DB code: D00476
CATH domain | 3.40.50.720 : Rossmann fold | |
---|---|---|
3.30.360.10 : Dihydrodipicolinate Reductase; domain 2 | Catalytic domain | |
E.C. | 1.2.1.59 | |
CSA | 1cf2 | |
M-CSA | 1cf2 | |
MACiE |
CATH domain | Related DB codes (homologues) |
---|---|
3.30.360.10 : Dihydrodipicolinate Reductase; domain 2 | T00219 D00003 D00010 D00017 D00023 D00027 D00028 D00034 |
3.40.50.720 : Rossmann fold | S00543 S00551 S00552 S00553 S00602 S00604 S00605 S00608 S00610 S00625 S00319 S00328 S00329 S00330 S00331 S00332 D00456 D00457 D00458 S00324 S00320 S00325 S00326 S00327 D00459 S00335 S00336 S00334 T00219 S00339 D00513 D00001 D00002 D00003 D00005 D00007 D00008 D00010 D00012 D00017 D00018 D00023 D00027 D00028 D00031 D00032 D00033 D00034 D00035 D00037 D00048 D00071 D00481 D00482 D00490 D00492 D00494 D00545 D00601 D00603 D00604 D00605 D00615 D00845 D00857 D00858 M00161 M00171 M00210 T00002 T00010 T00011 T00015 T00227 T00247 T00408 T00414 D00827 D00262 D00274 D00275 M00035 T00109 |
Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
---|---|---|---|---|
P10618 |
Glyceraldehyde-3-phosphate dehydrogenase
|
GAPDH
EC 1.2.1.59 NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase |
YP_004003841.1
(Protein)
NC_014658.1 (DNA/RNA sequence) |
PF02800
(Gp_dh_C)
PF00044 (Gp_dh_N) [Graphical View] |
P39460 |
Glyceraldehyde-3-phosphate dehydrogenase
|
GAPDH
EC 1.2.1.59 NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase |
NP_342058.1
(Protein)
NC_002754.1 (DNA/RNA sequence) |
PF02800
(Gp_dh_C)
PF00044 (Gp_dh_N) [Graphical View] |
KEGG enzyme name |
---|
glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+)(phosphorylating)
triosephosphate dehydrogenase (NAD(P)) glyceraldehyde-3-phosphate dehydrogenase (NAD(P)) (phosphorylating) |
UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
---|---|---|---|---|---|
P10618 | G3P_METFE | D-glyceraldehyde 3-phosphate + phosphate + NAD(P)(+) = 3-phospho-D-glyceroyl phosphate + NAD(P)H. | Homotetramer. | Cytoplasm. | |
P39460 | G3P_SULSO | D-glyceraldehyde 3-phosphate + phosphate + NAD(P)(+) = 3-phospho-D-glyceroyl phosphate + NAD(P)H. | Homotetramer. | Cytoplasm. |
KEGG Pathways | Map code | Pathways | E.C. |
---|---|---|
MAP00010 | Glycolysis / Gluconeogenesis | |
MAP00710 | Carbon fixation in photosynthetic organisms |
Compound table | ||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Substrates | Products | Intermediates | ||||||||||||
KEGG-id | C00118 | C00009 | C00003 | C00006 | C00236 | C00004 | C00005 | C00080 | ||||||
E.C. | ||||||||||||||
Compound | D-Glyceraldehyde 3-phosphate | Orthophosphate | NAD+ | NADP+ | 3-Phospho-D-glyceroyl phosphate | NADH | NADPH | H+ | ||||||
Type | carbohydrate,phosphate group/phosphate ion | phosphate group/phosphate ion | amide group,amine group,nucleotide | amide group,amine group,nucleotide | carbohydrate,phosphate group/phosphate ion | amide group,amine group,nucleotide | amide group,amine group,nucleotide | others | ||||||
ChEBI |
29052 29052 |
26078 26078 |
15846 15846 |
18009 18009 |
16001 16001 |
16908 16908 |
16474 16474 |
15378 15378 |
||||||
PubChem |
439168 439168 |
1004 22486802 1004 22486802 |
5893 5893 |
5886 5886 |
439191 439191 |
439153 439153 |
5884 5884 |
1038 1038 |
||||||
1b7gO01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1b7gQ01 | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1cf2O01 | Unbound | Unbound | Unbound | Bound:NAP | Unbound | Unbound | Unbound | |||||||
