ID F8C333_THEGP Unreviewed; 351 AA.
AC F8C333;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Selenide, water dikinase {ECO:0000256|HAMAP-Rule:MF_00625};
DE EC=2.7.9.3 {ECO:0000256|HAMAP-Rule:MF_00625};
DE AltName: Full=Selenium donor protein {ECO:0000256|HAMAP-Rule:MF_00625};
DE AltName: Full=Selenophosphate synthase {ECO:0000256|HAMAP-Rule:MF_00625};
GN Name=selD {ECO:0000256|HAMAP-Rule:MF_00625};
GN OrderedLocusNames=TOPB45_1445 {ECO:0000313|EMBL:AEH23524.1};
OS Thermodesulfobacterium geofontis (strain OPF15).
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfobacteriaceae;
OC Thermodesulfobacterium.
OX NCBI_TaxID=795359 {ECO:0000313|EMBL:AEH23524.1, ECO:0000313|Proteomes:UP000006583};
RN [1] {ECO:0000313|EMBL:AEH23524.1, ECO:0000313|Proteomes:UP000006583}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OPF15 {ECO:0000313|EMBL:AEH23524.1,
RC ECO:0000313|Proteomes:UP000006583};
RX PubMed=23580711; DOI=10.1128/genomea.00162-13;
RA Elkins J.G., Hamilton-Brehm S.D., Lucas S., Han J., Lapidus A., Cheng J.F.,
RA Goodwin L.A., Pitluck S., Peters L., Mikhailova N., Davenport K.W.,
RA Detter J.C., Han C.S., Tapia R., Land M.L., Hauser L., Kyrpides N.C.,
RA Ivanova N.N., Pagani I., Bruce D., Woyke T., Cottingham R.W.;
RT "Complete genome sequence of the hyperthermophilic sulfate-reducing
RT bacterium Thermodesulfobacterium geofontis OPF15T.";
RL Genome Announc. 1:E0016213-E0016213(2013).
CC -!- FUNCTION: Synthesizes selenophosphate from selenide and ATP.
CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_00625};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00625};
CC Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000256|HAMAP-Rule:MF_00625};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00625}.
CC -!- SIMILARITY: Belongs to the selenophosphate synthase 1 family. Class I
CC subfamily. {ECO:0000256|ARBA:ARBA00008026, ECO:0000256|HAMAP-
CC Rule:MF_00625}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00625}.
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DR EMBL; CP002829; AEH23524.1; -; Genomic_DNA.
DR STRING; 795359.TOPB45_1445; -.
DR KEGG; top:TOPB45_1445; -.
DR PATRIC; fig|795359.3.peg.1471; -.
DR eggNOG; COG0709; Bacteria.
DR HOGENOM; CLU_032859_0_1_0; -.
DR OrthoDB; 9767928at2; -.
DR Proteomes; UP000006583; 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; 3.90.650.10; PurM-like C-terminal domain; 1.
DR Gene3D; 3.30.1330.10; PurM-like, N-terminal domain; 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 NCBIfam; TIGR00476; selD; 1.
DR PANTHER; PTHR10256:SF0; INACTIVE SELENIDE, WATER DIKINASE-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR10256; SELENIDE, WATER DIKINASE; 1.
DR Pfam; PF00586; AIRS; 1.
DR Pfam; PF02769; AIRS_C; 1.
DR PIRSF; PIRSF036407; Selenphspht_syn; 1.
DR SUPFAM; SSF56042; PurM C-terminal domain-like; 1.
DR SUPFAM; SSF55326; PurM N-terminal domain-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00625};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00625};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00625};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00625};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00625};
KW Reference proteome {ECO:0000313|Proteomes:UP000006583};
KW Selenium {ECO:0000256|ARBA:ARBA00023266, ECO:0000256|HAMAP-Rule:MF_00625};
KW Selenocysteine {ECO:0000313|EMBL:AEH23524.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00625}.
FT DOMAIN 46..154
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 166..340
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 15
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625"
FT BINDING 18
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:0000256|HAMAP-Rule:MF_00625"
FT BINDING 48
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625"
FT BINDING 65
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:0000256|HAMAP-Rule:MF_00625"
FT BINDING 88
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625"
FT BINDING 88
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:0000256|HAMAP-Rule:MF_00625"
FT BINDING 136..138
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625"
FT BINDING 226
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625"
FT SITE 18
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625"
FT NON_STD 15
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:AEH23524.1"
SQ SEQUENCE 351 AA; 38437 MW; A982862A85566136 CRC64;
MQEIKLTQMT KASGUAAKLP QEFLVEILKD LEIPSHPYLI QSFEYGADAA IFKINENTAL
IFSADFFTPV IDDPFVFGQI SAANALSDIY VCGGKPLLAL NLICFPKKGI PKEILKKILE
GGLSKIKEAG AFLVGGHSID DPEPKYGLAV VGIAHPEKII SNKNAKEGDL LYLSKPIGLG
ILVTAYKGNL LDEKSNIYKA MIKTMTELNN KIAEILLELD IKAATDITGF GLLGHALEMA
IASKKDLIIY AHRVPYFKEA KDFIEMGIIP EGDYNNLNYC KKNVEIHPEV SENDLILLCD
AQTSGGFLIA VPQEKQEVFE KKAIDAGLNN LALIGEVKNP EGHCPTVRVY P
//
