KEGG   ENZYME: 1.4.7.1Help
Entry
EC 1.4.7.1                  Enzyme                                 

Name
glutamate synthase (ferredoxin);
ferredoxin-dependent glutamate synthase;
ferredoxin-glutamate synthase;
glutamate synthase (ferredoxin-dependent)
Class
Oxidoreductases;
Acting on the CH-NH2 group of donors;
With an iron-sulfur protein as acceptor
BRITE hierarchy
Sysname
L-glutamate:ferredoxin oxidoreductase (transaminating)
Reaction(IUBMB)
2 L-glutamate + 2 oxidized ferredoxin = L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+ (overall reaction) [RN:R00021];
(1a) L-glutamate + NH3 = L-glutamine + H2O [RN:R00256];
(1b) L-glutamate + 2 oxidized ferredoxin + H2O = NH3 + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+ [RN:R10086]
Reaction(KEGG)
Substrate
L-glutamate [CPD:C00025];
oxidized ferredoxin [CPD:C00139];
NH3 [CPD:C00014];
H2O [CPD:C00001]
Product
L-glutamine [CPD:C00064];
2-oxoglutarate [CPD:C00026];
reduced ferredoxin [CPD:C00138];
H+ [CPD:C00080];
H2O [CPD:C00001];
NH3 [CPD:C00014]
Comment
Binds a [3Fe-4S] cluster as well as FAD and FMN. 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. The NH3 is channeled through a 24 A channel in the active protein. No hydrolysis of glutamine takes place without ferredoxin and 2-oxoglutarate being bound to the protein [5,6].
History
EC 1.4.7.1 created 1976, modified 2012
Pathway
ec00630  Glyoxylate and dicarboxylate metabolism
ec00910  Nitrogen metabolism
ec01120  Microbial metabolism in diverse environments
Orthology
K00284  glutamate synthase (ferredoxin)
Genes
ATH: AT2G41220(GLU2) AT5G04140(GLU1)
ALY: ARALYDRAFT_483191 ARALYDRAFT_487193(GLU1)
CRB: 17889161
CSAT: 104708708 104734430 104768604 104782609 104785266 104793031
EUS: EUTSA_v10012425mg EUTSA_v10016134mg
BRP: 103847326 103857972 103865867
BNA: 106352787 106372522 106372673 106391644 106431110
BOE: 106317861 106335201 106342177
THJ: 104803262 104816414
CIT: 102609089
TCC: 18598741
GRA: 105786202
EGR: 104444178
GMX: 548016(GLU)
VRA: 106752554
VAR: 108328874
CAM: 101506279
ADU: 107492689
AIP: 107645553
LJA: Lj1g3v4154900.1(Lj1g3v4154900.1)
LANG: 109343289
FVE: 101314871
PPER: 18770391
PMUM: 103341391
PXB: 103928813
CSV: 101214380
CMO: 103486888
RCU: 8270489
JCU: 105642370
VVI: 100233082
SLY: 101246028
SPEN: 107013679
SOT: 102600112
INI: 109161932
SIND: 105159899
HAN: 110928568
BVG: 104889481
SOE: 110777056
NNU: 104611350
OSA: 4344164
OBR: 102718939
BDI: 100827937
SBI: 8073135
ZMA: 542710(fgs1)
SITA: 101766581
MUS: 103976157
ATR: 18444596
CRE: CHLREDRAFT_140487(GSF1)
VCN: VOLCADRAFT_127156(glu1)
MIS: MICPUN_63658(GLU)
CME: CymeCp051(gltB)
TPS: THAPSDRAFT_269900(glsF)
BCN: Bcen_2705
BCJ: BCAL0289(glt1)
BAM: Bamb_0321
BMU: Bmul_0305
BMJ: BMULJ_02949(gltS)
RFR: Rfer_2933
PNA: Pnap_0683
VEI: Veis_2395
GLO: Glov_3016
GBM: Gbem_2866(gltB)
GEM: GM21_1350
GEB: GM18_2725
ADE: Adeh_0817
BHA: BH1728(gltA)
BCE: BC3646
BCZ: BCE33L3348(gltB)
BTK: BT9727_3397(gltB)
BCL: ABC2035(gltA)
BPF: BpOF4_15820(gltA)
OIH: OB3408
PPY: PPE_01118
PPO: PPM_1088(gltA)
PMS: KNP414_07369(gltB2)
PMW: B2K_34950
CBK: CLL_A1048(gltA)
CBT: CLH_0984(gltA)
CBE: Cbei_4204
BPB: bpr_I0123(gltB)
DSY: DSY4385
DHD: Dhaf_0946
DRM: Dred_2805
DAE: Dtox_3758
PTH: PTH_0734(GltB)
SGY: Sgly_2702
HMO: HM1_1037(gltB)
AWO: Awo_c07380(gltA)
OVA: OBV_07580(gltB)
