DB code: D00022

CATH domain 3.40.605.10 : Aldehyde Dehydrogenase; Chain A, domain 1 Catalytic domain
3.40.309.10 : Aldehyde Dehydrogenase; Chain A, domain 2 Catalytic domain
E.C. 1.2.1.9
CSA
M-CSA
MACiE

CATH domain Related DB codes (homologues)
3.40.309.10 : Aldehyde Dehydrogenase; Chain A, domain 2 D00020 D00021 D00475 D00614
3.40.605.10 : Aldehyde Dehydrogenase; Chain A, domain 1 D00020 D00021 D00475 D00614

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam RefSeq
O57693
Glyceraldehyde-3-phosphate dehydrogenase (NADP+)
EC 1.2.1.9
PF00171 (Aldedh)
[Graphical View]
Q59931 NADP-dependent glyceraldehyde-3-phosphate dehydrogenase
EC 1.2.1.9
Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase
Glyceraldehyde-3-phosphate dehydrogenase [NADP+]
Triosephosphate dehydrogenase
PF00171 (Aldedh)
[Graphical View]
NP_721104.1 (Protein)
NC_004350.2 (DNA/RNA sequence)

KEGG enzyme name
glyceraldehyde-3-phosphate dehydrogenase (NADP+)
triosephosphate dehydrogenase
dehydrogenase, glyceraldehyde phosphate (nicotinamide adeninedinucleotide phosphate)
glyceraldehyde phosphate dehydrogenase (NADP+)
glyceraldehyde 3-phosphate dehydrogenase (NADP+)
NADP+-glyceraldehyde phosphate dehydrogenase
NADP+-glyceraldehyde-3-phosphate dehydrogenase
glyceraldehyde-3-phosphate:NADP+ reductase
nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase
glyceraldehyde-3-phosphate dehydrogenase (NADP+)

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
O57693 O57693_THETE
Q59931 GAPN_STRMU D-glyceraldehyde 3-phosphate + NADP(+) + H(2)O = 3-phospho-D-glycerate + NADPH. Homotetramer.

KEGG Pathways
Map code Pathways E.C.
MAP00010 Glycolysis / Gluconeogenesis

Compound table
Substrates Products Intermediates
KEGG-id C00118 C00006 C00001 C00197 C00005 C00080
E.C.
Compound D-Glyceraldehyde 3-phosphate NADP+ H2O 3-Phospho-D-glycerate NADPH H+
Type carbohydrate,phosphate group/phosphate ion amide group,amine group,nucleotide H2O carbohydrate,carboxyl group,phosphate group/phosphate ion amide group,amine group,nucleotide others
ChEBI 29052
29052
18009
18009
15377
15377
17794
17794
16474
16474
15378
15378
PubChem 439168
439168
5886
5886
22247451
962
22247451
962
439183
439183
5884
5884
1038
1038
1ky8A01 Unbound Bound:NAP Unbound Unbound
1uxnA01 Unbound Bound:NAP Unbound Unbound
1uxpA01 Unbound Bound:NAP Unbound Unbound
1uxqA01 Unbound Bound:NAP Unbound Unbound
1uxrA01 Unbound Bound:NAP Unbound Unbound
1uxtA01 Unbound Analogue:NAD Unbound Unbound
1uxuA01 Bound:G3H Analogue:NAP Unbound Unbound
1uxvA01 Unbound Bound:NAP Unbound Unbound
1euhA01 Unbound Unbound Unbound Unbound
1euhB01 Unbound Unbound Unbound Unbound
1euhC01 Unbound Unbound Unbound Unbound
1euhD01 Unbound Unbound Unbound Unbound
1qi1A01 Unbound Bound:NAP Unbound Unbound
1qi1B01 Unbound Bound:NAP Unbound Unbound
1qi1C01 Unbound Bound:NAP Unbound Unbound
1qi1D01 Unbound Bound:NAP Unbound Unbound
1qi6A01 Unbound Unbound Unbound Unbound
1qi6B01 Unbound Unbound Unbound Unbound
1qi6C01 Unbound Unbound Unbound Unbound
1qi6D01 Unbound Unbound Unbound Unbound
2euhA01 Unbound Bound:NAP Unbound Unbound
2euhB01 Unbound Bound:NAP Unbound Unbound
2euhC01 Unbound Bound:NAP Unbound Unbound
2euhD01 Unbound Bound:NAP Unbound Unbound
1ky8A02 Unbound Unbound Unbound Unbound
1uxnA02 Unbound Unbound Unbound Unbound
1uxpA02 Unbound Unbound Unbound Unbound
1uxqA02 Unbound Unbound Unbound Unbound
1uxrA02 Unbound Unbound Unbound Unbound
1uxtA02 Unbound Unbound Unbound Unbound
1uxuA02 Unbound Unbound Unbound Unbound
1uxvA02 Unbound Unbound Unbound Unbound
1euhA02 Unbound Unbound Unbound Unbound
1euhB02 Unbound Unbound Unbound Unbound
1euhC02 Unbound Unbound Unbound Unbound
1euhD02 Unbound Unbound Unbound Unbound
1qi1A02 Bound:G3H Unbound Unbound Unbound
1qi1B02 Bound:G3H Unbound Unbound Unbound
1qi1C02 Bound:G3H Unbound Unbound Unbound
1qi1D02 Bound:G3H Unbound Unbound Unbound
1qi6A02 Unbound Unbound Unbound Unbound
1qi6B02 Unbound Unbound Unbound Unbound
1qi6C02 Unbound Unbound Unbound Unbound
1qi6D02 Unbound Unbound Unbound Unbound
2euhA02 Unbound Unbound Unbound Unbound
2euhB02 Unbound Unbound Unbound Unbound
2euhC02 Unbound Unbound Unbound Unbound
2euhD02 Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;Q59931 & literature [5], [6], [7] & [10]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1ky8A01 ASN 168;GLU 263
1uxnA01 ASN 168;GLU 263
1uxpA01 ASN 168;GLU 263
1uxqA01 ASN 168;GLU 263
1uxrA01 ASN 168;GLU 263
1uxtA01 ASN 168;GLU 263
1uxuA01 ASN 168;GLU 263
1uxvA01 ASN 168;GLU 263
1euhA01 ASN 154;GLU 250
1euhB01 ASN 154;GLU 250
1euhC01 ASN 154;GLU 250
1euhD01 ASN 154;GLU 250
1qi1A01 ASN 154;GLU 250
1qi1B01 ASN 154;GLU 250
1qi1C01 ASN 154;GLU 250
1qi1D01 ASN 154;GLU 250
1qi6A01 ASN 154;GLU 250
1qi6B01 ASN 154;GLU 250
1qi6C01 ASN 154;GLU 250
1qi6D01 ASN 154;GLU 250
2euhA01 ASN 154;GLU 250
2euhB01 ASN 154;GLU 250
2euhC01 ASN 154;GLU 250
2euhD01 ASN 154;GLU 250
1ky8A02 CYS 297
1uxnA02 CYS 297
1uxpA02 CYS 297
1uxqA02 CYS 297
1uxrA02 CYS 297
1uxtA02 CYS 297
1uxuA02 CYS 297
1uxvA02 CYS 297
1euhA02 CYS 284
1euhB02 CYS 284
1euhC02 CYS 284
1euhD02 CYS 284
1qi1A02 mutant C284S
1qi1B02 mutant C284S
1qi1C02 mutant C284S
1qi1D02 mutant C284S
1qi6A02 CYS 284
1qi6B02 CYS 284
1qi6C02 CYS 284
1qi6D02 CYS 284
2euhA02 CYS 284
2euhB02 CYS 284
2euhC02 CYS 284
2euhD02 CYS 284

