Glyceraldehyde-3-phosphate dehydrogenase A (P0A9B2)

Identification
Name:Glyceraldehyde-3-phosphate dehydrogenase A
Synonyms:
  • GAPDH-A
Gene Name:gapA
Enzyme Class:
Biological Properties
General Function:Involved in oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Specific Function:D-glyceraldehyde 3-phosphate + phosphate + NAD(+) = 3-phospho-D-glyceroyl phosphate + NADH
Cellular Location:Cytoplasm
SMPDB Pathways:
KEGG Pathways:
  • Carbon fixation in photosynthetic organisms ec00710
  • Glycolysis / Gluconeogenesis ec00010
  • Metabolic pathways eco01100
  • Microbial metabolism in diverse environments ec01120
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+2.0Thumb+1.0Thumb
1.0D-Erythrose 4-phosphate + 1.0Water + 1.0NAD ↔ 1.04-Phospho-D-erythronate + 2.0Hydrogen ion + 1.0NADH
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0D-Glyceraldehyde 3-phosphate + 1.0NAD + 1.0Phosphate ↔ 1.0Glyceric acid 1,3-biphosphate + 1.0Hydrogen ion + 1.0NADH + 1.03-phospho-D-glyceroyl phosphate
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0D-Glyceraldehyde 3-phosphate + 1.0Phosphate + 1.0NAD ↔ 1.0Glyceric acid 1,3-biphosphate + 1.0NADH + 1.0Hydrogen ion
ReactionCard
SMPDB Reactions:
1.0D-Glyceraldehyde 3-phosphate+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Glyceric acid 1,3-biphosphate+1.0Thumb+1.0Thumb+1.0Thumb
1.0D-Glyceraldehyde 3-phosphate + 1.0NAD + 1.0Phosphate + 1.0D-Glyceraldehyde 3-phosphate → 1.0Glyceric acid 1,3-biphosphate + 1.0NADH + 1.0Hydrogen ion + 1.0Glyceric acid 1,3-biphosphate
ReactionCard
1.0Glyceric acid 1,3-biphosphate+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb+1.0D-Glyceraldehyde 3-phosphate+1.0Thumb
1.0Glyceric acid 1,3-biphosphate + 1.0NADH + 1.0Hydrogen ion + 1.0Glyceric acid 1,3-biphosphate → 1.0NAD + 1.0Phosphate + 1.0D-Glyceraldehyde 3-phosphate + 1.0D-Glyceraldehyde 3-phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+2.0Thumb+1.0Thumb
1.0D-Erythrose 4-phosphate + 1.0Water + 1.0NAD ↔ 1.04-Phospho-D-erythronate + 2.0Hydrogen ion + 1.0NADH
ReactionCard
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb+1.0Thumb
1.0D-Glyceraldehyde 3-phosphate + 1.0NAD + 1.0Phosphate ↔ 1.0Glyceric acid 1,3-biphosphate + 1.0Hydrogen ion + 1.0NADH + 1.03-phospho-D-glyceroyl phosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0D-Glyceraldehyde 3-phosphate + 1.0Inorganic phosphate + 1.0NAD → 1.03-phospho-D-glyceroyl phosphate + 1.0NADH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB231413-phospho-D-glyceroyl phosphateMetaboCard
ECMDB200954-Phospho-D-erythronateMetaboCard
ECMDB02649D-Erythrose 4-phosphateMetaboCard
ECMDB01112D-Glyceraldehyde 3-phosphateMetaboCard
ECMDB01270Glyceric acid 1,3-biphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB00902NADMetaboCard
ECMDB01487NADHMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
catalytic activity
glyceraldehyde-3-phosphate dehydrogenase activity
NAD or NADH binding
nucleotide binding
oxidoreductase activity
oxidoreductase activity, acting on the aldehyde or oxo group of donors
oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor
Process
alcohol metabolic process
glucose metabolic process
hexose metabolic process
metabolic process
monosaccharide metabolic process
oxidation reduction
small molecule metabolic process
Gene Properties
Blattner:b1779
Gene OrientationClockwise
Centisome Percentage:40.11
Left Sequence End1860795
Right Sequence End1861790
Gene Sequence:
>996 bp
ATGAAGCAAACAGTTTATATCGCCAGCCCTGAGAGCCAGCAAATTCACGTCTGGAATCTG
AATCATGAAGGCGCACTGACGCTGACACAGGTTGTCGATGTGCCGGGGCAGGTGCAGCCG
ATGGTGGTCAGCCCGGACAAACGTTATCTCTATGTTGGTGTTCGCCCTGAGTTTCGCGTC
CTGGCGTATCGTATCGCCCCGGACGATGGCGCACTGACCTTTGCCGCAGAGTCTGCGCTG
CCGGGTAGTCCGACGCATATTTCCACCGATCACCAGGGGCAGTTTGTCTTTGTAGGTTCT
