Inosine-5'-monophosphate dehydrogenase (P0ADG7)

Identification
Name:Inosine-5'-monophosphate dehydrogenase
Synonyms:
  • IMP dehydrogenase
  • IMPD
  • IMPDH
Gene Name:guaB
Enzyme Class:
Biological Properties
General Function:Involved in catalytic activity
Specific Function:Inosine 5'-phosphate + NAD(+) + H(2)O = xanthosine 5'-phosphate + NADH
Cellular Location:Not Available
SMPDB Pathways:
  • purine nucleotides de novo biosynthesis PW000910
  • purine nucleotides de novo biosynthesis 1435709748 PW000960
  • purine nucleotides de novo biosynthesis 2 PW002033
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Water + 1.0Inosinic acid + 1.0NAD ↔ 1.0Hydrogen ion + 1.0NADH + 1.0Xanthylic acid
ReactionCard
1.06-Thioinosine-5'-monophosphate+1.0Thumb+1.0Thumb ↔ 1.06-Thioxanthine 5'-monophosphate+1.0Thumb+1.0Thumb
1.06-Thioinosine-5'-monophosphate + 1.0NAD + 1.0Water ↔ 1.06-Thioxanthine 5'-monophosphate + 1.0NADH + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Water + 1.0NAD + 1.0Inosinic acid → 1.0Hydrogen ion + 1.0NADH + 1.0Xanthylic acid
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Water + 1.0Inosinic acid + 1.0NAD ↔ 1.0Hydrogen ion + 1.0NADH + 1.0Xanthylic acid
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Water + 1.0NAD + 1.0Inosinic acid → 1.0Hydrogen ion + 1.0NADH + 1.0Xanthylic acid
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Inosinic acid + 1.0NAD + 1.0Water → 1.0Xanthylic acid + 1.0NADH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB21225Hydrogen ionMetaboCard
ECMDB04085Inosinic acidMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB00494WaterMetaboCard
ECMDB01554Xanthylic acidMetaboCard
GO Classification:
Function
catalytic activity
IMP dehydrogenase activity
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Process
metabolic process
oxidation reduction
Gene Properties
Blattner:b2508
Gene OrientationCounterclockwise
Centisome Percentage:56.70
Left Sequence End2630626
Right Sequence End2632092
Gene Sequence:
>1467 bp
ATGAATACAATCGCCTCCGTTACGCTCCCGCATCATGTACACGCTCCACGCTATGATCGC
CAGCAGTTGCAATCACGTATCGTTCATTTTGGCTTTGGAGCCTTTCACCGCGCTCATCAG
GCGTTACTGACCGATCGTGTGCTGAATGCCCAGGGCGGCGACTGGGGGATCTGTGAAATC
AGCTTGTTCAGCGGTGATCAACTGATGAGCCAGCTCCGCGCACAGAACCATTTATATACC
GTGCTGGAGAAAGGTGCGGACGGCAATCAGGTGATAATTGTCGGTGCCGTTCACGAATGC
CTTAATGCAAAACTGGATTCCTTAGCGGCAATTATTGAGAAATTTTGCGAGCCACAGGTG
GCAATTGTTTCCCTGACGATTACCGAAAAAGGCTATTGTATTGACCCGGCCACCGGTGCA
CTCGACACCAGTAATCCGCGGATTATTCACGATCTACAAACCCCTGAAGAACCTCACTCC
GCACCGGGTATTCTCGTCGAAGCACTGAAACGCCGCCGTGAGCGCGGCCTTACACCGTTT
ACCGTGCTCTCCTGCGACAATATTCCCGACAATGGTCATGTGGTGAAAAACGCGGTGCTG
GGAATGGCAGAAAAACGTTCGCCAGAACTCGCCGGGTGGATAAAAGAGCACGTCAGTTTT
CCGGGAACCATGGTCGACCGCATTGTTCCGGCTGCAACCGACGAATCACTGGTGGAAATC
AGCCAGCATCTGGGGGTGAATGATCCCTGCGCGATTAGCTGCGAACCGTTTATCCAGTGG
GTGGTGGAAGATAACTTCGTCGCTGGGCGTCCTGCCTGGGAAGTCGCAGGTGTACAAATG
GTGAATGATGTCCTGCCATGGGAAGAGATGAAACTGCGGATGCTTAATGGCAGCCACTCT
TTTCTCGCTTATCTGGGTTACCTCTCAGGATTCGCCCATATCAGTGATTGCATGCAGGAT
CGCGCATTTCGCCATGCCGCCAGAACATTAATGCTGGATGAGCAAGCGCCGACACTGCAA
ATTAAAGATGTCGATTTAACACAATATGCGGATAAGTTAATTGCACGTTTTGCTAATCCG
