Glucarate dehydratase

Details

Name
Glucarate dehydratase
Synonyms
  • 4.2.1.40
  • GDH
  • ygcX
Gene Name
gudD
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0011469|Glucarate dehydratase
MSSQFTTPVVTEMQVIPVAGHDSMLMNLSGAHAPFFTRNIVIIKDNSGHTGVGEIPGGEK
IRKTLEDAIPLVVGKTLGEYKNVLTLVRNTFADRDAGGRGLQTFDLRTTIHVVTGIEAAM
LDLLGQHLGVNVASLLGDGQQRSEVEMLGYLFFVGNRKATPLPYQSQPDDSCDWYRLRHE
EAMTPDAVVRLAEAAYEKYGFNDFKLKGGVLAGEEEAESIVALAQRFPQARITLDPNGAW
SLNEAIKIGKYLKGSLAYAEDPCGAEQGFSGREVMAEFRRATGLPTATNMIATDWRQMGH
TLSLQSVDIPLADPHFWTMQGSVRVAQMCHEFGLTWGSHSNNHFDISLAMFTHVAAAAPG
KITAIDTHWIWQEGNQRLTKEPFEIKGGLVQVPEKPGLGVEIDMDQVMKAHELYQKHGLG
ARDDAMGMQYLIPGWTFDNKRPCMVR
Number of residues
446
Molecular Weight
49140.715
Theoretical pI
5.99
GO Classification
Functions
glucarate dehydratase activity / magnesium ion binding
Processes
D-glucarate catabolic process
General Function
Magnesium ion binding
Specific Function
Catalyzes the dehydration of glucarate to 5-keto-4-deoxy-D-glucarate (5-kdGluc). Also acts on L-idarate.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0011470|Glucarate dehydratase (gudD)
ATGAGTTCTCAATTTACGACGCCTGTTGTTACTGAAATGCAGGTTATCCCGGTGGCGGGT
CATGACAGTATGCTGATGAATCTGAGTGGTGCACACGCACCGTTCTTTACGCGTAATATT
GTGATTATCAAAGATAATTCTGGTCACACTGGCGTAGGGGAAATTCCCGGCGGCGAGAAA
ATCCGTAAAACGCTGGAAGATGCGATTCCGCTGGTGGTAGGTAAAACGCTGGGTGAATAC
AAAAACGTTCTGACGCTGGTGCGTAATACTTTTGCCGATCGTGATGCTGGTGGGCGCGGT
TTGCAGACATTTGACCTACGTACCACTATTCATGTAGTTACCGGGATAGAAGCGGCAATG
CTGGATCTGCTGGGGCAGCATCTGGGGGTAAACGTGGCATCGCTGCTGGGCGATGGTCAA
CAGCGTAGCGAAGTCGAAATGCTCGGTTATCTGTTCTTCGTCGGTAATCGCAAAGCCACG
CCGCTGCCGTATCAAAGCCAGCCGGATGACTCATGCGACTGGTATCGCCTGCGTCATGAA
GAAGCGATGACGCCGGATGCGGTGGTGCGCCTGGCGGAAGCGGCATATGAAAAATATGGC
TTCAACGATTTCAAACTGAAGGGCGGTGTACTGGCCGGGGAAGAAGAGGCCGAGTCTATT
GTGGCACTGGCGCAACGCTTCCCGCAGGCGCGTATTACGCTCGATCCTAACGGTGCCTGG
TCGCTGAACGAAGCGATTAAAATCGGTAAATACCTGAAAGGTTCGCTGGCTTATGCAGAA
GATCCGTGTGGTGCGGAGCAAGGTTTCTCCGGGCGTGAAGTGATGGCAGAGTTCCGTCGC
GCGACAGGTCTACCGACTGCAACCAATATGATCGCCACCGACTGGCGGCAAATGGGCCAT
ACGCTCTCCCTGCAATCCGTTGATATCCCGCTGGCGGATCCGCATTTCTGGACAATGCAA
GGTTCGGTACGTGTGGCGCAAATGTGCCATGAATTTGGCCTGACCTGGGGTTCACACTCT
AACAACCACTTCGATATTTCCCTGGCGATGTTTACCCATGTTGCCGCCGCTGCACCGGGT
AAAATTACTGCTATTGATACGCACTGGATTTGGCAGGAAGGCAATCAGCGCCTGACCAAA
GAACCGTTTGAGATCAAAGGCGGGCTGGTACAGGTGCCAGAAAAACCGGGGCTGGGTGTA
GAAATCGATATGGATCAAGTGATGAAAGCCCATGAGCTGTATCAGAAACACGGGCTTGGC
GCGCGTGACGATGCGATGGGAATGCAGTATCTGATTCCTGGCTGGACGTTCGATAACAAG
CGCCCGTGCATGGTGCGTTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0AES2
UniProtKB Entry NameGUDD_ECOLI
GenBank Protein ID1786182
GenBank Gene IDU00096
General References
  1. 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]
  2. 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]
  3. 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 al.: 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. 1997 Apr 28;4(2):91-113. [Article]
  4. Hubbard BK, Koch M, Palmer DR, Babbitt PC, Gerlt JA: Evolution of enzymatic activities in the enolase superfamily: characterization of the (D)-glucarate/galactarate catabolic pathway in Escherichia coli. Biochemistry. 1998 Oct 13;37(41):14369-75. [Article]
  5. Gulick AM, Hubbard BK, Gerlt JA, Rayment I: Evolution of enzymatic activities in the enolase superfamily: crystallographic and mutagenesis studies of the reaction catalyzed by D-glucarate dehydratase from Escherichia coli. Biochemistry. 2000 Apr 25;39(16):4590-602. [Article]
  6. Gulick AM, Hubbard BK, Gerlt JA, Rayment I: 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. 2001 Aug 28;40(34):10054-62. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB032124-DeoxyglucarateexperimentalunknownDetails
DB032372,3-Dihydroxy-5-Oxo-HexanedioateexperimentalunknownDetails
DB03603Glucaric acidexperimentalunknownDetails
DB03734XylarohydroxamateexperimentalunknownDetails