Glycerol-3-phosphate dehydrogenase [NAD+] 2, mitochondrial (P41911)

Identification
NameGlycerol-3-phosphate dehydrogenase [NAD+] 2, mitochondrial
SynonymsNot Available
Gene NameGPD2
Enzyme Class
Biological Properties
General FunctionInvolved in oxidoreductase activity
Specific FunctionCatalyzes the production of glycerol under anaerobic growth conditions. Glycerol production serves as a redox sink by consuming the excess cytosolic NADH during anaerobic metabolism
Cellular LocationCytoplasm. Mitochondrion
SMPDB Pathways
Choline metabolismPW002494 ThumbThumb?image type=greyscaleThumb?image type=simple
Glycerophospholipid metabolismPW002493 ThumbThumb?image type=greyscaleThumb?image type=simple
KEGG Pathways
Glycerophospholipid metabolismec00564 Map00564
SMPDB Reactions
Glycerone phosphate + NADH + hydron → NAD + Glycerol 3-phosphate
KEGG Reactions
NADH + Dihydroxyacetone phosphate + hydron → NAD + Glycerol 3-phosphate
Metabolites
YMDB IDNameView
YMDB00073Glycerol 3-phosphateShow
YMDB00110NADShow
YMDB00143NADHShow
YMDB00322Dihydroxyacetone phosphateShow
YMDB00412NAD(+)Show
YMDB00862hydronShow
YMDB16273Glycerone phosphateShow
GO Classification
Component
glycerol-3-phosphate dehydrogenase complex
cell part
intracellular part
macromolecular complex
cytoplasm
protein complex
Function
oxidoreductase activity
protein homodimerization activity
glycerol-3-phosphate dehydrogenase [NAD+] activity
cofactor binding
oxidoreductase activity, acting on CH-OH group of donors
catalytic activity
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor
binding
protein binding
NAD or NADH binding
coenzyme binding
nucleotide binding
identical protein binding
Process
oxidation reduction
small molecule metabolic process
glycerol-3-phosphate catabolic process
alcohol metabolic process
glycerol-3-phosphate metabolic process
polyol metabolic process
alditol metabolic process
metabolic process
glycerol metabolic process
primary metabolic process
carbohydrate metabolic process
Gene Properties
Chromosome Locationchromosome 15
LocusYOL059W
Gene Sequence>1323 bp ATGCTTGCTGTCAGAAGATTAACAAGATACACATTCCTTAAGCGAACGCATCCGGTGTTA TATACTCGTCGTGCATATAAAATTTTGCCTTCAAGATCTACTTTCCTAAGAAGATCATTA TTACAAACACAACTGCACTCAAAGATGACTGCTCATACTAATATCAAACAGCACAAACAC TGTCATGAGGACCATCCTATCAGAAGATCGGACTCTGCCGTGTCAATTGTACATTTGAAA CGTGCGCCCTTCAAGGTTACAGTGATTGGTTCTGGTAACTGGGGGACCACCATCGCCAAA GTCATTGCGGAAAACACAGAATTGCATTCCCATATCTTCGAGCCAGAGGTGAGAATGTGG GTTTTTGATGAAAAGATCGGCGACGAAAATCTGACGGATATCATAAATACAAGACACCAG AACGTTAAATATCTACCCAATATTGACCTGCCCCATAATCTAGTGGCCGATCCTGATCTT TTACACTCCATCAAGGGTGCTGACATCCTTGTTTTCAACATCCCTCATCAATTTTTACCA AACATAGTCAAACAATTGCAAGGCCACGTGGCCCCTCATGTAAGGGCCATCTCGTGTCTA AAAGGGTTCGAGTTGGGCTCCAAGGGTGTGCAATTGCTATCCTCCTATGTTACTGATGAG TTAGGAATCCAATGTGGCGCACTATCTGGTGCAAACTTGGCACCGGAAGTGGCCAAGGAG CATTGGTCCGAAACCACCGTGGCTTACCAACTACCAAAGGATTATCAAGGTGATGGCAAG GATGTAGATCATAAGATTTTGAAATTGCTGTTCCACAGACCTTACTTCCACGTCAATGTC