GCGCTGAAACATAAGACCTGGCAAATCGCGATGGATGGCAGCCAGAAATTACCGCAACGC
ATGCTGGCAGGTATTCGCATACATCAGGGGCGCGAAACGGACTGGTCGTTGCTGGCATTA
GGCGTTGCAGGCTGGATGCGTTACGTCAGCGGCGTTGATGATGCCGGAAATGCCATTGAT
GTTCGCGATCCGCTTAGCGATAAAATTCGCGAACTTGTTGCGGGCAGCAGCAGTGAACAA
CGCGTAACCGCCCTGCTTTCCCTGCGTGAAGTTTTCGGTGATGATCTGCCAGATAACCCG
CATTTTGTGCAGGCCATCGAACAAGCCTGGCAACAAATCGTACAATTCGGCGCACATCAG
GCGCTATTAAACACCCTCAAAATTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:488
Protein Molecular Weight:52022
Protein Theoretical pI:6
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Inosine-5'-monophosphate dehydrogenase
MLRIAKEALTFDDVLLVPAHSTVLPNTADLSTQLTKTIRLNIPMLSAAMDTVTEARLAIA
LAQEGGIGFIHKNMSIERQAEEVRRVKKHESGVVTDPQTVLPTTTLREVKELTERNGFAG
YPVVTEENELVGIITGRDVRFVTDLNQPVSVYMTPKERLVTVREGEAREVVLAKMHEKRV
EKALVVDDEFHLIGMITVKDFQKAERKPNACKDEQGRLRVGAAVGAGAGNEERVDALVAA
GVDVLLIDSSHGHSEGVLQRIRETRAKYPDLQIIGGNVATAAGARALAEAGCSAVKVGIG
PGSICTTRIVTGVGVPQITAVADAVEALEGTGIPVIADGGIRFSGDIAKAIAAGASAVMV
GSMLAGTEESPGEIELYQGRSYKSYRGMGSLGAMSKGSSDRYFQSDNAADKLVPEGIEGR
VAYKGRLKEIIHQQMGGLRSCMGLTGCGTIDELRTKAEFVRISGAGIQESHVHDVTITKE
SPNYRLGS
References
External Links:
ResourceLink
Uniprot ID:P0ADG7
Uniprot Name:IMDH_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675285
Ecogene ID:EG10421
Ecocyc:EG10421
ColiBase:b2508
Kegg Gene:b2508
EchoBASE ID:EB0416
CCDB:IMDH_ECOLI
BacMap:16130433
General Reference:
  • 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
  • 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
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Molloy, M. P., Herbert, B. R., Walsh, B. J., Tyler, M. I., Traini, M., Sanchez, J. C., Hochstrasser, D. F., Williams, K. L., Gooley, A. A. (1998). "Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis." Electrophoresis 19:837-844. Pubmed: 9629924
  • Tesfa-Selase, F., Drabble, W. T. (1992). "Regulation of the gua operon of Escherichia coli by the DnaA protein." Mol Gen Genet 231:256-264. Pubmed: 1736096
  • Thomas, M. S., Drabble, W. T. (1985). "Nucleotide sequence and organisation of the gua promoter region of Escherichia coli." Gene 36:45-53. Pubmed: 2998937
  • Tiedeman, A. A., Smith, J. M. (1985). "Nucleotide sequence of the guaB locus encoding IMP dehydrogenase of Escherichia coli K12." Nucleic Acids Res 13:1303-1316. Pubmed: 2860637
  • Wilkins, M. R., Gasteiger, E., Tonella, L., Ou, K., Tyler, M., Sanchez, J. C., Gooley, A. A., Walsh, B. J., Bairoch, A., Appel, R. D., Williams, K. L., Hochstrasser, D. F. (1998). "Protein identification with N and C-terminal sequence tags in proteome projects." J Mol Biol 278:599-608. Pubmed: 9600841
  • Yamamoto, Y., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kimura, S., Kitagawa, M., Makino, K., Miki, T., Mitsuhashi, N., Mizobuchi, K., Mori, H., Nakade, S., Nakamura, Y., Nashimoto, H., Oshima, T., Oyama, S., Saito, N., Sampei, G., Satoh, Y., Sivasundaram, S., Tagami, H., Horiuchi, T., et, a. l. .. (1997). "Construction of a contiguous 874-kb sequence of the Escherichia coli -K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." DNA Res 4:91-113. Pubmed: 9205837
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842