Selenide, water dikinase (P16456)

Identification
Name:Selenide, water dikinase
Synonyms:
  • Selenium donor protein
  • Selenophosphate synthase
Gene Name:selD
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Synthesizes selenophosphate from selenide and ATP
Cellular Location:Not Available
SMPDB Pathways:Not Available
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Hydrogen selenide + 1.0Water ↔ 1.0Adenosine monophosphate + 1.0Phosphoroselenoic acid + 1.0Phosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Water + 1.0Selenium → 1.0Adenosine monophosphate + 1.0Phosphate + 1.0Phosphoroselenoic acid
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Adenosine triphosphate + 1.0Hydrogen selenide + 1.0Water → 1.0Adenosine monophosphate + 1.0Phosphoroselenoic acid + 1.0Inorganic phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB00538Adenosine triphosphateMetaboCard
ECMDB11110Hydrogen selenideMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB03840Phosphoroselenoic acidMetaboCard
ECMDB01349SeleniumMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
adenyl nucleotide binding
adenyl ribonucleotide binding
ATP binding
binding
catalytic activity
kinase activity
nucleoside binding
purine nucleoside binding
selenide, water dikinase activity
transferase activity
transferase activity, transferring phosphorus-containing groups
Gene Properties
Blattner:b1764
Gene OrientationCounterclockwise
Centisome Percentage:39.77
Left Sequence End1844989
Right Sequence End1846032
Gene Sequence:
>1044 bp
ATGCGTATTGAAGAAGATCTGAAGTTAGGTTTTAAAGACGTTCTCATCCGCCCTAAACGC
TCCACTCTTAAAAGCCGTTCCGATGTTGAACTGGAACGTCAATTCACCTTCAAACATTCA
GGTCAGAGCTGGTCCGGCGTGCCGATTATCGCCGCAAATATGGACACCGTAGGCACATTT
TCTATGGCCTCTGCGCTGGCTTCTTTTGATATTTTGACTGCTGTGCATAAACACTATTCT
GTCGAAGAGTGGCAAGCGTTTATCAACAATTCTTCCGCTGATGTGCTGAAACATGTGATG
GTTTCTACCGGTACGTCTGATGCGGATTTCGAAAAAACTAAACAGATTCTCGACCTGAAC
CCGGCATTAAACTTCGTTTGTATTGACGTGGCGAATGGTTATTCCGAACACTTCGTGCAG
TTCGTTGCGAAAGCGCGTGAAGCGTGGCCGACCAAAACCATTTGTGCTGGTAACGTAGTG
ACTGGTGAAATGTGTGAGGAGCTTATCCTCTCAGGTGCCGATATCGTTAAAGTTGGCATT
GGCCCAGGTTCTGTTTGTACAACTCGCGTCAAAACAGGCGTCGGTTATCCGCAACTTTCT
GCGGTAATCGAATGTGCCGATGCTGCGCACGGTCTGGGCGGAATGATCGTCAGCGATGGT
GGCTGCACCACGCCGGGCGATGTGGCGAAAGCCTTTGGCGGCGGTGCCGATTTCGTCATG
CTTGGCGGCATGCTGGCGGGCCACGAAGAGAGCGGCGGTCGCATCGTTGAGGAGAACGGC
GAGAAATTTATGCTGTTCTACGGCATGAGCTCCGAGTCTGCGATGAAACGTCACGTTGGC
GGCGTTGCGGAATATCGCGCAGCAGAAGGTAAAACCGTTAAGCTGCCGCTGCGAGGCCCG
GTTGAAAATACCGCGCGAGATATTTTGGGCGGCCTGCGTTCAGCTTGTACATACGTTGGG
GCTTCACGCCTGAAAGAGCTGACCAAGCGCACCACGTTTATTCGTGTGCAGGAACAAGAA
AACCGCATCTTCAACAACCTGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:347
Protein Molecular Weight:36687
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Selenide, water dikinase
MSENSIRLTQYSHGAGCGCKISPKVLETILHSEQAKFVDPNLLVGNETRDDAAVYDLGNG
TSVISTTDFFMPIVDNPFDFGRIAATNAISDIFAMGGKPIMAIAILGWPINKLSPEIARE
VTEGGRYACRQAGIALAGGHSIDAPEPIFGLAVTGIVPTERVKKNSTAQAGCKLFLTKPL
GIGVLTTAEKKSLLKPEHQGLATEVMCRMNIAGASFANIEGVKAMTDVTGFGLLGHLSEM
CQGAGVQARVDYEAIPKLPGVEEYIKLGAVPGGTERNFASYGHLMGEMPREVRDLLCDPQ
TSGGLLLAVMPEAENEVKATAAEFGIELTAIGELVPARGGRAMVEIR
References
External Links:
ResourceLink
Uniprot ID:P16456
Uniprot Name:SELD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674329
Ecogene ID:EG10943
Ecocyc:EG10943
ColiBase:b1764
Kegg Gene:b1764
EchoBASE ID:EB0936
CCDB:SELD_ECOLI
BacMap:16129718
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • DiGate, R. J., Marians, K. J. (1989). "Molecular cloning and DNA sequence analysis of Escherichia coli topB, the gene encoding topoisomerase III." J Biol Chem 264:17924-17930. Pubmed: 2553698
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Kim, I. Y., Veres, Z., Stadtman, T. C. (1992). "Escherichia coli mutant SELD enzymes. The cysteine 17 residue is essential for selenophosphate formation from ATP and selenide." J Biol Chem 267:19650-19654. Pubmed: 1527085
  • Kim, I. Y., Veres, Z., Stadtman, T. C. (1993). "Biochemical analysis of Escherichia coli selenophosphate synthetase mutants. Lysine 20 is essential for catalytic activity and cysteine 17/19 for 8-azido-ATP derivatization." J Biol Chem 268:27020-27025. Pubmed: 8262938
  • Leinfelder, W., Forchhammer, K., Veprek, B., Zehelein, E., Bock, A. (1990). "In vitro synthesis of selenocysteinyl-tRNA(UCA) from seryl-tRNA(UCA): involvement and characterization of the selD gene product." Proc Natl Acad Sci U S A 87:543-547. Pubmed: 2405383