EzCatDB: D00022
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DB codeD00022
CATH domainDomain 13.40.605.10 : Aldehyde Dehydrogenase; Chain A, domain 1Catalytic domain
Domain 23.40.309.10 : Aldehyde Dehydrogenase; Chain A, domain 2Catalytic domain
E.C.1.2.1.9

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

Enzyme Name
UniProtKBKEGG

O57693Q59931
Protein name
NADP-dependent glyceraldehyde-3-phosphate dehydrogenaseglyceraldehyde-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+)
SynonymsGlyceraldehyde-3-phosphate dehydrogenase (NADP+)
EC 1.2.1.9
EC 1.2.1.9
Non-phosphorylating glyceraldehyde 3-phosphate dehydrogenase
Glyceraldehyde-3-phosphate dehydrogenase [NADP+]
Triosephosphate dehydrogenase
RefSeq
NP_721104.1 (Protein)
NC_004350.2 (DNA/RNA sequence)
PfamPF00171 (Aldedh)
[Graphical view]
PF00171 (Aldedh)
[Graphical view]

KEGG pathways
MAP codePathways
MAP00010Glycolysis / Gluconeogenesis

UniProtKB:Accession NumberO57693Q59931
Entry nameO57693_THETEGAPN_STRMU
Activity
D-glyceraldehyde 3-phosphate + NADP(+) + H(2)O = 3-phospho-D-glycerate + NADPH.
Subunit
Homotetramer.
Subcellular location

Cofactor


Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC00118C00006C00001C00197C00005C00080
CompoundD-Glyceraldehyde 3-phosphateNADP+H2O3-Phospho-D-glycerateNADPHH+
Typecarbohydrate,phosphate group/phosphate ionamide group,amine group,nucleotideH2Ocarbohydrate,carboxyl group,phosphate group/phosphate ionamide group,amine group,nucleotideothers
ChEBI29052
18009
15377
17794
16474
15378
PubChem439168
5886
962
22247451
439183
5884
1038
              
1ky8A01UnboundBound:NAP UnboundUnbound 
1uxnA01UnboundBound:NAP UnboundUnbound 
1uxpA01UnboundBound:NAP UnboundUnbound 
1uxqA01UnboundBound:NAP UnboundUnbound 
1uxrA01UnboundBound:NAP UnboundUnbound 
1uxtA01UnboundAnalogue:NAD UnboundUnbound 
1uxuA01Bound:G3HAnalogue:NAP UnboundUnbound 
1uxvA01UnboundBound:NAP UnboundUnbound 
1euhA01UnboundUnbound UnboundUnbound 
1euhB01UnboundUnbound UnboundUnbound 
1euhC01UnboundUnbound UnboundUnbound 
1euhD01UnboundUnbound UnboundUnbound 
1qi1A01UnboundBound:NAP UnboundUnbound 
1qi1B01UnboundBound:NAP UnboundUnbound 
1qi1C01UnboundBound:NAP UnboundUnbound 
1qi1D01UnboundBound:NAP UnboundUnbound 
1qi6A01UnboundUnbound UnboundUnbound 
1qi6B01UnboundUnbound UnboundUnbound 
1qi6C01UnboundUnbound UnboundUnbound 
1qi6D01UnboundUnbound UnboundUnbound 
2euhA01UnboundBound:NAP UnboundUnbound 
2euhB01UnboundBound:NAP UnboundUnbound 
2euhC01UnboundBound:NAP UnboundUnbound 
2euhD01UnboundBound:NAP UnboundUnbound 
1ky8A02UnboundUnbound UnboundUnbound 
1uxnA02UnboundUnbound UnboundUnbound 
1uxpA02UnboundUnbound UnboundUnbound 
1uxqA02UnboundUnbound UnboundUnbound 
1uxrA02UnboundUnbound UnboundUnbound 
1uxtA02UnboundUnbound UnboundUnbound 
1uxuA02UnboundUnbound UnboundUnbound 
1uxvA02UnboundUnbound UnboundUnbound 
1euhA02UnboundUnbound UnboundUnbound 
1euhB02UnboundUnbound UnboundUnbound 
1euhC02UnboundUnbound UnboundUnbound 
1euhD02UnboundUnbound UnboundUnbound 
1qi1A02Bound:G3HUnbound UnboundUnbound 
1qi1B02Bound:G3HUnbound UnboundUnbound 
1qi1C02Bound:G3HUnbound UnboundUnbound 
1qi1D02Bound:G3HUnbound UnboundUnbound 
1qi6A02UnboundUnbound UnboundUnbound 
1qi6B02UnboundUnbound UnboundUnbound 
1qi6C02UnboundUnbound UnboundUnbound 
1qi6D02UnboundUnbound UnboundUnbound 
2euhA02UnboundUnbound UnboundUnbound 
2euhB02UnboundUnbound UnboundUnbound 
2euhC02UnboundUnbound UnboundUnbound 
2euhD02UnboundUnbound UnboundUnbound 

Active-site residues
resource
Swiss-prot;Q59931 & literature [5], [6], [7] & [10]
pdbCatalytic residuescomment
          
