dTDP-glucose 4,6-dehydratase 2 (P27830)

Identification
Name:dTDP-glucose 4,6-dehydratase 2
Synonyms:Not Available
Gene Name:rffG
Enzyme Class:
Biological Properties
General Function:Involved in dTDP-glucose 4,6-dehydratase activity
Specific Function:Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6-deoxy-D-xylo-4-hexulose via a three-step process involving oxidation, dehydration and reduction
Cellular Location:Not Available
SMPDB Pathways:
  • Secondary Metabolites: enterobacterial common antigen biosynthesis PW000959
  • Secondary Metabolites: enterobacterial common antigen biosynthesis 2 PW002045
  • Secondary Metabolites: enterobacterial common antigen biosynthesis 3 PW002046
  • Starch and sucrose metabolism PW000941
KEGG Pathways:
KEGG Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0dTDP-D-Glucose ↔ 1.04,6-Dideoxy-4-oxo-dTDP-D-glucose + 1.0Water
ReactionCard
SMPDB Reactions:
1.0Thumb → 1.0dTDP-4-dehydro-6-deoxy-D-glucose+1.0Thumb
1.0dTDP-D-Glucose → 1.0dTDP-4-dehydro-6-deoxy-D-glucose + 1.0Water
ReactionCard
1.0Thumb → 1.0dTDP-4-dehydro-6-deoxy-D-glucose+1.0Thumb
1.0TDP-Glucose → 1.0dTDP-4-dehydro-6-deoxy-D-glucose + 1.0Water
ReactionCard
EcoCyc Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0dTDP-D-Glucose ↔ 1.04,6-Dideoxy-4-oxo-dTDP-D-glucose + 1.0Water
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB013994,6-Dideoxy-4-oxo-dTDP-D-glucoseMetaboCard
ECMDB01328dTDP-D-GlucoseMetaboCard
ECMDB20298TDP-GlucoseMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
carbon-oxygen lyase activity
catalytic activity
coenzyme binding
cofactor binding
dTDP-glucose 4,6-dehydratase activity
hydro-lyase activity
lyase activity
Process
cellular metabolic process
cellular nitrogen compound metabolic process
metabolic process
nitrogen compound metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleotide-sugar metabolic process
Gene Properties
Blattner:b3788
Gene OrientationClockwise
Centisome Percentage:85.58
Left Sequence End3970545
Right Sequence End3971612
Gene Sequence:
>1068 bp
ATGAGTGGTCAAGGAAAGCGATTAATGGTGATGGCAGGCGGAACCGGTGGACATGTATTC
CCGGGACTGGCGGTTGCGCACCATCTAATGGCTCAGGGTTGGCAAGTTCGCTGGCTGGGG
ACTGCCGACCGTATGGAAGCGGACTTAGTGCCAAAACATGGCATCGAAATTGATTTCATT
CGTATCTCTGGTCTGCGTGGAAAAGGTATAAAAGCACTGATAGCTGCCCCGCTGCGTATC
TTCAACGCCTGGCGTCAGGCGCGGGCGATTATGAAAGCGTACAAACCTGACGTGGTGCTC
GGTATGGGAGGCTACGTGTCAGGTCCAGGTGGTCTGGCCGCGTGGTCGTTAGGCATTCCG
GTTGTACTTCATGAACAAAACGGTATTGCGGGCTTAACCAATAAATGGCTGGCGAAGATT
GCCACCAAAGTGATGCAGGCGTTTCCAGGTGCTTTCCCTAATGCGGAAGTAGTGGGTAAC
CCGGTGCGTACCGATGTGTTGGCGCTGCCGTTGCCGCAGCAACGTTTGGCTGGACGTGAA
GGTCCGGTTCGTGTGCTGGTAGTGGGTGGTTCTCAGGGCGCACGCATTCTTAACCAGACA
ATGCCGCAGGTTGCTGCGAAACTGGGTGATTCAGTCACTATCTGGCATCAGAGCGGCAAA
GGTTCGCAACAATCCGTTGAACAGGCGTATGCCGAAGCGGGGCAACCGCAGCATAAAGTG
