ID G3PII2_GASAC Unreviewed; 382 AA.
AC G3PII2;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 56.
DE RecName: Full=selenide, water dikinase {ECO:0000256|ARBA:ARBA00011997};
DE EC=2.7.9.3 {ECO:0000256|ARBA:ARBA00011997};
OS Gasterosteus aculeatus (Three-spined stickleback).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Eupercaria; Perciformes; Cottioidei; Gasterosteales; Gasterosteidae;
OC Gasterosteus.
OX NCBI_TaxID=69293 {ECO:0000313|Ensembl:ENSGACP00000017410.1, ECO:0000313|Proteomes:UP000007635};
RN [1] {ECO:0000313|Ensembl:ENSGACP00000017410.1, ECO:0000313|Proteomes:UP000007635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Lindblad-Toh K., Mauceli E., Grabherr M., Chang J.L., Lander E.S.;
RL Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGACP00000017410.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (JUL-2023) to UniProtKB.
CC -!- FUNCTION: Synthesizes selenophosphate from selenide and ATP.
CC {ECO:0000256|ARBA:ARBA00003786}.
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|ARBA:ARBA00001359};
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DR AlphaFoldDB; G3PII2; -.
DR STRING; 69293.ENSGACP00000017410; -.
DR Ensembl; ENSGACT00000017444.1; ENSGACP00000017410.1; ENSGACG00000013165.1.
DR eggNOG; KOG3939; Eukaryota.
DR GeneTree; ENSGT00390000000950; -.
DR InParanoid; G3PII2; -.
DR OMA; LDQSERW; -.
DR TreeFam; TF313811; -.
DR Proteomes; UP000007635; Unassembled WGS sequence.
DR Bgee; ENSGACG00000013165; Expressed in embryo and 13 other cell types or tissues.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0004756; F:selenide, water dikinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 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; IPR004536; SPS/SelD.
DR NCBIfam; TIGR00476; selD; 1.
DR PANTHER; PTHR10256; SELENIDE, WATER DIKINASE; 1.
DR PANTHER; PTHR10256:SF1; SELENIDE, WATER DIKINASE 2; 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 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Reference proteome {ECO:0000313|Proteomes:UP000007635};
KW Selenium {ECO:0000256|ARBA:ARBA00023266};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 50..155
FT /note="PurM-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00586"
FT DOMAIN 176..350
FT /note="PurM-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02769"
FT REGION 363..382
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 366..382
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 382 AA; 40906 MW; 983B7CE7E04B58D4 CRC64;
GCKVPQEALL KLLAGLEADR ADGDREGRRP SVRLRPTAAR PSTRLLAGVG MDCCVIPLRH
GGLSLVQTTD FFYPLVEDPY MMGRIACANV LSDLYAMGIT ECDNMLMLLS VSQKMNDKDR
ERVMPLIIQG FRDAAEEGGT SVTGGQTVIN PWIIVGGVAS VVCQPNEFIM PDGAVPGDVL
VLTKPLGTQV AVNAHQWLDQ TERWNKIKLV VTKEEVKEAY QEAMFSMATL NRTAAGLMHK
FQAHAATDVT GFGLLGHANN LAAQQRDEVA FVIHNLPIIA KMAAISKACG NLFNLIQGTS
AETSGGLLVC LPREQAAKFC SEMKSQSSAA GGQGAAGGAW IIGIVEKGDR RARIIDKPRI
IEVPARGSQT ANQENNSASP SP
//