SELD_AQUAE
ID SELD_AQUAE Reviewed; 336 AA.
AC O67139;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 132.
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=aq_1030;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC07095.1; Type=Erroneous termination; Note=Truncated C-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE000657; AAC07095.1; ALT_SEQ; Genomic_DNA.
DR PIR; H70388; H70388.
DR RefSeq; NP_213702.1; NC_000918.1.
DR PDB; 2YYE; X-ray; 2.10 A; A/B=1-336.
DR PDB; 2ZAU; X-ray; 2.00 A; A/B/C=27-336.
DR PDB; 2ZOD; X-ray; 1.98 A; A/B=1-336.
DR PDBsum; 2YYE; -.
DR PDBsum; 2ZAU; -.
DR PDBsum; 2ZOD; -.
DR SMR; O67139; -.
DR STRING; 224324.aq_1030; -.
DR DNASU; 1193773; -.
DR EnsemblBacteria; AAC07095; AAC07095; aq_1030.
DR KEGG; aae:aq_1030; -.
DR PATRIC; fig|224324.8.peg.804; -.
DR eggNOG; COG0709; Bacteria.
DR HOGENOM; CLU_032859_0_1_0; -.
DR InParanoid; O67139; -.
DR OMA; DNEPKYG; -.
DR OrthoDB; 882590at2; -.
DR BRENDA; 2.7.9.3; 396.
DR EvolutionaryTrace; O67139; -.
DR Proteomes; UP000000798; 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; IEA:UniProtKB-UniRule.
DR GO; GO:0004756; F:selenide, water dikinase activity; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0016260; P:selenocysteine biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Reference proteome; Selenium; Selenocysteine;
KW Transferase.
FT CHAIN 1..336
FT /note="Selenide, water dikinase"
FT /id="PRO_0000127614"
FT ACT_SITE 13
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT BINDING 16
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 41..43
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 44
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT BINDING 60
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 83
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 83
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT BINDING 131..133
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 219
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT SITE 16
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625"
FT NON_STD 13
FT /note="Selenocysteine"
FT /evidence="ECO:0000255"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:2ZOD"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:2YYE"
FT HELIX 24..28
FT /evidence="ECO:0007829|PDB:2ZOD"
FT STRAND 36..40
FT /evidence="ECO:0007829|PDB:2ZAU"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:2ZAU"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:2ZOD"
FT STRAND 53..62
FT /evidence="ECO:0007829|PDB:2ZOD"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:2ZOD"
FT HELIX 69..86
FT /evidence="ECO:0007829|PDB:2ZOD"
FT STRAND 90..100
FT /evidence="ECO:0007829|PDB:2ZOD"
FT TURN 102..104
FT /evidence="ECO:0007829|PDB:2ZOD"
FT HELIX 107..123
FT /evidence="ECO:0007829|PDB:2ZOD"
FT STRAND 127..135
FT /evidence="ECO:0007829|PDB:2ZOD"
FT STRAND 140..148
FT /evidence="ECO:0007829|PDB:2ZOD"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:2ZOD"
FT STRAND 165..168
FT /evidence="ECO:0007829|PDB:2ZOD"
FT HELIX 174..182
FT /evidence="ECO:0007829|PDB:2ZOD"
FT HELIX 188..191
FT /evidence="ECO:0007829|PDB:2ZOD"
FT HELIX 192..199
FT /evidence="ECO:0007829|PDB:2ZOD"
FT HELIX 203..211
FT /evidence="ECO:0007829|PDB:2ZOD"
FT STRAND 215..219
FT /evidence="ECO:0007829|PDB:2ZOD"
FT HELIX 224..236
FT /evidence="ECO:0007829|PDB:2ZOD"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:2ZOD"
FT HELIX 244..246
FT /evidence="ECO:0007829|PDB:2ZOD"
FT HELIX 251..258
FT /evidence="ECO:0007829|PDB:2ZOD"
FT HELIX 264..273
FT /evidence="ECO:0007829|PDB:2ZOD"
FT TURN 274..276
FT /evidence="ECO:0007829|PDB:2ZOD"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:2ZAU"
FT HELIX 283..290
FT /evidence="ECO:0007829|PDB:2ZOD"
FT STRAND 298..302
FT /evidence="ECO:0007829|PDB:2ZOD"
FT HELIX 304..308
FT /evidence="ECO:0007829|PDB:2ZOD"
FT HELIX 310..317
FT /evidence="ECO:0007829|PDB:2ZOD"
FT STRAND 322..336
FT /evidence="ECO:0007829|PDB:2ZOD"
SQ SEQUENCE 336 AA; 36856 MW; 035E32948AB4755B CRC64;
MVELLKLVRS SGUAAKVGPG DLQEILKGFN IYTDESTLVS IGDDAGVYEH NGIIWVYTVD
IITPVVNDPY LWGAISTANA LSDVYAMGGI PVNALAISCF NNCELDIEIF REVIRGALDK
LREAKTVLLG GHTIDDKEPK FGLSVAGICP EGKYITQSGA QVGQLLILTK PIGTGILIKG
LKEGILKEED INEAIENMLA LNDKARNLML SLDATACTDV TGFGLLGHAW NICKNSNIGA
RIFFEKVPYY QLSENLVKKK IYPKGAIENL NFVKNYLKSN LDNWKLILLS DPVTSGGLLF
TINKEKLEKI DETAKELEVN YWIIGETIAE NVLEVL
