2-iminobutanoate/2-iminopropanoate deaminase

Details

Name
2-iminobutanoate/2-iminopropanoate deaminase
Synonyms
  • 3.5.99.10
  • Enamine/imine deaminase
  • yjgF
Gene Name
ridA
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0004074|2-iminobutanoate/2-iminopropanoate deaminase
MSKTIATENAPAAIGPYVQGVDLGNMIITSGQIPVNPKTGEVPADVAAQARQSLDNVKAI
VEAAGLKVGDIVKTTVFVKDLNDFATVNATYEAFFTEHNATFPARSCVEVARLPKDVKIE
IEAIAVRR
Number of residues
128
Molecular Weight
13611.475
Theoretical pI
5.16
GO Classification
Functions
deaminase activity / hydrolase activity / identical protein binding / unfolded protein binding
Processes
isoleucine biosynthetic process / response to toxic substance
Components
cytosol / membrane
General Function
Unfolded protein binding
Specific Function
Accelerates the release of ammonia from reactive enamine/imine intermediates of the PLP-dependent threonine dehydratase (IlvA) in the low water environment of the cell. It catalyzes the deamination of enamine/imine intermediates to yield 2-ketobutyrate and ammonia. It is required for the detoxification of reactive intermediates of IlvA due to their highly nucleophilic abilities. Involved in the isoleucine biosynthesis (By similarity).
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0019231|2-iminobutanoate/2-iminopropanoate deaminase (ridA)
ATGAGCAAAACTATCGCGACGGAAAATGCACCGGCAGCTATCGGTCCTTACGTACAGGGC
GTTGATCTGGGCAATATGATCATCACCTCCGGTCAGATCCCGGTAAATCCGAAAACGGGC
GAAGTACCGGCAGACGTCGCTGCACAGGCACGTCAGTCGCTGGATAACGTAAAAGCGATC
GTCGAAGCCGCTGGCCTGAAAGTGGGCGACATCGTTAAAACTACCGTGTTTGTAAAAGAT
CTGAACGACTTCGCAACCGTAAACGCCACTTACGAAGCCTTCTTCACCGAACACAACGCC
ACCTTCCCGGCACGTTCTTGCGTTGAAGTTGCCCGTCTGCCGAAAGACGTGAAGATTGAG
ATCGAAGCGATCGCTGTTCGTCGCTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0AF93
UniProtKB Entry NameRIDA_ECOLI
GenBank Gene IDU14003
General References
  1. Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. [Article]
  2. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  3. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  4. Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
  5. Fountoulakis M, Takacs MF, Berndt P, Langen H, Takacs B: Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite chromatography. Electrophoresis. 1999 Aug;20(11):2181-95. [Article]
  6. Volz K: A test case for structure-based functional assignment: the 1.2 A crystal structure of the yjgF gene product from Escherichia coli. Protein Sci. 1999 Nov;8(11):2428-37. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB03544S-PhosphocysteineexperimentalunknownDetails