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.
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
AJS: 
ACK: 
ADK: 
NII: 
DTI: 
MES: 
PZU: 
NPP: 
BSUB: 
CLO: 
MLU: 
Mlut_18410
TPI: 
TREPR_0394
SSM: 
Spirs_0990
SCC: 
Spico_0086
SGP: 
SpiGrapes_3134
CMR: 
Cycma_4563 Cycma_4565
EVI: 
Echvi_3157
MTT: 
Ftrac_2076
ZPR: 
ZPR_3400
SYN: 
sll1342(gap2)
SYZ: 
MYO_129570(gap2)
SYY: 
SYNGTS_2929(gap2)
SYT: 
SYNGTI_2928(gap2)
SYS: 
SYNPCCN_2927(gap2)
SYQ: 
SYNPCCP_2927(gap2)
SYW: 
SYNW0030(gap2)
SYC: 
syc2349_c(gap2)
SYF: 
Synpcc7942_1742
SYD: 
Syncc9605_0030
SYE: 
Syncc9902_0026
SYG: 
sync_0029(gap-1)
SYR: 
SynRCC307_0028(gap1)
SYX: 
SynWH7803_0029(gap1)
SYP: 
SYNPCC7002_A0106(gap)
CYA: 
CYA_0325(gap-2)
CYB: 
CYB_1704(gap-2)
SYNE: 
Syn6312_3152
SYNP: 
Syn7502_02294
TEL: 
tll1466
MAR: 
MAE_25030
CYP: 
PCC8801_2557
CYC: 
PCC7424_2221
CYN: 
Cyan7425_0946
CYH: 
Cyan8802_3549
CYJ: 
Cyan7822_4638
AMR: 
AM1_4369(gapA)
CGC: 
Cyagr_2332
CAN: 
Cyan10605_3072
CSN: 
Cyast_1687
DSL: 
Dacsa_1284
HAO: 
PCC7418_0720
GLP: 
Glo7428_3592
CMP: 
Cha6605_3592
GVI: 
gvip056(gap1)
ANA: 
all5062(gap2)
NPU: 
Npun_R0444
NOS: 
Nos7107_2266
NOP: 
Nos7524_5283
AVA: 
Ava_2318
ANB: 
ANA_C12497
ACY: 
Anacy_0265
NAZ: 
Aazo_0813
CSG: 
Cylst_5376
CALO: 
Cal7507_0037
CALT: 
Cal6303_4016
RIV: 
Riv7116_0750
PMA: 
Pro0023(gap2)
PMM: 
PMM0023(gap2)
PMT: 
PMT0028(gap2)
PMN: 
PMN2A_1350
PMI: 
PMT9312_0023
PMB: 
A9601_00221(gap2)
PMC: 
P9515_00221(gap2)
PMF: 
P9303_00271(gap2)
PMG: 
P9301_00221(gap2)
PMH: 
P9215_00221(gap2)
PMJ: 
P9211_00231(gap2)
PME: 
NATL1_00221(gap2)
TER: 
Tery_4030
LEP: 
Lepto7376_0133
GEI: 
GEI7407_2652
OAC: 
Oscil6304_0603
ONI: 
Osc7112_4898
PSEU: 
Pse7367_0081
CEP: 
Cri9333_2336
MIC: 
Mic7113_2091
ARP: 
NIES39_C00270(gap)
CTHE: 
Chro_4726
PLP: 
Ple7327_4413
SCS: 
Sta7437_0238
DLY: 
Dehly_0804
KOL: 
Kole_0996
MJA: 
MJ_1146
MFE: 
Mefer_0809
MVU: 
Metvu_0390
MFS: 
MFS40622_0779
MIF: 
Metin_0953
MIG: 
Metig_1019
MMP: 
MMP0325
MMQ: 
MmarC5_1348
MMX: 
MmarC6_0626
MMZ: 
MmarC7_1327
MMD: 
GYY_01675
MAE: 
Maeo_0627
MVN: 
Mevan_1336
MVO: 
Mvol_1211
MOK: 
Metok_0880
MAC: 
MA1018(gap) MA3345(gap)
MBA: 
Mbar_A2189 Mbar_A3564
MMA: 
MM_2782
MMAZ: 
MmTuc01_2831
MBU: 
Mbur_0851
MMH: 
Mmah_1159
MEV: 
Metev_0436
MZH: 
Mzhil_1145
MPY: 
Mpsy_2902
MHZ: 
Metho_0889
MTP: 
Mthe_0701
MCJ: 
MCON_2908
MHI: 
Mhar_1240
MHU: 
Mhun_2462
MLA: 
Mlab_1723
MEM: 
Memar_2497
MBG: 
BN140_2174(gapA) BN140_2612(gap)
MPI: 
Mpet_2779
MBN: 
