ID SELD_PORG3 Reviewed; 348 AA. AC B2RLG7; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 04-NOV-2026, entry version 94. 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}; GN OrderedLocusNames=PGN_1693; OS Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM OS 12257 / NCTC 11834 / 2561). OC Bacteria; Pseudomonadati; Bacteroidota; Bacteroidia; Bacteroidales; OC Porphyromonadaceae; Porphyromonas. OX NCBI_TaxID=431947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / RC 2561; RX PubMed=18524787; DOI=10.1093/dnares/dsn013; RA Naito M., Hirakawa H., Yamashita A., Ohara N., Shoji M., Yukitake H., RA Nakayama K., Toh H., Yoshimura F., Kuhara S., Hattori M., Hayashi T., RA Nakayama K.; RT "Determination of the genome sequence of Porphyromonas gingivalis strain RT ATCC 33277 and genomic comparison with strain W83 revealed extensive genome RT rearrangements in P. gingivalis."; RL DNA Res. 15:215-225(2008). CC -!- FUNCTION: Synthesizes selenophosphate from selenide and ATP. CC {ECO:0000255|HAMAP-Rule:MF_00625}. CC -!- CATALYTIC ACTIVITY: CC Reaction=hydrogenselenide + ATP + H2O = selenophosphate + AMP + CC phosphate + 2 H(+); 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; Evidence={ECO:0000255|HAMAP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AP009380; BAG34212.1; -; Genomic_DNA. DR RefSeq; WP_012458463.1; NC_010729.1. DR AlphaFoldDB; B2RLG7; -. DR SMR; B2RLG7; -. DR DNASU; 6330824; -. DR GeneID; 29256858; -. DR KEGG; pgn:PGN_1693; -. DR eggNOG; COG0709; Bacteria. DR HOGENOM; CLU_032859_0_1_10; -. DR OMA; AACRDMT; -. DR OrthoDB; 9772934at2; -. DR BioCyc; PGIN431947:G1G2V-1901-MONOMER; -. DR Proteomes; UP000008842; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter. 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:0016260; P:L-selenocysteine biosynthetic process; IEA:InterPro. DR CDD; cd02195; SelD; 1. DR FunFam; 3.30.1330.10:FF:000003; Selenide, water dikinase; 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; NF002098; selD; 1. 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; Kinase; Magnesium; Metal-binding; Nucleotide-binding; KW Reference proteome; Selenium; Transferase. FT CHAIN 1..348 FT /note="Selenide, water dikinase" FT /id="PRO_1000130521" FT ACT_SITE 17 FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625" FT BINDING 20 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 20 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00625" SQ SEQUENCE 348 AA; 36904 MW; 642E546C222075E4 CRC64; MNRSSFDLLS TVEYGGCSAK LDPAKLSELL HDIPLPVDSR IMVDVSTHDD AGVYRLNDDT ALIVTTDFFP PVCSDPYTFG RIAAANALSD VYAMGGRPLL VLNLTMFPSE GIPVEVLADI LRGGQQTIDE SGAFTMGGHT IDDPIPKYGL AVTGIVHPEH LVTNAGVRAG QCLVLTKPLG IGVAMAAHRL GLIGSEVYEA AIGQMCLLNR AGAELMQKYG IRGATDITGF GLLGHAKELA EASDVCLHID SRSVPVLPEC LSLLRDGCIP GATFRNLRFV GDMLRADCPT EYKMLLADAQ TSGGLLMAVD ADRAEDLVAD LHRTGLHPFA AIIGYATDAE DAAKLIVT //