D-malate dehydrogenase [decarboxylating] (P76251)

Identification
Name:D-malate dehydrogenase [decarboxylating]
Synonyms:
  • D-malate degradation protein A
  • D-malate oxidase
Gene Name:dmlA
Enzyme Class:
Biological Properties
General Function:Involved in magnesium ion binding
Specific Function:Catalyzes the NAD(+)-dependent oxidative decarboxylation of D-malate into pyruvate. Is essential for aerobic growth on D- malate as the sole carbon source. But is not required for anaerobic D-malate utilization, although DmlA is expressed and active in those conditions. Appears to be not able to use L- tartrate as a substrate for dehydrogenation instead of D-malate
Cellular Location:Cytoplasm
SMPDB Pathways:
  • Leucine Biosynthesis PW000811
  • Secondary Metabolite: Leucine biosynthesis PW000980
  • Secondary Metabolites: Valine and I-leucine biosynthesis from pyruvate PW000978
  • glycolate and glyoxylate degradation II PW002021
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0(R)-Malate + 1.0NAD ↔ 1.0Carbon dioxide + 1.0NADH + 1.0Pyruvic acid
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0(R)-Malate + 1.0NAD ↔ 1.0Pyruvic acid + 1.0Carbon dioxide + 1.0NADH + 1.0Hydrogen ion
ReactionCard
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Tartaric acid ↔ 1.0Glyceric acid + 1.0Carbon dioxide
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Meso-Tartaric acid + 1.0NAD ↔ 1.02-Hydroxy-3-oxosuccinate + 1.0NADH + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0Tartaric acid + 1.0NAD ↔ 1.02-Hydroxy-3-oxosuccinate + 1.0NADH + 1.0Hydrogen ion
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0(R)-Malate + 1.0NAD ↔ 1.0Carbon dioxide + 1.0NADH + 1.0Pyruvic acid
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0(R)-Malate + 1.0NAD ↔ 1.0Pyruvic acid + 1.0Carbon dioxide + 1.0NADH + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0NAD + 1.0(R)-Malate → 1.0NADH + 1.0Carbon dioxide + 1.0Pyruvic acid
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB20015(R)-MalateMetaboCard
ECMDB040802-Hydroxy-3-oxosuccinateMetaboCard
ECMDB121492-Isopropyl-3-oxosuccinateMetaboCard
ECMDB041583-IsopropylmalateMetaboCard
ECMDB04030Carbon dioxideMetaboCard
ECMDB04077Glyceric acidMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB20172Meso-Tartaric acidMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB00243Pyruvic acidMetaboCard
ECMDB00956Tartaric acidMetaboCard
GO Classification:
Function
binding
catalytic activity
cation binding
ion binding
magnesium ion binding
metal ion binding
NAD or NADH binding
nucleotide binding
oxidoreductase activity
oxidoreductase activity, acting on CH-OH group of donors
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
tartrate dehydrogenase activity
Process
metabolic process
oxidation reduction
Gene Properties
Blattner:b1800
Gene OrientationClockwise
Centisome Percentage:40.52
Left Sequence End1879936
Right Sequence End1881021
Gene Sequence:
>1086 bp