Mboo_1283 Mboo_2454
MFO: 
Metfor_0186
MPL: 
Mpal_2790
MPD: 
MCP_1270(gap-1) MCP_2688(gap-2)
MEZ: 
Mtc_0299(gap)
RCI: 
RCIX551(gap)
MTH: 
MTH1009
MMG: 
MTBMA_c13910(gap)
MST: 
Msp_1346(gap)
MSI: 
Msm_0962
MRU: 
mru_1856(gap)
MEL: 
Metbo_1751 Metbo_2379
MEW: 
MSWAN_0266
MFV: 
Mfer_0276
MKA: 
MK0618(GapA)
AFU: 
AF1732(gap)
APO: 
Arcpr_0732
AVE: 
Arcve_0098
AST: 
Asulf_01633
FPL: 
Ferp_1302
HAL: 
VNG0095G(gapB) VNG1297C
HSL: 
OE1154F(gapB)
HMA: 
rrnAC2262(gapB) rrnAC2363(gapA)
HHI: 
HAH_2730(gapA1) HAH_2803(gapA2)
HWA: 
HQ1360A(gapB) HQ1394A(gapB) HQ2025A(gapB)
HWC: 
Hqrw_1421(gapB1) Hqrw_1467(gapB3)
NPH: 
NP0012A(gapB)
NMO: 
Nmlp_1502(gap)
HLA: 
Hlac_1672 Hlac_2371
HUT: 
Huta_2548
HMU: 
Hmuk_0529 Hmuk_0659
HTU: 
Htur_0284
NMG: 
Nmag_2141 Nmag_3794
HVO: 
HVO_0478 HVO_0481(gap)
HME: 
HFX_0444(gapA) HFX_0447(gapA)
HJE: 
HacjB3_14550 HacjB3_14555
HBO: 
Hbor_26990 Hbor_27020
HXA: 
Halxa_1641 Halxa_1642
NAT: 
NJ7G_0220
NPE: 
Natpe_3640
NGE: 
Natgr_1663 Natgr_1664 Natgr_2895
HRU: 
Halru_0450 Halru_1319
NOU: 
Natoc_0189 Natoc_0190
TAC: 
Ta1103
TVO: 
TVN0458
PTO: 
PTO0742
TAR: 
TALC_01406
PHO: 
PH1830
PAB: 
PAB0257(gap)
PFU: 
PF1874
PFI: 
PFC_09215
PYN: 
PNA2_0429
PYA: 
PYCH_00860
PYS: 
Py04_1761
TKO: 
TK0765
TON: 
TON_0639
TGA: 
TGAM_1667(gap)
TSI: 
TSIB_0949
TBA: 
TERMP_00454
THE: 
GQS_01790
THA: 
TAM4_1537
THM: 
CL1_0086
ABI: 
Aboo_0431
ACF: 
AciM339_0618
MAX: 
MMALV_15110
APE: 
APE_0171.1
SMR: 
Smar_0241
SHC: 
Shell_0576
IHO: 
Igni_1001
DKA: 
DKAM_0185
DMU: 
Desmu_0845
DFD: 
Desfe_0262
TAG: 
Tagg_0301
THG: 
TCELL_1375
HBU: 
Hbut_0939
PFM: 
Pyrfu_1285
SSO: 
SSO0528(gap)
SOL: 
Ssol_1613
STO: 
ST1356
SAI: 
Saci_1356
SACN: 
SacN8_06615
SACR: 
SacRon12I_06605
SIS: 
LS215_1689
SIA: 
M1425_1581
SIM: 
M1627_1697
SID: 
M164_1578
SIY: 
YG5714_1585
SIN: 
YN1551_1251
SII: 
LD85_1789
SIH: 
SiH_1548
SIR: 
SiRe_1456
SIC: 
SiL_1458
MSE: 
Msed_1652
MCN: 
Mcup_0577
AHO: 
Ahos_1308
PAI: 
PAE1740
PIS: 
Pisl_1710
PCL: 
Pcal_0632
PAS: 
Pars_0743
PYR: 
P186_0070
POG: 
Pogu_1600
TNE: 
Tneu_0730
CMA: 
Cmaq_1790
TUZ: 
TUZN_2003
TTN: 
TTX_1534(gap)
VDI: 
Vdis_1977
VMO: 
VMUT_0389
TPE: 
Tpen_0757 Tpen_1765
ASC: 
ASAC_0892
CLG: 
Calag_0739
FFO: 
FFONT_0242
NMR: 
Nmar_0831
NKR: 
NKOR_04585
CSY: 
CENSYa_0972
NGA: 
Ngar_c16720(gap)
KCR: 
Kcr_0230
HAH: 
Halar_3698
 » 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 [GN:syn]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
39369-25-0
DBGET integrated database retrieval system