ID H5TC85_9ALTE Unreviewed; 350 AA.
AC H5TC85;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
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 ECO:0000313|EMBL:GAB55912.1};
GN ORFNames=GPUN_1796 {ECO:0000313|EMBL:GAB55912.1};
OS Glaciecola punicea ACAM 611.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Glaciecola.
OX NCBI_TaxID=1121923 {ECO:0000313|EMBL:GAB55912.1, ECO:0000313|Proteomes:UP000053586};
RN [1] {ECO:0000313|EMBL:GAB55912.1, ECO:0000313|Proteomes:UP000053586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB55912.1,
RC ECO:0000313|Proteomes:UP000053586};
RX PubMed=22628500; DOI=10.1128/JB.00463-12;
RA Qin Q.-L., Xie B.-B., Shu Y.-L., Rong J.-C., Zhao D.-L., Zhang X.-Y.,
RA Chen X.-L., Zhou B.-C., Zhanga Y.-Z.;
RT "Genome sequence of proteorhodopsin-containing sea ice bacterium Glaciecola
RT punicea ACAM 611T.";
RL J. Bacteriol. 194:3267-3267(2012).
RN [2] {ECO:0000313|EMBL:GAB55912.1, ECO:0000313|Proteomes:UP000053586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACAM 611 {ECO:0000313|EMBL:GAB55912.1,
RC ECO:0000313|Proteomes:UP000053586};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAB55912.1}.
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DR EMBL; BAET01000019; GAB55912.1; -; Genomic_DNA.
DR RefSeq; WP_006005508.1; NZ_BAET01000019.1.
DR AlphaFoldDB; H5TC85; -.
DR STRING; 56804.BAE46_06930; -.
DR eggNOG; COG0709; Bacteria.
DR OrthoDB; 9767928at2; -.
DR Proteomes; UP000053586; Unassembled WGS sequence.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000053586};
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 49..156
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 168..335
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT ACT_SITE 16
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625"
FT BINDING 19
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 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:0000256|HAMAP-Rule:MF_00625"
FT BINDING 50
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|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:0000256|HAMAP-Rule:MF_00625"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|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:0000256|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: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 19
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00625"
SQ SEQUENCE 350 AA; 37085 MW; 1077B5929B125C44 CRC64;
MSDKIRLTQF SHGAGCGCKI APNLLEQFLK TDFVPTPDPK LLVGNSTKDD AAVYDLGDGS
GIISTTDFFM PIVDDAFEFG KVAATNAISD VYAMGGTPIM AIAILGWPTK SLGPDIAQRV
IDGARHTCQE AGIQLAGGHS IDSPEPIFGL AVTGRVKLAH MKRNCSAKAG DHLFLTKPLG
VGILTTAEKQ GKLKAMHSRL AVNSMMQLNT IGEKLGSLNG VNAMTDVTGF GLLGHLLEIC
QGSRLKATVN SRAVPILDSA IYDYIKQGCV SGGSQRNWDS IHQHISQIDA ITQALLCDPQ
TSGGLLVAIA PKALGEAKNL LTQAGCYYEA IGYLQEISVN DPHPLIEVMI
//
