Entry
Name
glutamate synthase (NADH);
glutamate (reduced nicotinamide adenine dinucleotide) synthase;
NADH: GOGAT;
L-glutamate synthase (NADH);
L-glutamate synthetase;
NADH-glutamate synthase;
NADH-dependent glutamate synthase
Class
Oxidoreductases;
Acting on the CH-NH2 group of donors;
With NAD+ or NADP+ as acceptor
BRITE hierarchy
Sysname
L-glutamate:NAD+ oxidoreductase (transaminating)
Reaction(IUBMB)
2 L-glutamate + NAD+ = L-glutamine + 2-oxoglutarate + NADH + H+ [RN:
R00093 ];
(1a) L-glutamate + NH3 = L-glutamine + H2O [RN:
R00256 ];
(1b) L-glutamate + NAD+ + H2O = NH3 + 2-oxoglutarate + NADH + H+ [RN:
R00243 ]
Reaction(KEGG)
Substrate
Product
Comment
A flavoprotein (FMN). The reaction takes place in the direction of L-glutamate production. The protein is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC
3.5.1.2 , glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC
1.4.1.2 , glutamate dehydrogenase).
History
EC 1.4.1.14 created 1978, modified 2019
Pathway
ec00250 Alanine, aspartate and glutamate metabolism
ec01110 Biosynthesis of secondary metabolites
ec01120 Microbial metabolism in diverse environments
Orthology
K00264 glutamate synthase (NADH)
Genes
LPIC : 129258831 129258833 129259375 129259376
DSI : Dsimw501_GD12441(Dsim_GD12441)
CLON : 129610451 129618227
PPOI : 119102368 119102488
CSCU : 111624033 111638555
ABRU : 129975231 129984806
CEL : CELE_W07E11.1(W07E11.1)
CSAT : 104725863 104728554 104761363
MINC : 123198124 123206665 123226207
HSYR : 120117517 120184088 120206192
DZI : 111280486 111289287 111309227
AHF : 112697424 112705922 112755343 112765389
QSA : O6P43_015015 O6P43_019921
MSYL : 126624044 126629149
PXB : 103941488 103943433 103967236
MESC : 110617349 110630652
PALZ : 118033501 118057296
CILL : 122311011 122312965
CAVE : 132162263 132165333
SSPL : 121747965 121752173 121779747 121782410
SHIS : 125213241 125213411
APAN : 127256298 127259584
CCAV : 112508668 112515985
CSIN : 114285508 114310758
RVL : 131301738 131319786 131319792
MING : 122062882 122081042
PSOM : 113299164 113358466
OSA : 4324398 4339561(GLT2)
TAES : 123061864 123070558 123078967
MFLO : 136450302 136456380
PVIR : 120664696 120675270 120697894 120707627
PAUA : 133908489 133918129 133929376
MUS : 103980032 103996064 135617878
ZOF : 122020245 122025187 122026291 122032959 122033388
MSIN : 131241230 131245159
ACAK : 137942584 137961875
MPP : MICPUCDRAFT_57115(GLT)
NCS : NCAS_0A14190(NCAS0A14190)
NDI : NDAI_0A01860(NDAI0A01860)
TPF : TPHA_0F03070(TPHA0F03070)
TDL : TDEL_0C01870(TDEL0C01870)
KNG : KNAG_0C03720(KNAG0C03720)
SPAA : SPAPADRAFT_141734(GLT1)
LBG : 92205742(LODBEIA_P05460)
CAL : CAALFM_C106550WA(GLT1)
YLI : 2907005(YALI2_C00682g)
NTE : NEUTE1DRAFT65142(NEUTE1DRAFT_65142)
SMP : 10808319(SMAC4_02431)
PBEL : QC761_0055180(GLT1_2)
PPSD : QC762_0055380(GLT1)
PPSP : QC763_0054760(GLT1)
PPSA : QC764_0054500(GLT1)
FPOA : FPOAC1_001542(GLT1)
TRE : TRIREDRAFT_122287(glt1)
TATV : 25775645(TrAtP1_005625)
MBRN : 26239404(G6M90_00g034430)
PLJ : 28889325(PLICBS_008229)
CDET : 87942897(CDEST_06394)
BFU : BCIN_15g02460(Bcglt1)
PBL : PAAG_12483(PAAG_07998)
PTRR : 6342223(PtrM4_092930)
CDEP : 91088717(L203_104507)
KMG : 30161597(I203_107037)
KNE : 92182689(IAR55_005431)
CCAC : CcaHIS019_0602820(GLT1)
ABP : AGABI1DRAFT104661(AGABI1DRAFT_104661)
ABV : AGABI2DRAFT176670(AGABI2DRAFT_176670)
SCM : SCHCO_02607326(SCHCODRAFT_02607326)
SLA : SERLADRAFT_357441(NADH-GOGAT)
PLAG : 39744291(PADL01_1435300)
PBRS : 92372974(MKS88_004887)
PTI : PHATRDRAFT_51214(GltX)
» show all
Taxonomy
Reference
Authors
Roon RJ, Even HL, Larimore F
Title
Glutamate synthase: properties of the reduced nicotinamide adenine dinucleotide-dependent enzyme from Saccharomyces cerevisiae.
Journal
Reference
Authors
Boland MJ, Benny AG.
Title
Enzymes of nitrogen metabolism in legume nodules. Purification and properties of NADH-dependent glutamate synthase from lupin nodules.
Journal
Reference
Authors
Masters DS Jr, Meister A
Title
Inhibition of homocysteine sulfonamide of glutamate synthase purified from Saccharomyces cerevisiae.
Journal
J Biol Chem 257:8711-5 (1982)
Reference
Authors
Anderson MP, Vance CP, Heichel GH, Miller SS
Title
Purification and Characterization of NADH-Glutamate Synthase from Alfalfa Root Nodules.
Journal
Reference
Authors
Blanco L, Reddy PM, Silvente S, Bucciarelli B, Khandual S, Alvarado-Affantranger X, Sanchez F, Miller S, Vance C, Lara-Flores M
Title
Molecular cloning, characterization and regulation of two different NADH-glutamate synthase cDNAs in bean nodules.
Journal
Other DBs
ExplorEnz - The Enzyme Database: 1.4.1.14
ExPASy - ENZYME nomenclature database: 1.4.1.14