1cf2P01 | Unbound | Unbound | Unbound | Bound:NAP | Unbound | Unbound | Unbound | |||||||
1cf2Q01 | Unbound | Unbound | Unbound | Bound:NAP | Unbound | Unbound | Unbound | |||||||
1cf2R01 | Unbound | Unbound | Unbound | Bound:NAP | Unbound | Unbound | Unbound | |||||||
1b7gO02 | Unbound | Analogue:SO4_601 | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1b7gQ02 | Unbound | Analogue:SO4_602 | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1cf2O02 | Unbound | Analogue:SO4 | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1cf2P02 | Unbound | Analogue:SO4 | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1cf2Q02 | Unbound | Analogue:SO4 | Unbound | Unbound | Unbound | Unbound | Unbound | |||||||
1cf2R02 | Unbound | Analogue:SO4 | Unbound | Unbound | Unbound | Unbound | Unbound |
Reference for Active-site residues | ||
---|---|---|
resource | references | E.C. |
PDB;1b7g & literature [5], [6] & [9] |
Active-site residues | ||||||||||
---|---|---|---|---|---|---|---|---|---|---|
PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
1b7gO01 | mutant I2V | |||||||||
1b7gQ01 | mutant I2V | |||||||||
1cf2O01 | ||||||||||
1cf2P01 | ||||||||||
1cf2Q01 | ||||||||||
1cf2R01 | ||||||||||
1b7gO02 | CYS 139;HIS 219 | |||||||||
1b7gQ02 | CYS 139;HIS 219 | |||||||||
1cf2O02 | CYS 140;HIS 219 | |||||||||
1cf2P02 | CYS 140;HIS 219 | |||||||||
1cf2Q02 | CYS 140;HIS 219 | |||||||||
1cf2R02 | CYS 140;HIS 219 |
References for Catalytic Mechanism | ||
---|---|---|
References | Sections | No. of steps in catalysis |
[5]
|
p.655-656 | |
[6]
|
p.495-497 | |
[9]
|
p.115-117 |
References | |
---|---|
[1] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9761871 |
Journal | Acta Crystallogr D Biol Crystallogr |
Year | 1998 |
Volume | 54 |
Pages | 671-4 |
Authors | Fleming TM, Jones CE, Piper PW, Cowan DA, Isupov MN, Littlechild JA |
Title |
Characterization, |
Related PDB | |
Related UniProtKB | |
[2] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 9632884 |
Journal | Biochemistry (Mosc) |
Year | 1998 |
Volume | 63 |
Pages | 504-15 |
Authors | Nagradova NK, Schmalhausen EV |
Title | D-Glyceraldehyde-3-phosphate dehydrogenase: structural basis and functional role of the acyl transfer reactions. |
Related PDB | |
Related UniProtKB | |
[3] | |
Resource | |
Comments | X-ray crystallography |
Medline ID | |
PubMed ID | 10393306 |
Journal | Acta Crystallogr D Biol Crystallogr |
Year | 1999 |
Volume | 55 |
Pages | 1353-5 |
Authors | Charron C, Talfournier F, Isupov MN, Branlant G, Littlechild JA, Vitoux B, Aubry A |
Title | Crystallization and preliminary X-ray diffraction studies of D-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus. |
Related PDB | 1cf2 |
Related UniProtKB | |
[4] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 10491162 |
Journal | Eur J Biochem |
Year | 1999 |
Volume | 265 |
Pages | 93-104 |
Authors | Talfournier F, Colloc'h N, Mornon JP, Branlant G |
Title | Functional characterization of the phosphorylating D-glyceraldehyde 3-phosphate dehydrogenase from the archaeon Methanothermus fervidus by comparative molecular modelling and site-directed mutagenesis. |
Related PDB | |
Related UniProtKB | |
[5] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) |
Medline ID | 99380409 |
PubMed ID | 10448043 |
Journal | J Mol Biol |
Year | 1999 |
Volume | 291 |
Pages | 651-60 |
Authors | Isupov MN, Fleming TM, Dalby AR, Crowhurst GS, Bourne PC, Littlechild JA |