ATGGAAAGTGGTCATCGCTTTGATGCTCAGACGCTGCACAGTTTTATTCAGGCTGTATTT
CGTCAGATGGGTAGCGAGGAACAAGAAGCGAAATTAGTTGCCGATCATTTAATCGCGGCA
AACCTGGCAGGGCATGATTCACATGGTATTGGCATGATCCCAAGCTATGTACGCTCCTGG
AGTCAGGGGCACCTGCAAATTAACCATCATGCCAAAACCGTTAAAGAGGCGGGGGCGGCG
GTCACGCTCGATGGCGATCGCGCATTTGGTCAGGTCGCGGCACATGAAGCGATGGCGCTG
GGGATTGAGAAAGCGCATCAGCACGGTATTGCCGCCGTGGCGCTACATAACTCGCATCAT
ATCGGCCGTATCGGTTACTGGGCGGAGCAGTGTGCAGCGGCGGGGTTTGTCTCTATCCAC
TTTGTTAGCGTGGTCGGTATTCCAATGGTCGCGCCGTTCCACGGTCGCGACAGCCGCTTT
GGCACCAATCCGTTCTGTGTGGTTTTCCCTCGTAAAGATAATTTCCCGCTGTTGCTTGAT
TACGCCACCAGCGCCATTGCATTTGGCAAAACCCGCGTCGCCTGGCATAAAGGCGTCCCC
GTGCCGCCAGGTTGCCTGATTGACGTTAACGGCGTGCCGACGACCAATCCGGCGGTAATG
CAGGAGTCGCCGTTGGGTTCGCTGTTGACCTTTGCCGAACATAAAGGCTACGCCCTTGCA
GCGATGTGTGAAATTCTTGGCGGGGCGCTTTCCGGCGGTAAAACGACGCATCAGGAAACG
TTACAAACCAGTCCCGATGCCATTCTTAACTGCATGACCACTATCATCATCAACCCGGAA
CTCTTCGGCGCGCCGGATTGTAACGCGCAGACCGAAGCCTTTGCCGAGTGGGTGAAAGCC
TCGCCGCATGATGATGATAAGCCGATTTTGCTACCGGGCGAGTGGGAAGTGAACACGCGT
CGCGAACGGCAGAAGCAGGGGATTCCACTGGATGCGGGAAGCTGGCAGGCCATTTGTGAT
GCAGCGCGGCAGATTGGTATGCCGGAAGAGACGTTGCAGGCTTTCTGTCAGCAGTTAGCC
AGCTAA
Protein Properties
Pfam Domain Function:
Protein Residues:361
Protein Molecular Weight:40315
Protein Theoretical pI:5
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>D-malate dehydrogenase [decarboxylating]
MMKTMRIAAIPGDGIGKEVLPEGIRVLQAAAERWGFALSFEQMEWASCEYYSHHGKMMPD
DWHEQLSRFDAIYFGAVGWPDTVPDHISLWGSLLKFRREFDQYVNLRPVRLFPGVPCPLA
GKQPGDIDFYVVRENTEGEYSSLGGRVNEGTEHEVVIQESVFTRRGVDRILRYAFELAQS
RPRKTLTSATKSNGLAISMPYWDERVEAMAENYPEIRWDKQHIDILCARFVMQPERFDVV
VASNLFGDILSDLGPACTGTIGIAPSANLNPERTFPSLFEPVHGSAPDIYGKNIANPIAT
IWAGAMMLDFLGNGDERFQQAHNGILAAIEEVIAHGPKTPDMKGNATTPQVADAICKIIL
R
References
External Links:
ResourceLink
Uniprot ID:P76251
Uniprot Name:DMLA_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062362
Ecogene ID:EG13507
Ecocyc:EG13507
ColiBase:b1800
Kegg Gene:b1800
EchoBASE ID:EB3280
CCDB:DMLA_ECOLI
BacMap:16129754
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
  • 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
  • Itoh, T., Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Kasai, H., Kimura, S., Kitakawa, M., Kitagawa, M., Makino, K., Miki, T., Mizobuchi, K., Mori, H., Mori, T., Motomura, K., Nakade, S., Nakamura, Y., Nashimoto, H., Nishio, Y., Oshima, T., Saito, N., Sampei, G., Seki, Y., Horiuchi, T., et, a. l. .. (1996). "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map." DNA Res 3:379-392. Pubmed: 9097040
  • Lukas, H., Reimann, J., Kim, O. B., Grimpo, J., Unden, G. (2010). "Regulation of aerobic and anaerobic D-malate metabolism of Escherichia coli by the LysR-type regulator DmlR (YeaT)." J Bacteriol 192:2503-2511. Pubmed: 20233924
  • Reed, J. L., Patel, T. R., Chen, K. H., Joyce, A. R., Applebee, M. K., Herring, C. D., Bui, O. T., Knight, E. M., Fong, S. S., Palsson, B. O. (2006). "Systems approach to refining genome annotation." Proc Natl Acad Sci U S A 103:17480-17484. Pubmed: 17088549