PEPAC Reviewed; 347 AA.
AC Q9L4E1;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Selenide, water dikinase 2 {ECO:0000255|HAMAP-Rule:MF_00625};
DE EC=2.7.9.3 {ECO:0000255|HAMAP-Rule:MF_00625};
DE AltName: Full=Selenium donor protein 2 {ECO:0000255|HAMAP-Rule:MF_00625};
DE AltName: Full=Selenophosphate synthase 2 {ECO:0000255|HAMAP-Rule:MF_00625};
GN Name=selD2 {ECO:0000255|HAMAP-Rule:MF_00625}; Synonyms=selD1;
OS Peptoclostridium acidaminophilum (Eubacterium acidaminophilum).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptoclostridium.
OX NCBI_TaxID=1731;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 49065 / DSM 3953 / al-2;
RX PubMed=11041351; DOI=10.1007/s002030000196;
RA Gursinsky T., Jaeger J., Andreesen J.R., Soehling B.;
RT "A selDABC cluster for selenocysteine incorporation in Eubacterium
RT acidaminophilum.";
RL Arch. Microbiol. 174:200-212(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, ECO:0000305}.
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DR EMBL; AJ245960; CAB53233.1; -; Genomic_DNA.
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 Selenium; Selenocysteine; Transferase.
FT CHAIN 1..347
FT /note="Selenide, water dikinase 2"
FT /id="PRO_0000127623"
FT ACT_SITE 18
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT BINDING 21
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 48..50
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 51
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT BINDING 68
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 91
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 91
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 21
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT NON_STD 18
FT /note="Selenocysteine"
SQ SEQUENCE 347 AA; 36741 MW; 79F75206A19FF657 CRC64;
MKGSKEIKLT QMVTASGUAA KIGPEDLAKA LVGLPKMFDE RLLVGFDTSD DAAVYRLDDD
KALIQTLDFF TPMVDDPYLF GQIAASNSLS DVYAMVGKPI VAMNIVCFPS CHDMSILGEI
LKGGADKVIE SGAILVGGHT VDDKEPKYGL SVAGLVHPDK VLANSGARPG DALILTKPIG
TGIVSTGMKA AMVQKSTEDE VVKIMAHLNK YAAEALDGFN VNSVTDITGF GFLGHAAEMA
KGSGVTLEIS SKDIPIMSEA EELAKMGIIP AGMYRNKKFI QSDVLCEGVS EHIMDILYDP
QTSGGLLVSV PQEHARALAD KMTSCGSLAA KIVGRVLSKE EKSIIVI
