ID A0A1F8LZA7_9CHLR Unreviewed; 423 AA.
AC A0A1F8LZA7;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE RecName: Full=glutamate synthase (NADPH) {ECO:0000256|ARBA:ARBA00012079};
DE EC=1.4.1.13 {ECO:0000256|ARBA:ARBA00012079};
DE Flags: Fragment;
GN ORFNames=A2Z70_04080 {ECO:0000313|EMBL:OGN91675.1};
OS Chloroflexi bacterium RBG_13_48_17.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797621 {ECO:0000313|EMBL:OGN91675.1, ECO:0000313|Proteomes:UP000180319};
RN [1] {ECO:0000313|EMBL:OGN91675.1, ECO:0000313|Proteomes:UP000180319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + L-glutamine
CC + NADPH; Xref=Rhea:RHEA:15501, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58359; EC=1.4.1.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001895};
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OGN91675.1}.
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DR EMBL; MGMO01000032; OGN91675.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8LZA7; -.
DR Proteomes; UP000180319; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:InterPro.
DR CDD; cd02808; GltS_FMN; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR024188; GltB.
DR InterPro; IPR043578; GltB_archl_type.
DR InterPro; IPR002932; Glu_synthdom.
DR PANTHER; PTHR43819:SF1; ARCHAEAL GLUTAMATE SYNTHASE [NADPH]; 1.
DR PANTHER; PTHR43819; ARCHAEAL-TYPE GLUTAMATE SYNTHASE [NADPH]; 1.
DR Pfam; PF13187; Fer4_9; 1.
DR Pfam; PF01645; Glu_synthase; 1.
DR PIRSF; PIRSF500061; GOGAT_lg2_archl; 1.
DR PIRSF; PIRSF006429; GOGAT_lg_2; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|PIRSR:PIRSR006429-1};
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|PIRSR:PIRSR006429-1};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|PIRSR:PIRSR006429-
KW 1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR006429-1}.
FT DOMAIN 9..38
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 40..69
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 18
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 21
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 24
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 28
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 49
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 52
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 55
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT NON_TER 423
FT /evidence="ECO:0000313|EMBL:OGN91675.1"
SQ SEQUENCE 423 AA; 45487 MW; 55BB6A0399E26E1A CRC64;
MKTYLPSKFI VERDSNRCIQ CQVCVNQCSF DVHHYDAQDD EVRSREENCV GCHRCVVFCP
TNAVSIRENT LTYRENYNWR PDVIEDIIKQ AETGGVLLTG MGNDKSYRVY WDHLVLNASQ
VTNPSIDPLR EPMELVTYLG RKPDNVEVNE GALSLKTKLA PQVKLDIPVM FSAMSYGAVS
INVQESLARA AIEAGTLWNT GEGGLHPKLY KYGKNTIVQV ASGRFGVNPE YLDAAAAVEI
KIGQGAKPGI GGHLPGEKVS AEVAMTRMIP EGTDALSPAP QHDIYSIEDL AQLVYALKEA
TDYTKPVSVK IAAVHNSAAI ASGMVRAGAD IIVLDGLRGS TGAAPKVIRD NVGIPIEMAL
ASVDARLRQE GIRNQASIVI AGGIRNSGDV AKAIALGADA VYIATAALMA LGCTCCQQCH
TGK
//
