Glucarate dehydratase (P0AES2)

Identification
Name:Glucarate dehydratase
Synonyms:
  • GDH
  • GlucD
Gene Name:gudD
Enzyme Class:
Biological Properties
General Function:Involved in magnesium ion binding
Specific Function:Catalyzes the dehydration of glucarate to 5-keto-4- deoxy-D-glucarate (5-kdGluc). Also acts on L-idarate
Cellular Location:Not Available
SMPDB Pathways:
  • superpathway of D-glucarate and D-galactarate degradation PW000795
KEGG Pathways:
KEGG Reactions:
1.0D-Glucarate+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0D-Glucarate + 1.0Glucaric acid ↔ 1.05-Dehydro-4-deoxy-D-glucarate + 1.0Water
ReactionCard
1.0D-Glucarate ↔ 1.0Thumb+1.0Thumb
1.0D-Glucarate ↔ 1.02-Dehydro-3-deoxy-D-glucarate + 1.0Water
ReactionCard
SMPDB Reactions:
1.0D-Glucaric acid+1.0Thumb → 1.0Thumb+1.0Thumb
1.0D-Glucaric acid + 1.0Glucaric acid → 1.0Water + 1.05-dehydro-4-deoxy-D-glucarate(2−)
ReactionCard
1.0D-glucarate → 1.0Thumb+1.0Thumb
1.0D-glucarate → 1.05-dehydro-4-deoxy-D-glucarate(2−) + 1.0Water
ReactionCard
1.0Thumb → 1.0Thumb+1.0Thumb
1.0Glucaric acid → 1.0Water + 1.02-Dehydro-3-deoxy-D-glucarate
ReactionCard
EcoCyc Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.0Glucaric acid → 1.05-Dehydro-4-deoxy-D-glucarate + 1.0Water
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB200402-Dehydro-3-deoxy-D-glucarateMetaboCard
ECMDB201025-Dehydro-4-deoxy-D-glucarateMetaboCard
ECMDB241965-dehydro-4-deoxy-D-glucarate(2−)MetaboCard
ECMDB00663Glucaric acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
carbon-oxygen lyase activity
catalytic activity
cation binding
glucarate dehydratase activity
hydro-lyase activity
ion binding
lyase activity
magnesium ion binding
metal ion binding
Process
aldaric acid metabolic process
carbohydrate metabolic process
glucarate catabolic process
glucarate metabolic process
metabolic process
primary metabolic process
Gene Properties
Blattner:b2787
Gene OrientationCounterclockwise
Centisome Percentage:62.85
Left Sequence End2916067
Right Sequence End2917407
Gene Sequence:
>1341 bp
ATGAGTTCTCAATTTACGACGCCTGTTGTTACTGAAATGCAGGTTATCCCGGTGGCGGGT
CATGACAGTATGCTGATGAATCTGAGTGGTGCACACGCACCGTTCTTTACGCGTAATATT
GTGATTATCAAAGATAATTCTGGTCACACTGGCGTAGGGGAAATTCCCGGCGGCGAGAAA
ATCCGTAAAACGCTGGAAGATGCGATTCCGCTGGTGGTAGGTAAAACGCTGGGTGAATAC
AAAAACGTTCTGACGCTGGTGCGTAATACTTTTGCCGATCGTGATGCTGGTGGGCGCGGT
TTGCAGACATTTGACCTACGTACCACTATTCATGTAGTTACCGGGATAGAAGCGGCAATG
CTGGATCTGCTGGGGCAGCATCTGGGGGTAAACGTGGCATCGCTGCTGGGCGATGGTCAA
CAGCGTAGCGAAGTCGAAATGCTCGGTTATCTGTTCTTCGTCGGTAATCGCAAAGCCACG
CCGCTGCCGTATCAAAGCCAGCCGGATGACTCATGCGACTGGTATCGCCTGCGTCATGAA
GAAGCGATGACGCCGGATGCGGTGGTGCGCCTGGCGGAAGCGGCATATGAAAAATATGGC
