| Entry |
|
| Name |
gap2
|
| Definition |
glyceraldehyde-3-phosphate dehydrogenase (NAD(P)) [EC: 1.2.1.59]
|
| Pathway |
| Glycolysis / Gluconeogenesis | | Carbon fixation in photosynthetic organisms |
|
| Module |
| Glycolysis (Embden-Meyerhof pathway), glucose => pyruvate | | Glycolysis, core module involving three-carbon compounds | | Reductive pentose phosphate cycle (Calvin cycle) | | Reductive pentose phosphate cycle, RuBP + CO2 => glyceraldehyde-3P |
|
| Brite |
KEGG Orthology (KO) [BR:ko00001]
Metabolism
Carbohydrate metabolism
00010 Glycolysis / Gluconeogenesis
K00150 gap2; glyceraldehyde-3-phosphate dehydrogenase (NAD(P))
Energy metabolism
00710 Carbon fixation in photosynthetic organisms
K00150 gap2; glyceraldehyde-3-phosphate dehydrogenase (NAD(P))
KEGG pathway modules [BR:ko00002]
Pathway module
Energy metabolism
Carbon fixation
M00165 Reductive pentose phosphate cycle (Calvin cycle)
K00150 gap2; glyceraldehyde-3-phosphate dehydrogenase (NAD(P))
M00166 Reductive pentose phosphate cycle, RuBP + CO2 => glyceraldehyde-3P
K00150 gap2; glyceraldehyde-3-phosphate dehydrogenase (NAD(P))
Carbohydrate and lipid metabolism
Central carbohydrate metabolism
M00001 Glycolysis (Embden-Meyerhof pathway), glucose => pyruvate
K00150 gap2; glyceraldehyde-3-phosphate dehydrogenase (NAD(P))
M00002 Glycolysis, core module involving three-carbon compounds
K00150 gap2; glyceraldehyde-3-phosphate dehydrogenase (NAD(P))
Enzymes [BR:ko01000]
1. Oxidoreductases
1.2 Acting on the aldehyde or oxo group of donors
1.2.1 With NAD+ or NADP+ as acceptor
1.2.1.59 glyceraldehyde-3-phosphate dehydrogenase (NAD(P)+) (phosphorylating)
K00150 gap2; glyceraldehyde-3-phosphate dehydrogenase (NAD(P))
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| Other DBs |
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| Genes |
AJS: | | ACK: | | ADK: | | NII: | | DTI: | | MES: | | PZU: | | NPP: | | BSUB: | | CLO: | | MLU: | | TPI: | | SSM: | | SCC: | | SGP: | | CMR: | | EVI: | | MTT: | | ZPR: | | SYN: | | SYZ: | | SYY: | | SYT: | | SYS: | | SYQ: | | SYW: | | SYC: | | SYF: | | SYD: | | SYE: | | SYG: | | SYR: | | SYX: | | SYP: | | CYA: | | CYB: | | SYNE: | | SYNP: | | TEL: | | MAR: | | CYP: | | CYC: | | CYN: | | CYH: | | CYJ: | | AMR: | | CGC: | | CAN: | | CSN: | | DSL: | | HAO: | | GLP: | | CMP: | | GVI: | | ANA: | | NPU: | | NOS: | | NOP: | | AVA: | | ANB: | | ACY: | | NAZ: | | CSG: | | CALO: | | CALT: | | RIV: | | PMA: | | PMM: | | PMT: | | PMN: | | PMI: | | PMB: | | PMC: | | PMF: | | PMG: | | PMH: | | PMJ: | | PME: | | TER: | | LEP: | | GEI: | | OAC: | | ONI: | | PSEU: | | CEP: | | MIC: | | ARP: | | CTHE: | | PLP: | | SCS: | | DLY: | | KOL: | | MJA: | | MFE: | | MVU: | | MFS: | | MIF: | | MIG: | | MMP: | | MMQ: | | MMX: | | MMZ: | | MMD: | | MAE: | | MVN: | | MVO: | | MOK: | | MAC: | | MBA: | | MMA: | | MMAZ: | | MBU: | | MMH: | | MEV: | | MZH: | | MPY: | | MHZ: | | MTP: | | MCJ: | | MHI: | | MHU: | | MLA: | | MEM: | | MBG: | | MPI: | | MBN: | | MFO: | | MPL: | | MPD: | | MEZ: | | RCI: | | MTH: | | MMG: | | MST: | | MSI: | | MRU: | | MEL: | | MEW: | | MFV: | | MKA: | | AFU: | | APO: | | AVE: | | FPL: | | HAL: | | HSL: | | HMA: | | HHI: | | HWA: | | HWC: | | NPH: | | NMO: | | HLA: | | HUT: | | HMU: | | HTU: | | NMG: | | HVO: | | HME: | | HJE: | | HBO: | | HXA: | | NAT: | | NPE: | | NGE: | | HRU: | | NOU: | | TAC: | | TVO: | | PTO: | | TAR: | | PHO: | | PAB: | | PFU: | | PFI: | | PYN: | | PYA: | | PYS: | | TKO: | | TON: | | TGA: | | TSI: | | TBA: | | THE: | | THA: | | THM: | | ABI: | | ACF: | | MAX: | | APE: | | SMR: | | SHC: | | IHO: | | DKA: | | DMU: | | DFD: | | TAG: | | THG: | | HBU: | | PFM: | | SSO: | | SOL: | | STO: | | SAI: | | SACN: | | SACR: | | SIS: | | SIA: | | SIM: | | SID: | | SIY: | | SIN: | | SII: | | SIH: | | SIR: | | SIC: | | MSE: | | MCN: | | AHO: | | PAI: | | PIS: | | PCL: | | PAS: | | PYR: | | POG: | | CMA: | | TNE: | | TUZ: | | TTN: | | VDI: | | VMO: | | TPE: | | ASC: | | CLG: | | FFO: | | NMR: | | NKR: | | CSY: | | NGA: | | KCR: | | HAH: | | » show all
   |
| Reference |
|
| 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) |
| Reference |
|
| Authors |
Koksharova O, Schubert M, Shestakov S, Cerff R |
| Title |
Genetic and biochemical evidence for distinct key functions of two highly divergent GAPDH genes in catabolic and anabolic carbon flow of the cyanobacterium Synechocystis sp. PCC 6803. |
| Journal |
Plant Mol Biol 36:183-94 (1998) |