ATCGATGATGTTGCTGGTATATCCATTGCCGGTGCCTTGAAGAACGTCGTGGCACTTGCA TGTGGTTTCGTAGAAGGTATGGGATGGGGTAACAATGCCTCCGCAGCCATTCAAAGGCTG GGTTTAGGTGAAATTATCAAGTTCGGTAGAATGTTTTTCCCAGAATCCAAAGTCGAGACC TACTATCAAGAATCCGCTGGTGTTGCAGATCTGATCACCACCTGCTCAGGCGGTAGAAAC GTCAAGGTTGCCACATACATGGCCAAGACCGGTAAGTCAGCCTTGGAAGCAGAAAAGGAA TTGCTTAACGGTCAATCCGCCCAAGGGATAATCACATGCAGAGAAGTTCACGAGTGGCTA CAAACATGTGAGTTGACCCAAGAATTCCCATTATTCGAGGCAGTCTACCAGATAGTCTAC AACAACGTCCGCATGGAAGACCTACCGGAGATGATTGAAGAGCTAGACATCGATGACGAA TAG
Protein Properties
Pfam Domain Function
Protein Residues440
Protein Molecular Weight49421.30078
Protein Theoretical pI7.09
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Glycerol-3-phosphate dehydrogenase [NAD+] 2, mitochondrial MLAVRRLTRYTFLKRTHPVLYTRRAYKILPSRSTFLRRSLLQTQLHSKMTAHTNIKQHKH CHEDHPIRRSDSAVSIVHLKRAPFKVTVIGSGNWGTTIAKVIAENTELHSHIFEPEVRMW VFDEKIGDENLTDIINTRHQNVKYLPNIDLPHNLVADPDLLHSIKGADILVFNIPHQFLP NIVKQLQGHVAPHVRAISCLKGFELGSKGVQLLSSYVTDELGIQCGALSGANLAPEVAKE HWSETTVAYQLPKDYQGDGKDVDHKILKLLFHRPYFHVNVIDDVAGISIAGALKNVVALA CGFVEGMGWGNNASAAIQRLGLGEIIKFGRMFFPESKVETYYQESAGVADLITTCSGGRN VKVATYMAKTGKSALEAEKELLNGQSAQGIITCREVHEWLQTCELTQEFPLFEAVYQIVY NNVRMEDLPEMIEELDIDDE
References
External Links
ResourceLink
Saccharomyces Genome Database GPD2
Uniprot IDP41911
Uniprot NameGPD2_YEAST
GenBank Gene IDAY558560
Genebank Protein ID45271010
General Reference
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  • Dujon, B., Albermann, K., Aldea, M., Alexandraki, D., Ansorge, W., Arino, J., Benes, V., Bohn, C., Bolotin-Fukuhara, M., Bordonne, R., Boyer, J., Camasses, A., Casamayor, A., Casas, C., Cheret, G., Cziepluch, C., Daignan-Fornier, B., Dang, D. V., de Haan, M., Delius, H., Durand, P., Fairhead, C., Feldmann, H., Gaillon, L., Kleine, K., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV." Nature 387:98-102.9169874
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  • Ansell, R., Granath, K., Hohmann, S., Thevelein, J. M., Adler, L. (1997). "The two isoenzymes for yeast NAD+-dependent glycerol 3-phosphate dehydrogenase encoded by GPD1 and GPD2 have distinct roles in osmoadaptation and redox regulation." EMBO J 16:2179-2187.9171333
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  • Sickmann, A., Reinders, J., Wagner, Y., Joppich, C., Zahedi, R., Meyer, H. E., Schonfisch, B., Perschil, I., Chacinska, A., Guiard, B., Rehling, P., Pfanner, N., Meisinger, C. (2003). "The proteome of Saccharomyces cerevisiae mitochondria." Proc Natl Acad Sci U S A 100:13207-13212.14576278
  • Valadi, A., Granath, K., Gustafsson, L., Adler, L. (2004). "Distinct intracellular localization of Gpd1p and Gpd2p, the two yeast isoforms of NAD+-dependent glycerol-3-phosphate dehydrogenase, explains their different contributions to redox-driven glycerol production." J Biol Chem 279:39677-39685.15210723
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