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
p.167-168
[2]
p.1416
[3]
Fig.1, p.12956-12957
[5]
Fig.6, p.3333-3334
[6]
p.145-147
[7]
p.17-22
[9]
p.19942
[10]
p.824-825

References
[1]
Resource
Comments
Medline ID
PubMed ID 7545914
Journal J Mol Biol
Year 1994
Volume 237
Pages 165-71
Authors Habenicht A, Hellman U, Cerff R
Title Non-phosphorylating GAPDH of higher plants is a member of the aldehyde dehydrogenase superfamily with no sequence homology to phosphorylating GAPDH.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 9461340
Journal Biol Chem
Year 1997
Volume 378
Pages 1413-9
Authors Habenicht A
Title The non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase: biochemistry, structure, occurrence and evolution.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 10504267
Journal Biochemistry
Year 1999
Volume 38
Pages 12950-8
Authors Marchal S, Branlant G
Title Evidence for the chemical activation of essential cys-302 upon cofactor binding to nonphosphorylating glyceraldehyde 3-phosphate dehydrogenase from Streptococcus mutans.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10388564
Journal J Mol Biol
Year 1999
Volume 290
Pages 161-73
Authors Cobessi D, Tete-Favier F, Marchal S, Azza S, Branlant G, Aubry A
Title Apo and holo crystal structures of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans.
Related PDB 1euh 2euh
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 10727225
Journal Biochemistry
Year 2000
Volume 39
Pages 3327-35
Authors Marchal S, Rahuel-Clermont S, Branlant G
Title Role of glutamate-268 in the catalytic mechanism of nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans.
Related PDB
Related UniProtKB
[6]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10864505
Journal J Mol Biol
Year 2000
Volume 300
Pages 141-52
Authors Cobessi D, Tete-Favier F, Marchal S, Branlant G, Aubry A
Title Structural and biochemical investigations of the catalytic mechanism of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans.
Related PDB 1qi1 1qi6
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 11306027
Journal Chem Biol Interact
Year 2001
Volume 130-132
Pages 15-28
Authors Marchal S, Cobessi D, Rahuel-Clermont S, Tete-Favier F, Aubry A, Branlant G
Title Chemical mechanism and substrate binding sites of NADP-dependent aldehyde dehydrogenase from Streptococcus mutans.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 12163495
Journal J Biol Chem
Year 2002
Volume 277
Pages 39235-42
Authors Marchal S, Branlant G
Title Characterization of the amino acids involved in substrate specificity of nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 11842090
Journal J Biol Chem
Year 2002
Volume 277
Pages 19938-45
Authors Pohl E, Brunner N, Wilmanns M, Hensel R
Title The crystal structure of the allosteric non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeum Thermoproteus tenax.
Related PDB 1ky8
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 15288789
Journal J Mol Biol
Year 2004
Volume 341
Pages 815-28
Authors Lorentzen E, Hensel R, Knura T, Ahmed H, Pohl E
Title Structural Basis of allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde 3-Phosphate dehydrogenase from Thermoproteus tenax.
Related PDB 1uxn 1uxp 1uxq 1uxr 1uxt 1uxu 1uxv
Related UniProtKB

Comments
This enzyme catalyzed complex reactions, which can be divided into the following reactions (see [3] & [5]):
(A) Addition of nucleophilic Cys to carbonyl group of substrate
(B) Hydride transfer
(C) Hydrolysis

Created Updated
2004-03-16 2009-03-30