ID A8HRC1_AZOC5 Unreviewed; 415 AA. AC A8HRC1; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 10-JUN-2026, entry version 101. 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=AZC_1163 {ECO:0000313|EMBL:BAF87161.1}; OS Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG OS 6465 / NBRC 14845 / NCIMB 13405 / ORS 571). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Xanthobacteraceae; Azorhizobium. OX NCBI_TaxID=438753 {ECO:0000313|EMBL:BAF87161.1, ECO:0000313|Proteomes:UP000000270}; RN [1] {ECO:0000313|EMBL:BAF87161.1, ECO:0000313|Proteomes:UP000000270} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270}; RX PubMed=17720818; DOI=10.1128/AEM.01514-07; RA Suzuki S., Aono T., Lee KB., Suzuki T., Liu CT., Miwa H., Wakao S., Iki T., RA Oyaizu H.; RT "Rhizobial factors required for stem nodule maturation and maintenance in RT Sesbania rostrata-Azorhizobium caulinodans ORS571 symbiosis."; RL Appl. Environ. Microbiol. 73:6650-6659(2007). RN [2] {ECO:0000313|Proteomes:UP000000270} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270}; RA Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T., RA Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B., RA Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.; RT "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium RT caulinodans ORS571."; RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:BAF87161.1, ECO:0000313|Proteomes:UP000000270} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270}; RX PubMed=18522759; DOI=10.1186/1471-2164-9-271; RA Lee KB., Backer P.D., Aono T., Liu CT., Suzuki S., Suzuki T., Kaneko T., RA Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B., RA Binnewies T.T., Ussery D.W., D'Haeze W., Herder J.D., Gevers D., RA Vereecke D., Holsters M., Oyaizu H.; RT "The genome of the versatile nitrogen fixer Azorhizobium caulinodans RT ORS571."; RL BMC Genomics 9:271-271(2008). RN [4] {ECO:0000313|EMBL:BAF87161.1, ECO:0000313|Proteomes:UP000000270} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270}; RX PubMed=19542345; DOI=10.1128/AEM.00398-09; RA Tsukada S., Aono T., Akiba N., Lee KB., Liu CT., Toyazaki H., Oyaizu H.; RT "Comparative genome-wide transcriptional profiling of Azorhizobium RT caulinodans ORS571 grown under free-living and symbiotic conditions."; RL Appl. Environ. Microbiol. 75:5037-5046(2009). RN [5] {ECO:0000313|EMBL:BAF87161.1, ECO:0000313|Proteomes:UP000000270} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270}; RX PubMed=20382809; DOI=10.1128/AEM.00238-10; RA Akiba N., Aono T., Toyazaki H., Sato S., Oyaizu H.; RT "phrR-like gene praR of Azorhizobium caulinodans ORS571 is essential for RT symbiosis with Sesbania rostrata and is involved in expression of reb RT genes."; RL Appl. Environ. Microbiol. 76:3475-3485(2010). RN [6] {ECO:0000313|EMBL:BAF87161.1, ECO:0000313|Proteomes:UP000000270} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 / RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270}; RX PubMed=21571889; DOI=10.1128/AEM.02327-10; RA Liu CT., Lee KB., Wang YS., Peng MH., Lee KT., Suzuki S., Suzuki T., RA Oyaizu H.; RT "Involvement of the azorhizobial chromosome partition gene (parA) in the RT onset of bacteroid differentiation during Sesbania rostrata stem nodule RT development."; RL Appl. Environ. Microbiol. 77:4371-4382(2011). CC -!- FUNCTION: Synthesizes selenophosphate from selenide and ATP. CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_00625}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP- CC 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 --------------------------------------------------------------------------- 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; AP009384; BAF87161.1; -; Genomic_DNA. DR AlphaFoldDB; A8HRC1; -. DR STRING; 438753.AZC_1163; -. DR KEGG; azc:AZC_1163; -. DR eggNOG; COG0709; Bacteria. DR HOGENOM; CLU_032859_0_1_5; -. DR Proteomes; UP000000270; 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; PRK00943.1; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00625}; KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00625}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00625}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00625}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00625}; Reference proteome {ECO:0000313|Proteomes:UP000000270}; KW Selenium {ECO:0000256|ARBA:ARBA00023266, ECO:0000256|HAMAP-Rule:MF_00625}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00625}. FT DOMAIN 116..224 FT /note="PurM-like N-terminal" FT /evidence="ECO:0000259|Pfam:PF00586" FT DOMAIN 236..409 FT /note="PurM-like C-terminal" FT /evidence="ECO:0000259|Pfam:PF02769" FT ACT_SITE 84 FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625" FT BINDING 87 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 115..117 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 118 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625" FT BINDING 135 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 158 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625" FT BINDING 158 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 206..208 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 294 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625" FT SITE 87 FT /note="Important for catalytic activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625" SQ SEQUENCE 415 AA; 42882 MW; 189709E104F91E67 CRC64; MVLILIANGS KSLSPKPACA TGSLSRLRGR GGVGRGQNAP FVSRLPRPYQ VAAHPLSRST ECPMSQPVTE QPFRLTSLAH GGGCGCKLAP SVLQELLAGA PAAQPYAQLL VGMETGDDAA VWDLDGETCI VATTDFFMPV VDDPDHFGRI AATNAISDVY AMGGTPIMAL AILGMPLGKV DTGIVRKILE GGSAACAAAG IPVAGGHSID SVEPIYGLAV IGTVRKALVR RNADARPGDA LILTKAVGVG VYSAAFKKEA LSSDAYDEMI ASTTLLNKVG SALAKDSAVH AMTDVTGFGV IGHALEVARG SKLAVTIEAD RVPLMAHAEA LVRQGFVTGA SIRNWASYGA EARLPADFPE WRRHLLTDPQ TSGGLLVSCA PEEADRLVEE IQAAGYPNAR RIGAVTEGAV GLTVA //