D-galactarate dehydratase (P39829)

Identification
Name:D-galactarate dehydratase
Synonyms:
  • GalcD
Gene Name:garD
Enzyme Class:
Biological Properties
General Function:Involved in hydro-lyase activity
Specific Function:D-galactarate = 5-dehydro-4-deoxy-D-glucarate + H(2)O
Cellular Location:Not Available
SMPDB Pathways:
  • superpathway of D-glucarate and D-galactarate degradation PW000795
KEGG Pathways:
  • Ascorbate and aldarate metabolism ec00053
KEGG Reactions:
1.0D-Galactarate+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0D-Galactarate + 1.0Galactaric acid ↔ 1.05-Dehydro-4-deoxy-D-glucarate + 1.0Water
ReactionCard
SMPDB Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.0Galactaric acid → 1.0Water + 1.05-dehydro-4-deoxy-D-glucarate(2−)
ReactionCard
EcoCyc Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.0Galactaric acid → 1.05-Dehydro-4-deoxy-D-glucarate + 1.0Water
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB201025-Dehydro-4-deoxy-D-glucarateMetaboCard
ECMDB241965-dehydro-4-deoxy-D-glucarate(2−)MetaboCard
ECMDB00639Galactaric acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
carbon-oxygen lyase activity
catalytic activity
hydro-lyase activity
lyase activity
Gene Properties
Blattner:b3128
Gene OrientationClockwise
Centisome Percentage:70.55
Left Sequence End3273304
Right Sequence End3274875
Gene Sequence:
>1572 bp
ATGGCCAACATCGAAATCAGACAAGAAACGCCAACTGCGTTTTATATAAAAGTTCACGAC
ACAGATAATGTGGCAATTATTGTTAATGATAATGGCCTGAAAGCAGGAACGCGTTTTCCG
GATGGGCTGGAATTAATTGAACATATTCCCCAGGGGCATAAAGTCGCATTGCTGGACATT
CCGGCTAATGGTGAAATTATTCGTTATGGCGAAGTGATTGGTTACGCCGTGCGTGCAATC
CCACGCGGAAGCTGGATCGACGAATCAATGGTTGTACTACCGGAAGCGCCGCCGTTACAC
ACGCTGCCACTGGCAACCAAAGTCCCGGAACCCTTACCGCCGCTGGAAGGATACACCTTT
GAGGGCTATCGCAATGCCGATGGCAGCGTGGGCACCAAAAACCTGCTCGGTATCACCACC
AGCGTCCACTGTGTGGCAGGCGTGGTGGACTATGTAGTAAAAATCATTGAACGCGATCTG
CTACCGAAATACCCGAACGTCGATGGCGTGGTGGGGCTGAATCATTTGTACGGTTGTGGC
GTGGCGATTAACGCACCGGCGGCAGTTGTACCTATCCGTACCATTCACAATATTTCGCTG
AATCCTAACTTTGGCGGCGAAGTAATGGTGATTGGCCTGGGTTGTGAAAAGTTGCAGCCT
GAGCGCCTGCTGACTGGAACGGATGATGTGCAAGCTATTCCAGTAGAAAGCGCCAGCATT
GTCAGTTTGCAGGATGAAAAGCATGTCGGTTTTCAGTCCATGGTCGAGGATATTTTGCAG
ATCGCCGAACGCCATCTACAAAAACTGAATCAACGGCAGCGAGAAACCTGCCCGGCTTCA
GAACTGGTCGTTGGTATGCAGTGCGGTGGCAGCGATGCGTTTTCTGGTGTAACGGCAAAC
CCGGCGGTTGGCTATGCGTCTGATCTACTGGTGCGCTGCGGCGCAACGGTGATGTTTTCA
GAAGTAACGGAAGTGCGTGACGCGATCCATCTGCTGACACCACGCGCAGTGAACGAAGAG
GTCGGCAAACGGCTGCTGGAGGAGATGGAGTGGTACGATAACTATCTCAATATGGGAAAA
ACCGACCGCAGCGCCAACCCTTCGCCGGGCAACAAGAAAGGCGGTCTGGCAAACGTGGTA
GAGAAGGCACTCGGCTCCATTGCTAAATCGGGTAAAAGCGCAATTGTTGAAGTGCTGTCG
CCCGGTCAACGCCCGACTAAACGCGGATTAATTTACGCCGCGACGCCAGCCAGCGATTTT
GTCTGTGGCACGCAACAGGTGGCTTCGGGTATCACAGTGCAAGTGTTTACGACCGGTCGT
GGTACGCCGTACGGCCTGATGGCGGTACCCGTCATTAAAATGGCAACCCGCACCGAGCTG
GCGAACCGCTGGTTTGATTTAATGGATATTAATGCGGGCACCATCGCTACCGGCGAAGAA
ACTATTGAAGAGGTGGGCTGGAAGTTGTTCCACTTTATTCTCGACGTCGCCAGCGGGAAG
AAGAAAACCTTCTCGGATCAATGGGGGCTGCATAACCAGCTGGCGGTGTTTAACCCGGCA
CCGGTGACCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:523
Protein Molecular Weight:56401
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>D-galactarate dehydratase
MANIEIRQETPTAFYIKVHDTDNVAIIVNDNGLKAGTRFPDGLELIEHIPQGHKVALLDI
PANGEIIRYGEVIGYAVRAIPRGSWIDESMVVLPEAPPLHTLPLATKVPEPLPPLEGYTF
EGYRNADGSVGTKNLLGITTSVHCVAGVVDYVVKIIERDLLPKYPNVDGVVGLNHLYGCG
VAINAPAAVVPIRTIHNISLNPNFGGEVMVIGLGCEKLQPERLLTGTDDVQAIPVESASI
VSLQDEKHVGFQSMVEDILQIAERHLQKLNQRQRETCPASELVVGMQCGGSDAFSGVTAN
PAVGYASDLLVRCGATVMFSEVTEVRDAIHLLTPRAVNEEVGKRLLEEMEWYDNYLNMGK
TDRSANPSPGNKKGGLANVVEKALGSIAKSGKSAIVEVLSPGQRPTKRGLIYAATPASDF
VCGTQQVASGITVQVFTTGRGTPYGLMAVPVIKMATRTELANRWFDLMDINAGTIATGEE
TIEEVGWKLFHFILDVASGKKKTFSDQWGLHNQLAVFNPAPVT
References
External Links:
ResourceLink
Uniprot ID:P39829
Uniprot Name:GARD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675925
Ecogene ID:EG12522
Ecocyc:EG12522
ColiBase:b3128
Kegg Gene:b3128
EchoBASE ID:EB2413
CCDB:GARD_ECOLI
BacMap:16131020
General Reference:
  • Baird, L., Georgopoulos, C. (1990). "Identification, cloning, and characterization of the Escherichia coli sohA gene, a suppressor of the htrA (degP) null phenotype." J Bacteriol 172:1587-1594. Pubmed: 2407727
  • 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
  • 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
  • Monterrubio, R., Baldoma, L., Obradors, N., Aguilar, J., Badia, J. (2000). "A common regulator for the operons encoding the enzymes involved in D-galactarate, D-glucarate, and D-glycerate utilization in Escherichia coli." J Bacteriol 182:2672-2674. Pubmed: 10762278