TACAATGCGGGTAACGTGAGCGTAACGCGTCTGGAAGATGGCCTGCCAGTGGGCGTCGTC
GATGTGGTCGAGGGGCTGGACGGTTGCCATTCCGCCAATATCTCACCGGACAACCGTACG
CTGTGGGTTCCGGCATTAAAGCAGGATCGCATTTGCCTGTTTACGGTCAGCGATGATGGT
CATCTCGTGGCGCAGGACCCTGCGGAAGTGACCACCGTTGAAGGGGCCGGCCCGCGTCAT
ATGGTATTCCATCCAAACGAACAATATGCGTATTGCGTCAATGAGTTAAACAGCTCAGTG
GATGTCTGGGAACTGAAAGATCCGCACGGTAATATCGAATGTGTCCAGACGCTGGATATG
ATGCCGGAAAACTTCTCCGACACCCGTTGGGCGGCTGATATTCATATCACCCCGGATGGT
CGCCATTTATACGCCTGCGACCGTACCGCCAGCCTGATTACCGTTTTCAGCGTTTCGGAA
GATGGCAGCGTGTTGAGTAAAGAAGGCTTCCAGCCAACGGAAACCCAGCCGCGCGGCTTC
AATGTTGATCACAGCGGCAAGTATCTGATTGCCGCCGGGCAAAAATCTCACCACATCTCG
GTATACGAAATTGTTGGCGAGCAGGGGCTACTGCATGAAAAAGGCCGCTATGCGGTCGGG
CAGGGACCAATGTGGGTGGTGGTTAACGCACACTAA
Protein Properties
Pfam Domain Function:
Protein Residues:331
Protein Molecular Weight:35532
Protein Theoretical pI:7
PDB File:1S7C
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Glyceraldehyde-3-phosphate dehydrogenase A
MTIKVGINGFGRIGRIVFRAAQKRSDIEIVAINDLLDADYMAYMLKYDSTHGRFDGTVEV
KDGHLIVNGKKIRVTAERDPANLKWDEVGVDVVAEATGLFLTDETARKHITAGAKKVVMT
GPSKDNTPMFVKGANFDKYAGQDIVSNASCTTNCLAPLAKVINDNFGIIEGLMTTVHATT
ATQKTVDGPSHKDWRGGRGASQNIIPSSTGAAKAVGKVLPELNGKLTGMAFRVPTPNVSV
VDLTVRLEKAATYEQIKAAVKAAAEGEMKGVLGYTEDDVVSTDFNGEVCTSVFDAKAGIA
LNDNFVKLVSWYDNETGYSNKVLDLIAHISK
References
External Links:
ResourceLink
Uniprot ID:P0A9B2
Uniprot Name:G3P1_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4062334
PDB ID:1S7C
Ecogene ID:EG10367
Ecocyc:EG10367
ColiBase:b1779
Kegg Gene:b1779
EchoBASE ID:EB0362
CCDB:G3P1_ECOLI
BacMap:16129733
General Reference:
  • Aiba, H., Baba, T., Hayashi, K., Inada, T., Isono, K., Itoh, T., Kasai, H., Kashimoto, K., 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., Horiuchi, T., et, a. l. .. (1996). "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." DNA Res 3:363-377. Pubmed: 9097039
  • 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
  • Branlant, G., Branlant, C. (1985). "Nucleotide sequence of the Escherichia coli gap gene. Different evolutionary behavior of the NAD+-binding domain and of the catalytic domain of D-glyceraldehyde-3-phosphate dehydrogenase." Eur J Biochem 150:61-66. Pubmed: 2990926
  • Doolittle, R. F., Feng, D. F., Anderson, K. L., Alberro, M. R. (1990). "A naturally occurring horizontal gene transfer from a eukaryote to a prokaryote." J Mol Evol 31:383-388. Pubmed: 2124629
  • Duee, E., Olivier-Deyris, L., Fanchon, E., Corbier, C., Branlant, G., Dideberg, O. (1996). "Comparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde 3-phosphate dehydrogenases: implication for NAD binding and cooperativity." J Mol Biol 257:814-838. Pubmed: 8636984
  • Guttman, D. S., Dykhuizen, D. E. (1994). "Detecting selective sweeps in naturally occurring Escherichia coli." Genetics 138:993-1003. Pubmed: 7896119
  • 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
  • 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
  • Nelson, K., Whittam, T. S., Selander, R. K. (1991). "Nucleotide polymorphism and evolution in the glyceraldehyde-3-phosphate dehydrogenase gene (gapA) in natural populations of Salmonella and Escherichia coli." Proc Natl Acad Sci U S A 88:6667-6671. Pubmed: 1862091
  • Soukri, A., Mougin, A., Corbier, C., Wonacott, A., Branlant, C., Branlant, G. (1989). "Role of the histidine 176 residue in glyceraldehyde-3-phosphate dehydrogenase as probed by site-directed mutagenesis." Biochemistry 28:2586-2592. Pubmed: 2659073
  • Yun, M., Park, C. G., Kim, J. Y., Park, H. W. (2000). "Structural analysis of glyceraldehyde 3-phosphate dehydrogenase from Escherichia coli: direct evidence of substrate binding and cofactor-induced conformational changes." Biochemistry 39:10702-10710. Pubmed: 10978154
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842