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
ec00010  Glycolysis / Gluconeogenesis
ec00710  Carbon fixation in photosynthetic organisms
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
ec01120  Microbial metabolism in diverse environments
ec01130  Biosynthesis of antibiotics
Orthology
K00150  glyceraldehyde-3-phosphate dehydrogenase (NAD(P))
Genes
BGJ: AWC36_21420
PAEU: BN889_06934
MARI: ACP86_11820
MLQ: ASQ50_01600
MARA: D0851_08505
HAM: HALO1614
GBI: PG2T_06825
AJS: Ajs_2165 Ajs_2680
ACK: C380_06000
ACID: CBP33_07180
HYB: Q5W_09960
MES: Meso_3884
RBM: TEF_02830
PZU: PHZ_p0131
SPKC: KC8_13855
AAY: WYH_02517
CMQ: B840_12970(gapB2)
ARX: ARZXY2_1270(gap2)
SYN: sll1342(gap2)
SYZ: MYO_129570(gap2)
SYY: SYNGTS_2929(gap2)
SYT: SYNGTI_2928(gap2)
SYS: SYNPCCN_2927(gap2)
SYQ: SYNPCCP_2927(gap2)
SYJ: D082_08170(gap2)
SYO: C7I86_15305(gap)
SYW: SYNW0030(gap2)
SYC: syc2349_c(gap2)
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)
SYNK: KR100_00955(gapA)
SYNR: KR49_09050(gapA)
SYND: KR52_02330(gapA)
SYH: Syncc8109_0030(gap2)
SYNW: SynWH8103_00029(gap2)
TEL: tll1466
THN: NK55_02785(gap2)
CYI: CBM981_2391(gap)
LET: O77CONTIG1_02614(gap2)
LBO: LBWT_1060
HHG: XM38_038250(gap2)
PMA: Pro_0023(gap2)
PMM: PMM0023(gap2)
PMT: PMT_0028
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)
PRC: EW14_0023
PRM: EW15_0024
AMR: AM1_4369(gapA)
MAR: MAE_25030
MPK: VL20_4417
CYL: AA637_07255(gap2)
TER: Tery_4030
ARP: NIES39_C00270(gap)
GVI: gvip056(gap1)
GLJ: GKIL_1218(gap2)
ANA: all5062(gap2)
NOE: CLI64_04785(gap)
AVA: Ava_2318
NAZ: Aazo_0813
CALH: IJ00_23650
CTHE: Chro_4726
DFO: Dform_01359(gap2)
GFL: GRFL_3040
ZPR: ZPR_3400
KOL: Kole_0996
MJA: MJ_1146
MMP: MMP0325
MMD: GYY_01675
MAE: Maeo_0627
MVO: Mvol_1211
MTH: MTH_1009
MMG: MTBMA_c13910(gap)
METC: MTCT_0917
MWO: MWSIV6_1395(gap)
METE: tca_00970
MST: Msp_1346(gap)
MSI: Msm_0962
MRU: mru_1856(gap)
MEB: Abm4_1478(gap)
MMIL: sm9_1923(gap)
MEYE: TL18_09080
MOL: YLM1_1311
METH: MBMB1_0326(gap)
MFC: BRM9_1942(gap)
MFI: DSM1535_0130(gap)
MCUB: MCBB_0298(gap)
MFV: Mfer_0276
MKA: MK0618(gapA)
AFU: AF_1732
FPL: Ferp_1302
GAC: GACE_0477
GAH: GAH_01734
TAC: Ta1103
TVO: TVG0444310(TVG0444310)
PTO: PTO0742
FAI: FAD_0549
CDIV: CPM_0301
MEAR: Mpt1_c00900(gap)
MARC: AR505_0154
ABI: Aboo_0431
PHO: PH1830(PH1830)
PAB: PAB0257(gap)
PFU: PF1874
PFI: PFC_09215
PYN: PNA2_0429
PYS: Py04_1761
TKO: TK0765
TON: TON_0639
TGA: TGAM_1667(gap)
TSI: TSIB_0949
THE: GQS_01790
THA: TAM4_1537
THM: CL1_0086
TLT: OCC_07249
THS: TES1_0542
TNU: BD01_0756
TEU: TEU_08915
PPAC: PAP_02855
MAC: MA_1018(gap) MA_3345(gap)
MMA: MM_2782
MMAC: MSMAC_1180
METM: MSMTP_1360
MTHE: MSTHC_0292
MTHR: MSTHT_0429
MBU: Mbur_0851
MMET: MCMEM_0983
MMH: Mmah_1159
MPY: Mpsy_2902
MTP: Mthe_0701
MCJ: MCON_2908
MHI: Mhar_1240
MHU: Mhun_2462
MLA: Mlab_1723
MBG: BN140_2174(gapA) BN140_2612(gap)
MEMA: MMAB1_3505(gap)
MPI: Mpet_2779
MPL: Mpal_2790
MPD: MCP_1270(gap-1) MCP_2688(gap-2)
MEZ: Mtc_0299(gap)
RCI: RCIX551(gap)
HAL: VNG_0095G(gapB) VNG_1297C
HSL: OE_1154F(gap)
HHB: Hhub_1290(gap)
HALH: HTSR_0246(gapB)
HHSR: HSR6_0233(gapB)
HSU: HLASF_0350(gapB)
HSF: HLASA_0349(gapB)
HMA: rrnAC2262(gapB)
HHI: HAH_2730(gapA1)
NPH: NP_0012A(gap)
NMO: Nmlp_1502(gap)
HMU: Hmuk_0529
HWA: HQ_1360A(gap1) HQ_2025A(gap3)
HWC: Hqrw_1421(gap1)
HVO: HVO_0478(gap1)
HME: HFX_0444(gapA)
HLA: Hlac_1672
HTU: Htur_0284
NMG: Nmag_2141(gap1)
NAT: NJ7G_0220
SALI: L593_02145
ACJ: ACAM_0134
SMR: Smar_0241
IHO: Igni_1001
IIS: EYM_03900
DKA: DKAM_0185
TAG: Tagg_0301
HBU: Hbut_0939
STO: STK_13560(gap)
SSO: SSO0528(gap)
SOL: Ssol_1613
SSOA: SULA_1640
SSOL: SULB_1641
SSOF: SULC_1639
SAI: Saci_1356
SID: M164_1578
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
ASC: ASAC_0892
ACIA: SE86_05130
NMR: Nmar_0831
NCT: NMSP_0789(gap)
NGA: Ngar_c16720(gap)
NVN: NVIE_005380(gap)
NEV: NTE_01905
NCV: NCAV_1503(gap)
NBV: T478_0731
NDV: NDEV_1047(gap)
KCR: Kcr_0230
BARC: AOA65_1541(gap)
 » 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 179:4513-22 (1997)
DOI:10.1128/JB.179.14.4513-4522.1997
  Sequence
[syn:sll1342]
Other DBs
ExplorEnz - The Enzyme Database: 1.2.1.59
IUBMB Enzyme Nomenclature: 1.2.1.59
ExPASy - ENZYME nomenclature database: 1.2.1.59
BRENDA, the Enzyme Database: 1.2.1.59
CAS: 39369-25-0

DBGET integrated database retrieval system