Title | Crystal structure of the glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Sulfolobus solfataricus. |
Related PDB | 1b7g |
Related UniProtKB | P39460 |
[6] | |
Resource | |
Comments | X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) |
Medline ID | 20181873 |
PubMed ID | 10715215 |
Journal | J Mol Biol |
Year | 2000 |
Volume | 297 |
Pages | 481-500 |
Authors | Charron C, Talfournier F, Isupov MN, Littlechild JA, Branlant G, Vitoux B, Aubry A |
Title | The crystal structure of d-glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeon Methanothermus fervidus in the presence of NADP(+) at 2.1 A resolution. |
Related PDB | |
Related UniProtKB | P10618 |
[7] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12369901 |
Journal | Curr Protein Pept Sci |
Year | 2001 |
Volume | 2 |
Pages | 61-72 |
Authors | Brune B, Mohr S |
Title | Protein thiol modification of glyceraldehyde-3-phosphate dehydrogenase and caspase-3 by nitric oxide. |
Related PDB | |
Related UniProtKB | |
[8] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11438534 |
Journal | J Biol Chem |
Year | 2001 |
Volume | 276 |
Pages | 35247-52 |
Authors | Qi J, Isupov MN, Littlechild JA, Anderson LE |
Title | Chloroplast glyceraldehyde-3-phosphate dehydrogenase contains a single disulfide bond located in the C-terminal extension to the B subunit. |
Related PDB | |
Related UniProtKB | |
[9] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11265453 |
Journal | Methods Enzymol |
Year | 2001 |
Volume | 331 |
Pages | 105-17 |
Authors | Littlechild JA, Isupov M |
Title | Glyceraldehyde-3-phosphate dehydrogenase from Sulfolobus solfataricus. |
Related PDB | |
Related UniProtKB | |
[10] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 12382287 |
Journal | Biopolymers |
Year | 2002 |
Volume | 65 |
Pages | 263-73 |
Authors | Charron C, Vitoux B, Aubry A |
Title | Comparative analysis of thermoadaptation within the archaeal glyceraldehyde-3-phosphate dehydrogenases from mesophilic Methanobacterium bryantii and thermophilic Methanothermus fervidus. |
Related PDB | |
Related UniProtKB | |
[11] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 11742130 |
Journal | Protein Sci |
Year | 2002 |
Volume | 11 |
Pages | 137-46 |
Authors | Orru S, Ruoppolo M, Francese S, Vitagliano L, Marino G, Esposito C |
Title | Identification of tissue transglutaminase-reactive lysine residues in glyceraldehyde-3-phosphate dehydrogenase. |
Related PDB | |
Related UniProtKB | |
[12] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 15046583 |
Journal | Biochem Soc Trans |
Year | 2004 |
Volume | 32 |
Pages | 255-8 |
Authors | Littlechild JA, Guy JE, Isupov MN |
Title | Hyperthermophilic dehydrogenase enzymes. |
Related PDB | |
Related UniProtKB | |
[13] | |
Resource | |
Comments | |
Medline ID | |
PubMed ID | 15048777 |
Journal | Biopolymers |
Year | 2004 |
Volume | 73 |
Pages | 533-41 |
Authors | Waingeh VF, Lowe SL, Thomasson KA |
Title | Brownian dynamics of interactions between glyceraldehyde-3-phosphate dehydrogenase (GAPDH) mutants and F-actin. |
Related PDB | |
Related UniProtKB |
Comments |
---|
There are several types of glyceraldehyde-3-phosphate dehydrogenases:
NADP-dependent GAPDH (E.C. NAD(P)-dependent GAPDH (phosphorylating) (E.C. GAPDH (phosphorylating) (E.C. NADP-dependent GAPDH (phosphorylating) (E.C. This enzyme corresponds to NAD(P)-dependent GAPDH (phosphorylating) (E.C. |
Created | Updated |
---|---|
2005-01-14 | 2009-02-26 |