KEGG   ENZYME: 1.4.1.14
Entry
EC 1.4.1.14                 Enzyme                                 

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
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
L-glutamate [CPD:C00025];
NAD+ [CPD:C00003];
NH3 [CPD:C00014];
H2O [CPD:C00001]
Product
L-glutamine [CPD:C00064];
2-oxoglutarate [CPD:C00026];
NADH [CPD:C00004];
H+ [CPD:C00080];
H2O [CPD:C00001];
NH3 [CPD:C00014]
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
ec00910  Nitrogen metabolism
ec01100  Metabolic pathways
ec01110  Biosynthesis of secondary metabolites
ec01120  Microbial metabolism in diverse environments
Orthology
K00264  glutamate synthase (NADH)
Genes
BFO: 118423229
SPU: 754163
DME: Dmel_CG9674(CG9674)
DER: 6543630
DSE: 6606013
DSI: Dsimw501_GD12441(Dsim_GD12441)
DYA: Dyak_GE22188
DAN: 6493372
DSR: 110190291
DPO: Dpse_GA21956
DPE: 6601003
DMN: 108152363
DWI: 6645095
DAZ: 108613420
DNV: 108650790
DHE: 111605684
DVI: 6622079
MDE: 101893373
AAG: 5565246
AALB: 109410517
AME: 413372
BIM: 100743936
BTER: 100648506
CCAL: 108629149
OBB: 114879469
SOC: 105197574
MPHA: 105838501
AEC: 105149802
ACEP: 105627138
PBAR: 105424147
VEM: 105559493
HST: 105181045
DQU: 106749864
CFO: 105259420
LHU: 105677426
PGC: 109859877
OBO: 105286430
PCF: 106785427
MDL: 103570096
TCA: 658584
DPA: 109543624
ATD: 109601527
API: 100158883
DNX: 107164646
AGS: 114126871
RMD: 113555018
BTAB: 109029618
ZNE: 110836732
CEL: CELE_W07E11.1(W07E11.1)
CBR: CBG01975
BMY: Bm1_40910
ATH: AT5G53460(GLT1)
ALY: 9300320
CRB: 17876423
BRP: 103857079
BOE: 106332590
RSZ: 108845736
THJ: 104811925
CPAP: 110823143
CIT: 102620225
TCC: 18605743
GRA: 105765457
GHI: 107947250
GAB: 108479092
EGR: 104437859
GMX: 100815931
GSJ: 114410308
VRA: 106764633
VAR: 108331410
VUN: 114194130
CCAJ: 109814577
CAM: 101509615
ADU: 107495014
AIP: 107605257
LANG: 109326556
FVE: 101309397
RCN: 112183464
PPER: 18785174
PMUM: 103333633
PAVI: 110767133
MDM: 103443818
ZJU: 107414598
CSV: 101213224
CMO: 103485701
MCHA: 111011404
CMAX: 111482791
CMOS: 111430634
CPEP: 111810135
RCU: 8274353
JCU: 105648339
POP: 7453835
PEU: 105110510
VVI: 100246868
SLY: 101254281
SPEN: 107013700
SOT: 102580516
CANN: 107855963
NSY: 104244568
NAU: 109213942
INI: 109183410
SIND: 105160371
OEU: 111405628
LSV: 111918005
BVG: 104888263
SOE: 110783090
DOSA: Os05t0555600-01(Os05g0555600)
OBR: 102713634 102721892(NGS)
ATS: 109760356(LOC109760356)
SBI: 8068026
SITA: 101785947
DCT: 110110468
PEQ: 110020245
AOF: 109840747
ATR: 18442390
PPP: 112283025
CRE: CHLREDRAFT_205746(GSN1)
APRO: F751_6615
MIS: MICPUN_105473(GLT)
SCE: YDL171C(GLT1)
ERC: Ecym_4713
KMX: KLMA_50304(GLT1)
NCS: NCAS_0A14190(NCAS0A14190)
NDI: NDAI_0A01860(NDAI0A01860)
TPF: TPHA_0F03070(TPHA0F03070)
TDL: TDEL_0C01870(TDEL0C01870)
PIC: PICST_87428(GLT1)
SPAA: SPAPADRAFT_141734(GLT1)
CAL: CAALFM_C106550WA(GLT1)
NCR: NCU01744(en(am)-2)
NTE: NEUTE1DRAFT65142(NEUTE1DRAFT_65142)
MGR: MGG_07187
SSCK: SPSK_08269
TRE: TRIREDRAFT_122287(glt1)
MAW: MAC_00032
MAJ: MAA_01819
CMT: CCM_03495
BFU: BCIN_15g02460(Bcglt1)
MBE: MBM_04374
ANI: AN5134.2
ANG: ANI_1_1272064(An07g09920)
PBL: PAAG_12483(PAAG_07998)
ABE: ARB_04215
TVE: TRV_01094
PTE: PTT_08692
SPO: SPAPB1E7.07(glt1)
CNE: CNJ02910
CNB: CNBJ0620
TASA: A1Q1_06977
ABP: AGABI1DRAFT104661(AGABI1DRAFT_104661)
ABV: AGABI2DRAFT176670(AGABI2DRAFT_176670)
SLA: SERLADRAFT_357441(NADH-GOGAT)
MGL: MGL_2017
MRT: MRET_1549
PTI: PHATRDRAFT_51214(GltX)
 » show all
Reference
1  [PMID:4362465]
  Authors
Roon RJ, Even HL, Larimore F
  Title
Glutamate synthase: properties of the reduced nicotinamide adenine dinucleotide-dependent enzyme from Saccharomyces cerevisiae.
  Journal
J Bacteriol 118:89-95 (1974)
DOI:10.1128/JB.118.1.89-95.1974
Reference
2  [PMID:21790]
  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
Eur J Biochem 79:355-62 (1977)
DOI:10.1111/j.1432-1033.1977.tb11816.x
Reference
3  [PMID:7047525]
  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
4  [PMID:16666762]
  Authors
Anderson MP, Vance CP, Heichel GH, Miller SS
  Title
Purification and Characterization of NADH-Glutamate Synthase from Alfalfa Root Nodules.
  Journal
Plant Physiol 90:351-8 (1989)
DOI:10.1104/pp.90.1.351
Reference
5  [PMID:18182018]
  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
Plant Cell Environ 31:454-72 (2008)
DOI:10.1111/j.1365-3040.2008.01774.x
Other DBs
ExplorEnz - The Enzyme Database: 1.4.1.14
IUBMB Enzyme Nomenclature: 1.4.1.14
ExPASy - ENZYME nomenclature database: 1.4.1.14
BRENDA, the Enzyme Database: 1.4.1.14
CAS: 65589-88-0

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