1ky8A01ASN 168;GLU 263
 
1uxnA01ASN 168;GLU 263
 
1uxpA01ASN 168;GLU 263
 
1uxqA01ASN 168;GLU 263
 
1uxrA01ASN 168;GLU 263
 
1uxtA01ASN 168;GLU 263
 
1uxuA01ASN 168;GLU 263
 
1uxvA01ASN 168;GLU 263
 
1euhA01ASN 154;GLU 250
 
1euhB01ASN 154;GLU 250
 
1euhC01ASN 154;GLU 250
 
1euhD01ASN 154;GLU 250
 
1qi1A01ASN 154;GLU 250
 
1qi1B01ASN 154;GLU 250
 
1qi1C01ASN 154;GLU 250
 
1qi1D01ASN 154;GLU 250
 
1qi6A01ASN 154;GLU 250
 
1qi6B01ASN 154;GLU 250
 
1qi6C01ASN 154;GLU 250
 
1qi6D01ASN 154;GLU 250
 
2euhA01ASN 154;GLU 250
 
2euhB01ASN 154;GLU 250
 
2euhC01ASN 154;GLU 250
 
2euhD01ASN 154;GLU 250
 
1ky8A02CYS 297
 
1uxnA02CYS 297
 
1uxpA02CYS 297
 
1uxqA02CYS 297
 
1uxrA02CYS 297
 
1uxtA02CYS 297
 
1uxuA02CYS 297
 
1uxvA02CYS 297
 
1euhA02CYS 284
 
1euhB02CYS 284
 
1euhC02CYS 284
 
1euhD02CYS 284
 
1qi1A02       
mutant C284S
1qi1B02       
mutant C284S
1qi1C02       
mutant C284S
1qi1D02       
mutant C284S
1qi6A02CYS 284
 
1qi6B02CYS 284
 
1qi6C02CYS 284
 
1qi6D02CYS 284
 
2euhA02CYS 284
 
2euhB02CYS 284
 
2euhC02CYS 284
 
2euhD02CYS 284
 

References for Catalytic Mechanism
ReferencesSectionsNo. 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]
PubMed ID7545914
JournalJ Mol Biol
Year1994
Volume237
Pages165-71
AuthorsHabenicht A, Hellman U, Cerff R
TitleNon-phosphorylating GAPDH of higher plants is a member of the aldehyde dehydrogenase superfamily with no sequence homology to phosphorylating GAPDH.
[2]
PubMed ID9461340
JournalBiol Chem
Year1997
Volume378
Pages1413-9
AuthorsHabenicht A
TitleThe non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase: biochemistry, structure, occurrence and evolution.
[3]
PubMed ID10504267
JournalBiochemistry
Year1999
Volume38
Pages12950-8
AuthorsMarchal S, Branlant G
TitleEvidence for the chemical activation of essential cys-302 upon cofactor binding to nonphosphorylating glyceraldehyde 3-phosphate dehydrogenase from Streptococcus mutans.
[4]
CommentsX-ray crystallography
PubMed ID10388564
JournalJ Mol Biol
Year1999
Volume290
Pages161-73
AuthorsCobessi D, Tete-Favier F, Marchal S, Azza S, Branlant G, Aubry A
TitleApo and holo crystal structures of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans.
Related PDB1euh,2euh
[5]
PubMed ID10727225
JournalBiochemistry
Year2000
Volume39
Pages3327-35
AuthorsMarchal S, Rahuel-Clermont S, Branlant G
TitleRole of glutamate-268 in the catalytic mechanism of nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans.
[6]
CommentsX-ray crystallography
PubMed ID10864505
JournalJ Mol Biol
Year2000
Volume300
Pages141-52
AuthorsCobessi D, Tete-Favier F, Marchal S, Branlant G, Aubry A
TitleStructural and biochemical investigations of the catalytic mechanism of an NADP-dependent aldehyde dehydrogenase from Streptococcus mutans.
Related PDB1qi1,1qi6
[7]
PubMed ID11306027
JournalChem Biol Interact
Year2001
Volume130-132
Pages15-28
AuthorsMarchal S, Cobessi D, Rahuel-Clermont S, Tete-Favier F, Aubry A, Branlant G
TitleChemical mechanism and substrate binding sites of NADP-dependent aldehyde dehydrogenase from Streptococcus mutans.
[8]
PubMed ID12163495
JournalJ Biol Chem
Year2002
Volume277
Pages39235-42
AuthorsMarchal S, Branlant G
TitleCharacterization of the amino acids involved in substrate specificity of nonphosphorylating glyceraldehyde-3-phosphate dehydrogenase from Streptococcus mutans.
[9]
PubMed ID11842090
JournalJ Biol Chem
Year2002
Volume277
Pages19938-45
AuthorsPohl E, Brunner N, Wilmanns M, Hensel R
TitleThe crystal structure of the allosteric non-phosphorylating glyceraldehyde-3-phosphate dehydrogenase from the hyperthermophilic archaeum Thermoproteus tenax.
Related PDB1ky8
[10]
PubMed ID15288789
JournalJ Mol Biol
Year2004
Volume341
Pages815-28
AuthorsLorentzen E, Hensel R, Knura T, Ahmed H, Pohl E
TitleStructural Basis of allosteric regulation and substrate specificity of the non-phosphorylating glyceraldehyde 3-Phosphate dehydrogenase from Thermoproteus tenax.
Related PDB1uxn,1uxp,1uxq,1uxr,1uxt,1uxu,1uxv

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

createdupdated
2004-03-162009-03-30


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
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