Malate dehydrogenase (P61889)

Identification
Name:Malate dehydrogenase
Synonyms:Not Available
Gene Name:mdh
Enzyme Class:
Biological Properties
General Function:Involved in oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
Specific Function:Catalyzes the reversible oxidation of malate to oxaloacetate
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Malic acid + 1.0NAD ↔ 1.0Hydrogen ion + 1.0NADH + 1.0Oxalacetic acid
ReactionCard
SMPDB Reactions:
1.0L-Malic acid+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Malic acid + 1.0NAD + 1.0L-Malic acid → 1.0Oxalacetic acid + 1.0NADH + 1.0Hydrogen ion
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Malic acid + 1.0NAD ↔ 1.0Hydrogen ion + 1.0NADH + 1.0Oxalacetic acid
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0L-Malic acid + 1.0NAD → 1.0Oxalacetic acid + 1.0NADH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB210023-Sulfopyruvic acidMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00156L-Malic acidMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB00223Oxalacetic acidMetaboCard
GO Classification:
Function
binding
catalytic activity
L-malate dehydrogenase activity
malate dehydrogenase activity
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
Process
carbohydrate metabolic process
carboxylic acid metabolic process
cellular carbohydrate metabolic process
cellular metabolic process
dicarboxylic acid metabolic process
malate metabolic process
metabolic process
organic acid metabolic process
oxidation reduction
oxoacid metabolic process
primary metabolic process
Gene Properties
Blattner:b3236
Gene OrientationCounterclockwise
Centisome Percentage:72.88
Left Sequence End3381352
Right Sequence End3382290
Gene Sequence:
>939 bp
ATGGATATCATCTTTTATCACCCAACGTTCGATACCCAATGGTGGATTGAGGCACTGCGC
AAAGCTATTCCTCAGGCAAGAGTCAGAGCATGGAAAAGCGGAGATAATGACTCTGCTGAT
TATGCTTTAGTCTGGCATCCTCCTGTTGAAATGCTGGCAGGGCGCGATCTTAAAGCGGTG
TTCGCACTCGGGGCCGGTGTTGATTCTATTTTGAGCAAGCTACAGGCACACCCTGAAATG
CTGAACCCTTCTGTTCCACTTTTTCGCCTGGAAGATACCGGTATGGGCGAGCAAATGCAG
GAATATGCTGTCAGTCAGGTGCTGCATTGGTTTCGACGTTTTGACGATTATCGCATCCAG
CAAAATAGTTCGCATTGGCAACCGCTGCCTGAATATCATCGGGAAGATTTTACCATCGGC
ATTTTGGGCGCAGGCGTACTGGGCAGTAAAGTTGCTCAGAGTCTGCAAACCTGGCGCTTT
CCGCTGCGTTGCTGGAGTCGAACCCGTAAATCGTGGCCTGGCGTGCAAAGCTTTGCCGGA
CGGGAAGAACTGTCTGCATTTCTGAGCCAATGTCGGGTATTGATTAATTTGTTACCGAAT
ACCCCTGAAACCGTCGGCATTATTAATCAACAATTACTCGAAAAATTACCGGATGGCGCG
TATCTCCTCAACCTGGCGCGTGGTGTTCATGTTGTGGAAGATGACCTGCTCGCGGCGCTG
GATAGCGGCAAAGTTAAAGGCGCAATGTTGGATGTTTTTAATCGTGAACCCTTACCGCCT
GAAAGTCCGCTCTGGCAACATCCACGCGTGACGATAACACCACATGTCGCCGCGATTACC
CGTCCCGCTGAAGCTGTGGAGTACATTTCTCGCACCATTGCCCAGCTCGAAAAAGGGGAG
AGGGTCTGCGGGCAAGTCGACCGCGCACGCGGCTACTAA
Protein Properties
Pfam Domain Function:
Protein Residues:312
Protein Molecular Weight:32337
Protein Theoretical pI:5
PDB File:2CMD
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Malate dehydrogenase
MKVAVLGAAGGIGQALALLLKTQLPSGSELSLYDIAPVTPGVAVDLSHIPTAVKIKGFSG
EDATPALEGADVVLISAGVARKPGMDRSDLFNVNAGIVKNLVQQVAKTCPKACIGIITNP
VNTTVAIAAEVLKKAGVYDKNKLFGVTTLDIIRSNTFVAELKGKQPGEVEVPVIGGHSGV
TILPLLSQVPGVSFTEQEVADLTKRIQNAGTEVVEAKAGGGSATLSMGQAAARFGLSLVR
ALQGEQGVVECAYVEGDGQYARFFSQPLLLGKNGVEERKSIGTLSAFEQNALEGMLDTLK
KDIALGEEFVNK
References
External Links:
ResourceLink
Uniprot ID:P61889
Uniprot Name:MDH_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062597
PDB ID:2CMD
Ecogene ID:EG10576
Ecocyc:EG10576
ColiBase:b3236
Kegg Gene:b3236
EchoBASE ID:EB0571