ACGGAATTTATTGATGATATGGCGGCGGCGTATGCGTGGGCGGATGTCGTCGTTTGCCGC
TCCGGTGCGTTAACGGTGAGTGAAATCGCCGCGGCAGGACTACCGGCGTTGTTTGTGCCG
TTTCAACATAAAGACCGCCAGCAATACTGGAATGCGCTACCGCTGGAAAAAGCGGGCGCA
GCCAAAATTATCGAGCAGCCACAGCTTAGCGTGGATGCTGTCGCCAACACCCTGGCCGGG
TGGTCGCGAGAAACCTTATTAACCATGGCAGAACGCGCCCGCGCTGCATCCATTCCGGAT
GCCACCGAGCGAGTGGCAAATGAAGTGAGCCGGGTTGCCCGGGCGTAA
Protein Properties
Pfam Domain Function:
Protein Residues:355
Protein Molecular Weight:39754
Protein Theoretical pI:6
PDB File:1BXK
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>dTDP-glucose 4,6-dehydratase 2
MRKILITGGAGFIGSALVRYIINETSDAVVVVDKLTYAGNLMSLAPVAQSERFAFEKVDI
CDRAELARVFTEHQPDCVMHLAAESHVDRSIDGPAAFIETNIVGTYTLLEAARAYWNALT
EDKKSAFRFHHISTDEVYGDLHSTDDFFTETTPYAPSSPYSASKASSDHLVRAWLRTYGL
PTLITNCSNNYGPYHFPEKLIPLMILNALAGKSLPVYGNGQQIRDWLYVEDHARALYCVA
TTGKVGETYNIGGHNERKNLDVVETICELLEELAPNKPHGVAHYRDLITFVADRPGHDLR
YAIDASKIARELGWLPQETFESGMRKTVQWYLANESWWKQVQDGSYQGERLGLKG
References
External Links:
ResourceLink
Uniprot ID:P27830
Uniprot Name:RMLB2_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:21321971
PDB ID:1BXK
Ecogene ID:EG11453
Ecocyc:EG11453
ColiBase:b3788
Kegg Gene:b3788
EchoBASE ID:EB1422
CCDB:RMLB2_ECOLI
BacMap:49176411
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
  • Daniels, D. L., Plunkett, G. 3rd, Burland, V., Blattner, F. R. (1992). "Analysis of the Escherichia coli genome: DNA sequence of the region from 84.5 to 86.5 minutes." Science 257:771-778. Pubmed: 1379743
  • Gross, J. W., Hegeman, A. D., Gerratana, B., Frey, P. A. (2001). "Dehydration is catalyzed by glutamate-136 and aspartic acid-135 active site residues in Escherichia coli dTDP-glucose 4,6-dehydratase." Biochemistry 40:12497-12504. Pubmed: 11601973
  • 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
  • Hegeman, A. D., Gross, J. W., Frey, P. A. (2001). "Probing catalysis by Escherichia coli dTDP-glucose-4,6-dehydratase: identification and preliminary characterization of functional amino acid residues at the active site." Biochemistry 40:6598-6610. Pubmed: 11380254
  • Marolda, C. L., Valvano, M. A. (1995). "Genetic analysis of the dTDP-rhamnose biosynthesis region of the Escherichia coli VW187 (O7:K1) rfb gene cluster: identification of functional homologs of rfbB and rfbA in the rff cluster and correct location of the rffE gene." J Bacteriol 177:5539-5546. Pubmed: 7559340
  • Riley, M., Abe, T., Arnaud, M. B., Berlyn, M. K., Blattner, F. R., Chaudhuri, R. R., Glasner, J. D., Horiuchi, T., Keseler, I. M., Kosuge, T., Mori, H., Perna, N. T., Plunkett, G. 3rd, Rudd, K. E., Serres, M. H., Thomas, G. H., Thomson, N. R., Wishart, D., Wanner, B. L. (2006). "Escherichia coli K-12: a cooperatively developed annotation snapshot--2005." Nucleic Acids Res 34:1-9. Pubmed: 16397293