T3DB: Glucarate dehydratase

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 magnesium ion binding glucarate dehydratase activity 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	MR_MLE_C (PF13378 )
Transmembrane Regions	Not Available
GenBank Protein ID	1786182
UniProtKB ID	P0AES2
UniProtKB Entry Name	GUDD_ECOLI
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
GenBank Gene ID	U00096
GeneCard ID	Not Available
GenAtlas ID	Not Available
HGNC ID	Not Available
Chromosome Location	Not Available
Locus	Not Available
References	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. 9278503 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. 16738553 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. 9205837 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. 9772162 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. 10769114 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. 11513584