KEGG   ENZYME: 1.4.1.14Help
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
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
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
ec01130  Biosynthesis of antibiotics
Orthology
K00264  glutamate synthase (NADH)
Genes
RSS: 109439942
BFO: BRAFLDRAFT_129259
SPU: 754163
APLC: 110978866
SKO: 100371963
DME: Dmel_CG9674(CG9674)
DPO: Dpse_GA21956
DAN: Dana_GF10502
DER: 6543630
DPE: 6601003
DSI: Dsimw501_GD12441(Dsim_GD12441)
DWI: 6645095
DAZ: 108613420
DNV: 108650790
DHE: 111605684
MDE: 101893373
AAG: 5565246
AME: 413372
BIM: 100743936
BTER: 100648506
SOC: 105197574
MPHA: 105838501
AEC: 105149802
ACEP: 105627138
PBAR: 105424147
HST: 105181045
DQU: 106749864
CFO: 105259420
LHU: 105677426
PGC: 109859877
OBO: 105286430
PCF: 106785427
NVI: 100122109
MDL: 103570096
TCA: 658584
DPA: 109543624
NVL: 108563867
BMOR: 751838(Gogat)
PMAC: 106710933
HAW: 110374537
TNL: 113502498
API: 100158883
DNX: 107164646
AGS: 114126871
CLEC: 106667559
ZNE: 110836732
FCD: 110854382
TUT: 107364085
DPTE: 113798827
CEL: CELE_W07E11.1(W07E11.1)
CBR: CBG01975
BMY: Bm1_40910
TSP: Tsp_01351
PCAN: 112565988
CRG: 105337796
OBI: 106883777
SHX: MS3_01901
EGL: EGR_01992
EPA: 110251849
ADF: 107355563
PDAM: 113678838
SPIS: 111333886
ATH: AT5G53460(GLT1)
ALY: ARALYDRAFT_918424(GLT1)
CRB: 17876423
BRP: 103857079
BOE: 106332590
THJ: 104811925
CPAP: 110823143
CIT: 102620225
TCC: 18605743
GRA: 105765457
GHI: 107947250
GAB: 108479092
EGR: 104437859
CAM: 101509615
LJA: Lj0g3v0129059.1(Lj0g3v0129059.1) Lj0g3v0129059.2(Lj0g3v0129059.2) Lj0g3v0254949.2(Lj0g3v0254949.2)
FVE: 101309397
PPER: 18785174
PMUM: 103333633
PAVI: 110767133
ZJU: 107414598
CSV: 101213224
CMO: 103485701
MCHA: 111011404
RCU: 8274353
JCU: 105648339
VVI: 100246868
SLY: 101254281
SPEN: 107013700
SOT: 102580516
NSY: 104244568
NTO: 104098510
NAU: 109213942
INI: 109183410
SIND: 105160371
LSV: 111918005
BVG: 104888263
DOSA: Os05t0555600-01(Os05g0555600)
OBR: 102713634 102721892(NGS)
ATS: 109760356(LOC109760356)
DCT: 110110468
PEQ: 110020245
AOF: 109840747
ATR: 18442390
CRE: CHLREDRAFT_205746(GSN1)
MIS: MICPUN_105473(GLT)
APRO: F751_6615
SCE: YDL171C(GLT1)
ERC: Ecym_4713
KMX: KLMA_50304(GLT1)
NCS: NCAS_0A14190(NCAS0A14190)
NDI: NDAI_0A01860(NDAI0A01860)
TPF: TPHA_0F03070(TPHA0F03070)
TBL: TBLA_0A09100(TBLA0A09100)
TDL: TDEL_0C01870(TDEL0C01870)
PIC: PICST_87428(GLT1)
SPAA: SPAPADRAFT_141734(GLT1)
CAL: CAALFM_C106550WA(GLT1)
SLB: AWJ20_5040(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
ABP: AGABI1DRAFT104661(AGABI1DRAFT_104661)
ABV: AGABI2DRAFT176670(AGABI2DRAFT_176670)
SLA: SERLADRAFT_357441(NADH-GOGAT)
MGL: MGL_2017
PYO: PY17X_1011100(PY03719)
PCB: PCHAS_101040(PC000809.03.0)
SMIN: v1.2.014989.t1(symbB.v1.2.014989.t1) v1.2.017142.t1(symbB.v1.2.017142.t1) v1.2.017146.t1(symbB.v1.2.017146.t1)
PTI: PHATRDRAFT_51214(GltX)
SPAR: SPRG_06781
 » show all
Taxonomy
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)
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)
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)
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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