(data stored in ACNUC7421 zone)

SWISSPROT: D6XWP4_BACIE

ID   D6XWP4_BACIE            Unreviewed;       321 AA.
AC   D6XWP4;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 66.
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=Bsel_0346 {ECO:0000313|EMBL:ADH97886.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97886.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97886.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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;
CC         EC=2.7.9.3; 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   -!- SIMILARITY: Belongs to the selenophosphate synthase 1 family.
CC       Class I subfamily. {ECO:0000256|HAMAP-Rule:MF_00625,
CC       ECO:0000256|SAAS:SAAS00847687}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00625}.
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DR   EMBL; CP001791; ADH97886.1; -; Genomic_DNA.
DR   STRING; 439292.Bsel_0346; -.
DR   EnsemblBacteria; ADH97886; ADH97886; Bsel_0346.
DR   KEGG; bse:Bsel_0346; -.
DR   eggNOG; ENOG4105D4F; Bacteria.
DR   eggNOG; COG0709; LUCA.
DR   HOGENOM; HOG000219299; -.
DR   KO; K01008; -.
DR   OMA; PIRLTQY; -.
DR   Proteomes; UP000000271; Chromosome.
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:selenocysteine biosynthetic process; IEA:InterPro.
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   3: Inferred from homology;
DR   PRODOM; D6XWP4.
DR   SWISS-2DPAGE; D6XWP4.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00625};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00625, ECO:0000313|EMBL:ADH97886.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00625};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00625};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Selenium {ECO:0000256|HAMAP-Rule:MF_00625};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00625}.
FT   DOMAIN       30    128       AIRS. {ECO:0000259|Pfam:PF00586}.
FT   DOMAIN      140    317       AIRS_C. {ECO:0000259|Pfam:PF02769}.
FT   NP_BIND     201    207       ATP. {ECO:0000256|HAMAP-Rule:MF_00625}.
SQ   SEQUENCE   321 AA;  34085 MW;  A70A69463E1A9E5E CRC64;
     MRHLPEGTKN ENLLVGLDTS DDGGVFKLTD DLAIVQSIDY FTPICDDPYM FGQIAAANAL
     SDIYAMGGKP VTALNIVGYP IKKMPPETLA EILRGGADKI QESGAVLAGG HSIDDQEPKY
     GLSVTGTVHP DAIFKNVGAK TGDKLVLTKP LGAGIITTAI KFGKASEQEQ KDVMTAMATL
     NKTAAETLAD FHPHAVTDVT GFGLTGHGFE MASGSNVTLH ISYKDVPVIN GTLSHARNKV
     IPGGGRENRD YLLEHVEHAP HIELADQLIL SDSITSGGLL VSLPADEADA YVEAYNRAQD
     TFKAAVIGHV TDFEGHAIKI R
//

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