| ID |
2329 |
| Name |
Malate dehydrogenase |
| Synonyms |
|
| Gene Name |
mdh |
| Protein Sequence |
>Malate dehydrogenase
MRKKISIIGAGFVGSTTAHWLAAKELGDIVLLDIVEGVPQGKALDLYEASPIEGFDVRVT
GTNNYADTANSDVIVVTSGAPRKPGMSREDLIKVNADITRACISQAAPLSPNAVIIMVNN
PLDAMTYLAAEVSGFPKERVIGQAGVLDAARYRTFIAMEAGVSVEDVQAMLMGGHGDEMV
PLPRFSTISGIPVSEFIAPDRLAQIVERTRKGGGEIVNLLKTGSAYYAPAAATAQMVEAV
LKDKKRVMPVAAYLTGQYGLNDIYFGVPVILGAGGVEKILELPLNEEEMALLNASAKAVR
ATLDTLKSL
|
| Number of Residues |
309 |
| Molecular Weight |
32717 |
| Theoretical pI |
4.91 |
| GO Classification |
| Function |
| catalytic activity |
| oxidoreductase activity |
| L-malate dehydrogenase activity |
| malate dehydrogenase activity |
| oxidoreductase activity, acting on CH-OH group of donors |
| lactate dehydrogenase activity |
| L-lactate dehydrogenase activity |
| Process |
| hexose metabolism |
| glucose metabolism |
| physiological process |
| glucose catabolism |
| glycolysis |
| metabolism |
| cellular metabolism |
| malate metabolism |
| generation of precursor metabolites and energy |
| tricarboxylic acid cycle intermediate metabolism |
| energy derivation by oxidation of organic compounds |
| main pathways of carbohydrate metabolism |
| alcohol metabolism |
| monosaccharide metabolism |
|
| General Function |
Energy production and conversion |
| Specific Function |
Catalyzes the reversible oxidation of malate to oxaloacetate |
| Pathways |
Not Available |
| Reactions |
- (S)-malate + NAD+ = oxaloacetate + NADH + H+
|
| Pfam Domain Function |
|
| Signals |
None |
| Transmembrane Regions |
None |
| Essentiality |
Non-Essential |
| GenBank Protein ID |
1491644  |
| UniProtKB ID |
P80040 |
| UniProtKB Entry Name |
MDH_CHLAA |
| PDB ID |
1UXG |
| PDB File |
show |
| 3D Structure |
View 3D Structure |
| Cellular Location |
Not Available |
| Gene Sequence |
>930 bp
ATGCGCAAGAAGATTAGTATTATCGGGGCAGGATTTGTCGGTTCGACGACAGCTCACTGG
CTGGCCGCTAAAGAATTAGGTGACATTGTTCTGCTTGATATTGTCGAGGGTGTGCCTCAA
GGCAAGGCTCTCGATCTCTACGAGGCATCACCAATTGAAGGGTTTGATGTTCGGGTGACC
GGCACGAACAACTACGCCGATACTGCCAACTCGGATGTCATCGTTGTTACGTCAGGTGCT
CCGCGCAAGCCGGGCATGAGCCGTGAGGATTTGATCAAGGTCAACGCCGACATCACCCGT
GCCTGTATCAGTCAGGCTGCCCCGCTCTCGCCGAATGCCGTGATTATCATGGTCAATAAT
CCTCTGGATGCGATGACCTATCTGGCGGCGGAGGTTAGTGGCTTCCCCAAAGAGCGTGTC
ATTGGTCAGGCCGGCGTCCTCGATGCGGCCCGCTATCGCACCTTCATTGCCATGGAGGCG
GGTGTTTCGGTTGAAGATGTTCAGGCGATGCTGATGGGTGGTCACGGCGATGAGATGGTA
CCGCTGCCCCGGTTTTCAACCATTAGCGGTATTCCGGTGAGCGAGTTCATTGCGCCTGAT
CGTCTGGCTCAGATTGTTGAGCGCACCCGGAAGGGTGGTGGCGAGATTGTGAATCTGCTG
AAGACCGGCAGTGCGTATTATGCTCCCGCCGCCGCCACAGCGCAGATGGTCGAAGCGGTG
CTCAAAGACAAGAAGCGGGTCATGCCGGTGGCAGCCTACCTGACCGGTCAGTACGGCCTG
AATGATATTTACTTTGGTGTACCGGTGATCCTCGGTGCCGGTGGAGTAGAGAAAATTCTC
GAATTGCCGCTCAACGAAGAGGAGATGGCACTGCTGAACGCATCGGCGAAAGCGGTACGT
GCCACCCTCGACACGCTGAAGTCTCTCTAA
|
| GenBank Gene ID |
X89038 |
| GeneCard ID |
Not Available |
| GenAtlas ID |
Not Available |
| HGNC ID |
Not Available |
| HPRD ID |
Not Available |
| IUPHAR ID |
Not Available |
| Guide to Pharmacology ID |
Not Available |
| Chromosome Location |
Not Available |
| Locus |
Not Available |
| SNPs |
mdh |
| General References |
- Synstad B, Emmerhoff O, Sirevag R: Malate dehydrogenase from the green gliding bacterium Chloroflexus aurantiacus is phylogenetically related to lactic dehydrogenases. Arch Microbiol. 1996 May;165(5):346-53. Pubmed
- Rolstad AK, Howland E, Sirevag R: Malate dehydrogenase from the thermophilic green bacterium Chloroflexus aurantiacus: purification, molecular weight, amino acid composition, and partial amino acid sequence. J Bacteriol. 1988 Jul;170(7):2947-53. Pubmed
|
| Drugs |
| # |
DrugBank ID |
Drug Name |
Drug Type |
Drug Groups |
| 1 |
DB01677 |
Fumarate |
small molecule |
experimental |
| 2 |
DB01907 |
Nicotinamide-Adenine-Dinucleotide |
small molecule |
experimental |
|
