Malate dehydrogenase
Details
- Name
- Malate dehydrogenase
- Synonyms
- 1.1.1.37
- Gene Name
- mdh
- UniProtKB Entry
- P61889Swiss-Prot
- Organism
- Escherichia coli (strain K12)
- NCBI Taxonomy ID
- 83333
- Amino acid sequence
>lcl|BSEQ0016007|Malate dehydrogenase MKVAVLGAAGGIGQALALLLKTQLPSGSELSLYDIAPVTPGVAVDLSHIPTAVKIKGFSG EDATPALEGADVVLISAGVARKPGMDRSDLFNVNAGIVKNLVQQVAKTCPKACIGIITNP VNTTVAIAAEVLKKAGVYDKNKLFGVTTLDIIRSNTFVAELKGKQPGEVEVPVIGGHSGV TILPLLSQVPGVSFTEQEVADLTKRIQNAGTEVVEAKAGGGSATLSMGQAAARFGLSLVR ALQGEQGVVECAYVEGDGQYARFFSQPLLLGKNGVEERKSIGTLSAFEQNALEGMLDTLK KDIALGEEFVNK
- Number of residues
- 312
- Molecular Weight
- 32337.065
- Theoretical pI
- 5.46
- GO Classification
- FunctionsL-malate dehydrogenase activity / malate dehydrogenase activity / oxidoreductase activityProcessesanaerobic respiration / fermentation / glycolytic process / malate metabolic process / tricarboxylic acid cycleComponentscytoplasm / cytosol / extrinsic component of membrane / membrane
- General Function
- Catalyzes the reversible oxidation of malate to oxaloacetate.
- Specific Function
- L-malate dehydrogenase activity
- Pfam Domain Function
- Signal Regions
- Not Available
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0016008|Malate dehydrogenase (mdh) ATGAAAGTCGCAGTCCTCGGCGCTGCTGGCGGTATTGGCCAGGCGCTTGCACTACTGTTA AAAACCCAACTGCCTTCAGGTTCAGAACTCTCTCTGTATGATATCGCTCCAGTGACTCCC GGTGTGGCTGTCGATCTGAGCCATATCCCTACTGCTGTGAAAATCAAAGGTTTTTCTGGT GAAGATGCGACTCCGGCGCTGGAAGGCGCAGATGTCGTTCTTATCTCTGCAGGCGTAGCG CGTAAACCGGGTATGGATCGTTCCGACCTGTTTAACGTTAACGCCGGCATCGTGAAAAAC CTGGTACAGCAAGTTGCGAAAACCTGCCCGAAAGCGTGCATTGGTATTATCACTAACCCG GTTAACACCACAGTTGCAATTGCTGCTGAAGTGCTGAAAAAAGCCGGTGTTTATGACAAA AACAAACTGTTCGGCGTTACCACGCTGGATATCATTCGTTCCAACACCTTTGTTGCGGAA CTGAAAGGCAAACAGCCAGGCGAAGTTGAAGTGCCGGTTATTGGCGGTCACTCTGGTGTT ACCATTCTGCCGCTGCTGTCACAGGTTCCTGGCGTTAGTTTTACCGAGCAGGAAGTGGCT GATCTGACCAAACGCATCCAGAACGCGGGTACTGAAGTGGTTGAAGCGAAGGCCGGTGGC GGGTCTGCAACCCTGTCTATGGGCCAGGCAGCTGCACGTTTTGGTCTGTCTCTGGTTCGT GCACTGCAGGGCGAACAAGGCGTTGTCGAATGTGCCTACGTTGAAGGCGACGGTCAGTAC GCCCGTTTCTTCTCTCAACCGCTGCTGCTGGGTAAAAACGGCGTGGAAGAGCGTAAATCT ATCGGTACCCTGAGCGCATTTGAACAGAACGCGCTGGAAGGTATGCTGGATACGCTGAAG AAAGATATCGCCCTGGGCGAAGAGTTCGTTAATAAGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P61889 UniProtKB Entry Name MDH_ECOLI GenBank Protein ID 41989 GenBank Gene ID Y00129 PDB ID(s) 1CME, 1EMD, 1IB6, 1IE3, 2CMD, 2PWZ, 3HHP KEGG ID ecj:JW3205 NCBI Gene ID 947854 - General References
- McAlister-Henn L, Blaber M, Bradshaw RA, Nisco SJ: Complete nucleotide sequence of the Escherichia coli gene encoding malate dehydrogenase. Nucleic Acids Res. 1987 Jun 25;15(12):4993. [Article]
- Vogel RF, Entian KD, Mecke D: Cloning and sequence of the mdh structural gene of Escherichia coli coding for malate dehydrogenase. Arch Microbiol. 1987;149(1):36-42. [Article]
- 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. [Article]
- 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. [Article]
- Sutherland P, McAlister-Henn L: Isolation and expression of the Escherichia coli gene encoding malate dehydrogenase. J Bacteriol. 1985 Sep;163(3):1074-9. [Article]
- Fernley RT, Lentz SR, Bradshaw RA: Malate dehydrogenase: isolation from E. coli and comparison with the eukaryotic mitochondrial and cytoplasmic forms. Biosci Rep. 1981 Jun;1(6):497-507. [Article]
- Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
- Charnock C: 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. 1997 Jun;179(12):4066-70. [Article]
- Henzel WJ, Billeci TM, Stults JT, Wong SC, Grimley C, Watanabe C: Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5011-5. [Article]
- Nystrom T, Larsson C, Gustafsson L: Bacterial defense against aging: role of the Escherichia coli ArcA regulator in gene expression, readjusted energy flux and survival during stasis. EMBO J. 1996 Jul 1;15(13):3219-28. [Article]
- Wilkins MR, Gasteiger E, Tonella L, Ou K, Tyler M, Sanchez JC, Gooley AA, Walsh BJ, Bairoch A, Appel RD, Williams KL, Hochstrasser DF: Protein identification with N and C-terminal sequence tags in proteome projects. J Mol Biol. 1998 May 8;278(3):599-608. [Article]
- Boyd EF, Nelson K, Wang FS, Whittam TS, Selander RK: 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. 1994 Feb 15;91(4):1280-4. [Article]
- Pupo GM, Karaolis DK, Lan R, Reeves PR: Evolutionary relationships among pathogenic and nonpathogenic Escherichia coli strains inferred from multilocus enzyme electrophoresis and mdh sequence studies. Infect Immun. 1997 Jul;65(7):2685-92. [Article]
- Pupo GM, Lan R, Reeves PR, Baverstock PR: Population genetics of Escherichia coli in a natural population of native Australian rats. Environ Microbiol. 2000 Dec;2(6):594-610. [Article]
- VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
- Hall MD, Levitt DG, Banaszak LJ: Crystal structure of Escherichia coli malate dehydrogenase. A complex of the apoenzyme and citrate at 1.87 A resolution. J Mol Biol. 1992 Aug 5;226(3):867-82. [Article]
- Hall MD, Banaszak LJ: Crystal structure of a ternary complex of Escherichia coli malate dehydrogenase citrate and NAD at 1.9 A resolution. J Mol Biol. 1993 Jul 5;232(1):213-22. [Article]
- Bell JK, Yennawar HP, Wright SK, Thompson JR, Viola RE, Banaszak LJ: Structural analyses of a malate dehydrogenase with a variable active site. J Biol Chem. 2001 Aug 17;276(33):31156-62. Epub 2001 Jun 1. [Article]
Associated Data
- Bio-Entities
Bio-Entity Type Malate dehydrogenase (Escherichia coli (strain K12)) protein primary- Drug Relations
- Not Available