CCDB:MDH_ECOLI
BacMap:16131126
General Reference:
  • Bell, J. K., Yennawar, H. P., Wright, S. K., Thompson, J. R., Viola, R. E., Banaszak, L. J. (2001). "Structural analyses of a malate dehydrogenase with a variable active site." J Biol Chem 276:31156-31162. Pubmed: 11389141
  • 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
  • Boyd, E. F., Nelson, K., Wang, F. S., Whittam, T. S., Selander, R. K. (1994). "Molecular genetic basis of allelic polymorphism in malate dehydrogenase (mdh) in natural populations of Escherichia coli and Salmonella enterica." Proc Natl Acad Sci U S A 91:1280-1284. Pubmed: 8108402
  • Charnock, C. (1997). "Structural studies of malate dehydrogenases (MDHs): MDHs in Brevundimonas species are the first reported MDHs in Proteobacteria which resemble lactate dehydrogenases in primary structure." J Bacteriol 179:4066-4070. Pubmed: 9190829
  • Fernley, R. T., Lentz, S. R., Bradshaw, R. A. (1981). "Malate dehydrogenase: isolation from E. coli and comparison with the eukaryotic mitochondrial and cytoplasmic forms." Biosci Rep 1:497-507. Pubmed: 7028159
  • Hall, M. D., Banaszak, L. J. (1993). "Crystal structure of a ternary complex of Escherichia coli malate dehydrogenase citrate and NAD at 1.9 A resolution." J Mol Biol 232:213-222. Pubmed: 8331658
  • Hall, M. D., Levitt, D. G., Banaszak, L. J. (1992). "Crystal structure of Escherichia coli malate dehydrogenase. A complex of the apoenzyme and citrate at 1.87 A resolution." J Mol Biol 226:867-882. Pubmed: 1507230
  • 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
  • Henzel, W. J., Billeci, T. M., Stults, J. T., Wong, S. C., Grimley, C., Watanabe, C. (1993). "Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases." Proc Natl Acad Sci U S A 90:5011-5015. Pubmed: 8506346
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • McAlister-Henn, L., Blaber, M., Bradshaw, R. A., Nisco, S. J. (1987). "Complete nucleotide sequence of the Escherichia coli gene encoding malate dehydrogenase." Nucleic Acids Res 15:4993. Pubmed: 3299262
  • Nystrom, T., Larsson, C., Gustafsson, L. (1996). "Bacterial defense against aging: role of the Escherichia coli ArcA regulator in gene expression, readjusted energy flux and survival during stasis." EMBO J 15:3219-3228. Pubmed: 8670822
  • Pupo, G. M., Karaolis, D. K., Lan, R., Reeves, P. R. (1997). "Evolutionary relationships among pathogenic and nonpathogenic Escherichia coli strains inferred from multilocus enzyme electrophoresis and mdh sequence studies." Infect Immun 65:2685-2692. Pubmed: 9199437
  • Pupo, G. M., Lan, R., Reeves, P. R., Baverstock, P. R. (2000). "Population genetics of Escherichia coli in a natural population of native Australian rats." Environ Microbiol 2:594-610. Pubmed: 11214793
  • Sutherland, P., McAlister-Henn, L. (1985). "Isolation and expression of the Escherichia coli gene encoding malate dehydrogenase." J Bacteriol 163:1074-1079. Pubmed: 2993232
  • Vogel, R. F., Entian, K. D., Mecke, D. (1987). "Cloning and sequence of the mdh structural gene of Escherichia coli coding for malate dehydrogenase." Arch Microbiol 149:36-42. Pubmed: 3322223
  • Wilkins, M. R., Gasteiger, E., Tonella, L., Ou, K., Tyler, M., Sanchez, J. C., Gooley, A. A., Walsh, B. J., Bairoch, A., Appel, R. D., Williams, K. L., Hochstrasser, D. F. (1998). "Protein identification with N and C-terminal sequence tags in proteome projects." J Mol Biol 278:599-608. Pubmed: 9600841