TTCAACGATTTCAAACTGAAGGGCGGTGTACTGGCCGGGGAAGAAGAGGCCGAGTCTATT
GTGGCACTGGCGCAACGCTTCCCGCAGGCGCGTATTACGCTCGATCCTAACGGTGCCTGG
TCGCTGAACGAAGCGATTAAAATCGGTAAATACCTGAAAGGTTCGCTGGCTTATGCAGAA
GATCCGTGTGGTGCGGAGCAAGGTTTCTCCGGGCGTGAAGTGATGGCAGAGTTCCGTCGC
GCGACAGGTCTACCGACTGCAACCAATATGATCGCCACCGACTGGCGGCAAATGGGCCAT
ACGCTCTCCCTGCAATCCGTTGATATCCCGCTGGCGGATCCGCATTTCTGGACAATGCAA
GGTTCGGTACGTGTGGCGCAAATGTGCCATGAATTTGGCCTGACCTGGGGTTCACACTCT
AACAACCACTTCGATATTTCCCTGGCGATGTTTACCCATGTTGCCGCCGCTGCACCGGGT
AAAATTACTGCTATTGATACGCACTGGATTTGGCAGGAAGGCAATCAGCGCCTGACCAAA
GAACCGTTTGAGATCAAAGGCGGGCTGGTACAGGTGCCAGAAAAACCGGGGCTGGGTGTA
GAAATCGATATGGATCAAGTGATGAAAGCCCATGAGCTGTATCAGAAACACGGGCTTGGC
GCGCGTGACGATGCGATGGGAATGCAGTATCTGATTCCTGGCTGGACGTTCGATAACAAG
CGCCCGTGCATGGTGCGTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:446
Protein Molecular Weight:49141
Protein Theoretical pI:6
PDB File:1EC7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Glucarate dehydratase
MSSQFTTPVVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIKDNSGHTGVGEIPGGEK
IRKTLEDAIPLVVGKTLGEYKNVLTLVRNTFADRDAGGRGLQTFDLRTTIHVVTGIEAAM
LDLLGQHLGVNVASLLGDGQQRSEVEMLGYLFFVGNRKATPLPYQSQPDDSCDWYRLRHE
EAMTPDAVVRLAEAAYEKYGFNDFKLKGGVLAGEEEAESIVALAQRFPQARITLDPNGAW
SLNEAIKIGKYLKGSLAYAEDPCGAEQGFSGREVMAEFRRATGLPTATNMIATDWRQMGH
TLSLQSVDIPLADPHFWTMQGSVRVAQMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPG
KITAIDTHWIWQEGNQRLTKEPFEIKGGLVQVPEKPGLGVEIDMDQVMKAHELYQKHGLG
ARDDAMGMQYLIPGWTFDNKRPCMVR
References
External Links:
ResourceLink
Uniprot ID:P0AES2
Uniprot Name:GUDH_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675606
PDB ID:1EC7
Ecogene ID:EG13167
Ecocyc:EG13167
ColiBase:b2787
Kegg Gene:b2787
EchoBASE ID:EB2959
CCDB:GUDH_ECOLI
BacMap:16130694
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
  • Gulick, A. M., Hubbard, B. K., Gerlt, J. A., Rayment, I. (2000). "Evolution of enzymatic activities in the enolase superfamily: crystallographic and mutagenesis studies of the reaction catalyzed by D-glucarate dehydratase from Escherichia coli." Biochemistry 39:4590-4602. Pubmed: 10769114
  • Gulick, A. M., Hubbard, B. K., Gerlt, J. A., Rayment, I. (2001). "Evolution of enzymatic activities in the enolase superfamily: identification of the general acid catalyst in the active site of D-glucarate dehydratase from Escherichia coli." Biochemistry 40:10054-10062. Pubmed: 11513584
  • 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
  • Hubbard, B. K., Koch, M., Palmer, D. R., Babbitt, P. C., Gerlt, J. A. (1998). "Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli." Biochemistry 37:14369-14375. Pubmed: 9772162
  • 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