KEGG   ENZYME: 1.2.1.59Help
Entry
EC 1.2.1.59                 Enzyme                                 

Name
glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating);
triosephosphate dehydrogenase (NAD(P));
glyceraldehyde-3-phosphate dehydrogenase (NAD(P)) (phosphorylating)
Class
Oxidoreductases;
Acting on the aldehyde or oxo group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
D-glyceraldehyde 3-phosphate:NAD(P)+ oxidoreductase (phosphorylating)
Reaction(IUBMB)
D-glyceraldehyde 3-phosphate + phosphate + NAD(P)+ = 3-phospho-D-glyceroyl phosphate + NAD(P)H + H+ [RN:R01061 R01063]
Reaction(KEGG)
Substrate
D-glyceraldehyde 3-phosphate [CPD:C00118];
phosphate [CPD:C00009];
NAD+ [CPD:C00003];
NADP+ [CPD:C00006]
Product
3-phospho-D-glyceroyl phosphate [CPD:C00236];
NADH [CPD:C00004];
NADPH [CPD:C00005];
H+ [CPD:C00080]
Comment
NAD+ and NADP+ can be used as cofactors with similar efficiency, unlike EC 1.2.1.12 glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) and EC 1.2.1.13 glyceraldehyde-3-phosphate dehydrogenase (NADP+) (phosphorylating), which are NAD+- and NADP+-dependent, respectively.
History
EC 1.2.1.59 created 1999
Pathway
Glycolysis / Gluconeogenesis
Carbon fixation in photosynthetic organisms
Metabolic pathways
Biosynthesis of secondary metabolites
Microbial metabolism in diverse environments
Orthology
K00150  
glyceraldehyde-3-phosphate dehydrogenase (NAD(P))
Genes
PAEU: 
AJS: 
ACK: 
ADK: 
NII: 
DTI: 
MES: 
PZU: 
NPP: 
BSUB: 
CLO: 
MLU: 
TPI: 
SSM: 
SCC: 
SGP: 
SYN: 
sll1342(gap2)
SYZ: 
SYY: 
SYT: 
SYS: 
SYQ: 
SYW: 
SYNW0030(gap2)
SYC: 
syc2349_c(gap2)
SYF: 
SYD: 
SYE: 
SYG: 
sync_0029(gap-1)
SYR: 
SYX: 
SYP: 
CYA: 
CYA_0325(gap-2)
CYB: 
CYB_1704(gap-2)
SYNE: 
SYNP: 
TEL: 
THN: 
MAR: 
CYP: 
CYC: 
CYN: 
CYH: 
CYJ: 
AMR: 
AM1_4369(gapA)
CGC: 
CAN: 
CSN: 
DSL: 
HAO: 
GLP: 
CMP: 
TER: 
LEP: 
GEI: 
OAC: 
ONI: 
PSEU: 
CEP: 
MIC: 
ARP: 
GVI: 
gvip056(gap1)
GLJ: 
GKIL_1218(gap2)
ANA: 
all5062(gap2)
NPU: 
NOS: 
NOP: 
AVA: 
ANB: 
ACY: 
NAZ: 
CSG: 
CALO: 
CALT: 
RIV: 
PMA: 
Pro_0023(gap2)
PMM: 
PMM0023(gap2)
PMT: 
PMT0028(gap2)
PMN: 
PMI: 
PMB: 
PMC: 
PMF: 
PMG: 
PMH: 
PMJ: 
PME: 
CTHE: 
PLP: 
SCS: 
CMR: 
EVI: 
MTT: 
ZPR: 
DLY: 
KOL: 
MJA: 
MFE: 
MVU: 
MFS: 
MIF: 
MIG: 
MMP: 
MMQ: 
MMX: 
MMZ: 
MMD: 
MAE: 
MVN: 
MVO: 
MOK: 
MAC: 
MA1018(gap) MA3345(gap)
MBA: 
MMA: 
MMAZ: 
MBU: 
MMH: 
MEV: 
MZH: 
MPY: 
MHZ: 
MTP: 
MCJ: 
MHI: 
MHU: 
MLA: 
MEM: 
MBG: 
MPI: 
MBN: 
MFO: 
MPL: 
MPD: 
MCP_1270(gap-1) MCP_2688(gap-2)
MEZ: 
RCI: 
RCIX551(gap)
MER: 
MTH: 
MMG: 
MST: 
MSI: 
MRU: 
MEB: 
MEL: 
MEW: 
METH: 
MFV: 
MKA: 
MK0618(GapA)
MAX: 
AFU: 
AF1732(gap)
APO: 
AVE: 
AST: 
FPL: 
HAL: 
HSL: 
OE1154F(gapB)
HMA: 
rrnAC2262(gapB)
HHI: 
HAH_2730(gapA1)
HHN: 
HWA: 
HQ1360A(gapB) HQ2025A(gapB)
HWC: 
Hqrw_1421(gap1)
NPH: 
NP0012A(gapB)
NMO: 
HLA: 
HMU: 
HTU: 
NMG: 
HVO: 
HME: 
HFX_0444(gapA)
HJE: 
HBO: 
HXA: 
NAT: 
NPE: 
NGE: 
HRU: 
NOU: 
SALI: 
TAC: 
TVO: 
PTO: 
FAC: 
TAR: 
PHO: 
PAB: 
PAB0257(gap)
PFU: 
PFI: 
PYN: 
PYA: 
PYS: 
TKO: 
TON: 
TGA: 
TSI: 
TBA: 
THE: 
THA: 
THM: 
TLT: 
THS: 
TNU: 
ABI: 
ACF: 
APE: 
ACJ: 
SMR: 
SHC: 
IHO: 
DKA: 
DMU: 
DFD: 
TAG: 
THG: 
HBU: 
PFM: 
SSO: 
SSO0528(gap)
SOL: 
STO: 
SAI: 
SACN: 
SACR: 
SACS: 
SIS: 
SIA: 
SIM: 
SID: 
SIY: 
SIN: 
SII: 
SIH: 
SIR: 
SIC: 
MSE: 
MCN: 
AHO: 
PAI: 
PIS: 
PCL: 
PAS: 
PYR: 
POG: 
TNE: 
CMA: 
TUZ: 
TTN: 
VDI: 
VMO: 
TPE: 
ASC: 
CLG: 
FFO: 
NMR: 
NKR: 
CSY: 
NGA: 
CSU: 
KCR: 
HAH: 
 » show all
Taxonomy
Reference
1
  Authors
Valverde, F., Losada, M. and Serrano, A.
  Title
Cloning by functional complementation in E. coli of the gap2 gene of Synechocystis PCC 6803 supports an amphibolic role for cyanobacterial NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase.
  Journal
In: P. Mathis (Ed.), Photosynthesis: From Light to Biosphere, vol. 1, Kluwer Academic Publishers, 1995, p. 959-962.
Reference
2  [PMID:9226260]
  Authors
Valverde F, Losada M, Serrano A.
  Title
Functional complementation of an Escherichia coli gap mutant supports an amphibolic role for NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase of Synechocystis sp. strain PCC 6803.
  Journal
J. Bacteriol. 179 (1997) 4513-22.
  Organism
Synechocystis sp. PCC6803
  Sequence
[syn:sll1342]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
39369-25-0

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