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
RSS: 109440093
ATH: AT2G41220(GLU2) AT5G04140(GLU1)
ALY: ARALYDRAFT_483191 ARALYDRAFT_487193(GLU1)
CRB: 17882431 17889161
CSAT: 104708708 104734430 104768604 104782609 104785266 104793031
EUS: EUTSA_v10012425mg EUTSA_v10016134mg
BRP: 103847326 103857972 103865867
BNA: 106352787 106372522 106372673 106391644 106394113 106394114 106431110
BOE: 106317861 106335201 106342177
THJ: 104803262 104816414
CPAP: 110822870
CIT: 102609089
TCC: 18598741
GRA: 105786202
EGR: 104444178
VRA: 106752554
VAR: 108328874
CCAJ: 109815625
CAM: 101506279
LJA: Lj1g3v4154900.1(Lj1g3v4154900.1) Lj1g3v4154900.2(Lj1g3v4154900.2) Lj1g3v4154900.3(Lj1g3v4154900.3) Lj4g3v1200810.1(Lj4g3v1200810.1)
LANG: 109343289
FVE: 101314871
PPER: 18770391
PMUM: 103341391
PAVI: 110758098
PXB: 103928813
CSV: 101214380
CMO: 103486888
MCHA: 111016634
RCU: 8270489
JCU: 105642370
VVI: 100233082
SLY: 101246028
SPEN: 107013679
SOT: 102600112
CANN: 107852264
NSY: 104241431
NTO: 104118686
INI: 109161932
SIND: 105159899
HAN: 110928568
LSV: 111891706
CCAV: 112512315
BVG: 104889481
SOE: 110777056
NNU: 104611350
OSA: 4344164
DOSA: Os07t0658400-01(Os07g0658400)
OBR: 102718939
BDI: 100827937
ATS: 109733233(LOC109733233)
SBI: 8073135
ZMA: 542710(fgs1)
SITA: 101766581
MUS: 103976157
AOF: 109849057
ATR: 18444596
CRE: CHLREDRAFT_140487(GSF1)
VCN: VOLCADRAFT_127156(glu1)
MIS: MICPUN_63658(GLU)
APRO: F751_5489
CME: CymeCp051(gltB)
GSL: Gasu_40050 JL72_p025(gltB)
CCP: CHC_1080(gltB)
TPS: THAPSDRAFT_269900(glsF)
TMR: Tmar_0631
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)
SYJ: D082_27210(glsF) D082_30770(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)
SYNR: KR49_10635
SYND: KR52_00805
SYH: Syncc8109_0331(glsF)
SYNW: SynWH8103_02451(glsF)
TEL: tll1368(glsF)
THN: NK55_02305(glsF)
CYI: CBM981_1898(gltS)
LET: O77CONTIG1_00376(gltS_1) O77CONTIG1_00377(gltS_2) O77CONTIG1_04635(gltB_2)
HHG: XM38_009140(gltS)
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)
PRM: EW15_2017
AMR: AM1_1662(gltB) AM1_6366
MAR: MAE_07560(gltB) MAE_29110(glsF)
CHON: NIES4102_36890(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)
CALH: IJ00_19245
CEO: ETSB_0993(glsF)
RCA: Rcas_1903
CAU: Caur_3258
CAG: Cagg_0145
HAU: Haur_4476
TRO: trd_1105
CAP: CLDAP_26600(gltB)
TRA: Trad_0209
GES: VT84_11790(gltS)
CTS: Ctha_0711
HHB: Hhub_1568(gltB)
HSU: HLASF_0085(gltA1)
HSF: HLASA_0085(gltA1)
HMA: rrnAC0169(gltB)
HHI: HAH_0919(gltB)
NPH: NP_1794A(gltB)
NMO: Nmlp_2987(gltB)
HMU: Hmuk_3135
HWA: HQ_1714A(gltB)
HWC: Hqrw_1833(gltB)
HVO: HVO_0869(gltB)
HME: HFX_0844(gltS)
HLA: Hlac_0912
HTU: Htur_3198
NMG: Nmag_2529(gltB)
NAT: NJ7G_2607
SALI: L593_09320
 » show all
Taxonomy
Reference
1  [PMID:24254054]
  Authors
Galvan F, Marquez AJ, Vega JM
  Title
Purification and molecular properties of ferredoxin-glutamate synthase from Chlamydomonas reinhardii.
  Journal
Planta 162:180-7 (1984)
DOI:10.1007/BF00410216
Reference
2  [PMID:4423889]
  Authors
Lea PJ, Miflin BJ.
  Title
Alternative route for nitrogen assimilation in higher plants.
  Journal
Nature 251:614-6 (1974)
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 41:8120-33 (2002)
DOI:10.1021/bi020083r
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 379:267-76 (2000)
DOI:10.1006/abbi.2000.1894
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 277:24579-83 (2002)
DOI:10.1074/jbc.M202541200
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 330:113-28 (2003)
DOI:10.1016/S0022-2836(03)00522-9
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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