TMR: Tmar_0631
VPR: Vpar_1637
MED: MELS_0304
NCA: Noca_0279
SYN: sll1499(gltB) sll1502(gltB)
SYZ: MYO_130230(gltB) MYO_14470(gltB)
SYY: SYNGTS_0442(gltB) SYNGTS_2989(gltB)
SYT: SYNGTI_0442(gltB) SYNGTI_2988(gltB)
SYS: SYNPCCN_0442(gltB) SYNPCCN_2987(gltB)
SYQ: SYNPCCP_0442(gltB) SYNPCCP_2987(gltB)
SYW: SYNW2132(glsF)
SYC: syc0650_c(glsF)
SYG: sync_0387
SYR: SynRCC307_2164(gltS)
SYX: SynWH7803_0385(gltS)
SYP: SYNPCC7002_A2393(gltS)
CYA: CYA_2704(gltS)
CYB: CYB_1253(gltS)
TEL: tll1368(glsF)
THN: NK55_02305(glsF)
PMA: Pro_1668(glsF)
PMM: PMM1512(glsF)
PMT: PMT_1777
PMB: A9601_17161(gltB)
PMC: P9515_16921(gltB)
PMF: P9303_23581(gltB)
PMG: P9301_17041(gltB)
PMH: P9215_17801(gltB)
PMJ: P9211_16351(gltB)
PME: NATL1_19531(gltB)
AMR: AM1_1662(gltB) AM1_6366
MAR: MAE_07560(gltB) MAE_29110(glsF)
CYT: cce_4353(glsF)
TER: Tery_0466
ARP: NIES39_J05540(glsF)
GVI: gvip210(glsF)
GLJ: GKIL_0118(gltS)
ANA: alr4344(gltS)
AVA: Ava_1294
NAZ: Aazo_0653
ANB: ANA_C10135(gltS)
RCA: Rcas_1903
CAU: Caur_3258
CAG: Cagg_0145
HAU: Haur_4476
CAP: CLDAP_26600(gltB)
DGE: Dgeo_2626
TRA: Trad_0209
TTR: Tter_0474
OTE: Oter_0894
CAA: Caka_1869
IPA: Isop_2214
LIL: LB_286(gltB2)
LIC: LIC_20220(gltB)
RMR: Rmar_1260
GFO: GFO_2908(gltB)
FJO: Fjoh_2161
FBR: FBFL15_1970(gltB)
ZPR: ZPR_3938
CTE: CT0401(gltB)
CPC: Cpar_1492
CCH: Cag_0186
CLI: Clim_1937
PVI: Cvib_0558
PLT: Plut_0502
PPH: Ppha_0781
PAA: Paes_0612
PMO: Pmob_1794
MOX: DAMO_0867(gltB)
 » show all
Taxonomy
Reference
1
  Authors
Galvan, F., Marquez, A.J. and Vega, J.M.
  Title
Purification and molecular properties of ferredoxin-glutamate synthase from Chlamydomonas reinhardii.
  Journal
Planta 162 (1984) 180-187.
Reference
2  [PMID:4423889]
  Authors
Lea PJ, Miflin BJ.
  Title
Alternative route for nitrogen assimilation in higher plants.
  Journal
Nature. 251 (1974) 614-6.
Reference
3  [PMID:12069605]
  Authors
Ravasio S, Dossena L, Martin-Figueroa E, Florencio FJ, Mattevi A, Morandi P, Curti B, Vanoni MA
  Title
Properties of the recombinant ferredoxin-dependent glutamate synthase of Synechocystis PCC6803. Comparison with the Azospirillum brasilense NADPH-dependent enzyme and its isolated alpha subunit.
  Journal
Biochemistry. 41 (2002) 8120-33.
Reference
4  [PMID:10898944]
  Authors
Navarro F, Martin-Figueroa E, Candau P, Florencio FJ
  Title
Ferredoxin-dependent iron-sulfur flavoprotein glutamate synthase (GlsF) from the  Cyanobacterium synechocystis sp. PCC 6803: expression and assembly in Escherichia coli.
  Journal
Arch. Biochem. Biophys. 379 (2000) 267-76.
Reference
5  [PMID:11967268]
  Authors
van den Heuvel RH, Ferrari D, Bossi RT, Ravasio S, Curti B, Vanoni MA, Florencio FJ, Mattevi A
  Title
Structural studies on the synchronization of catalytic centers in glutamate synthase.
  Journal
J. Biol. Chem. 277 (2002) 24579-83.
Reference
6  [PMID:12818206]
  Authors
van den Heuvel RH, Svergun DI, Petoukhov MV, Coda A, Curti B, Ravasio S, Vanoni MA, Mattevi A
  Title
The active conformation of glutamate synthase and its binding to ferredoxin.
  Journal
J. Mol. Biol. 330 (2003) 113-28.
Other DBs
ExplorEnz - The Enzyme Database: 1.4.7.1
IUBMB Enzyme Nomenclature: 1.4.7.1
ExPASy - ENZYME nomenclature database: 1.4.7.1
BRENDA, the Enzyme Database: 1.4.7.1
CAS: 62213-56-3

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