ID G0H188_METMI Unreviewed; 510 AA.
AC G0H188;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE RecName: Full=Archaeal glutamate synthase [NADPH] {ECO:0000256|PIRNR:PIRNR006429};
DE EC=1.4.1.13 {ECO:0000256|PIRNR:PIRNR006429};
GN ORFNames=GYY_00415 {ECO:0000313|EMBL:AEK18973.1};
OS Methanococcus maripaludis X1.
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=1053692 {ECO:0000313|Proteomes:UP000008889};
RN [1] {ECO:0000313|EMBL:AEK18973.1, ECO:0000313|Proteomes:UP000008889}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=X1 {ECO:0000313|EMBL:AEK18973.1,
RC ECO:0000313|Proteomes:UP000008889};
RX PubMed=21914896; DOI=10.1128/JB.05835-11;
RA Wang X., Greenfield P., Li D., Hendry P., Volk H., Sutherland T.D.;
RT "Complete Genome Sequence of a Nonculturable Methanococcus maripaludis
RT Strain Extracted in a Metagenomic Survey of Petroleum Reservoir Fluids.";
RL J. Bacteriol. 193:5595-5595(2011).
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 ECO:0000256|PIRNR:PIRNR006429};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000256|PIRNR:PIRNR006429};
CC -!- SIMILARITY: Belongs to the glutamate synthase family.
CC {ECO:0000256|ARBA:ARBA00009716, ECO:0000256|PIRNR:PIRNR006429}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002913; AEK18973.1; -; Genomic_DNA.
DR RefSeq; WP_013998558.1; NC_015847.1.
DR AlphaFoldDB; G0H188; -.
DR DNASU; 10981503; -.
DR GeneID; 10981503; -.
DR KEGG; mmd:GYY_00415; -.
DR PATRIC; fig|1053692.7.peg.83; -.
DR HOGENOM; CLU_023342_1_1_2; -.
DR Proteomes; UP000008889; Chromosome.
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:UniProtKB-KW.
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; PF13237; Fer4_10; 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 ECO:0000256|PIRNR:PIRNR006429};
KW Flavoprotein {ECO:0000256|PIRNR:PIRNR006429};
KW FMN {ECO:0000256|PIRNR:PIRNR006429};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164,
KW ECO:0000256|PIRNR:PIRNR006429}; Iron {ECO:0000256|PIRSR:PIRSR006429-1};
KW Iron-sulfur {ECO:0000256|PIRSR:PIRSR006429-1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR006429-1};
KW NADP {ECO:0000256|PIRNR:PIRNR006429};
KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR006429}.
FT DOMAIN 10..39
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 40..68
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT BINDING 19
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 29
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 48
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
FT BINDING 58
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR006429-1"
SQ SEQUENCE 510 AA; 55169 MW; 3105312952F632CD CRC64;
MIPSTVPPKY KVFVDPERCM LCERCTTECS WGVYRRQGNK ILTYPNRCGA CLRCVSLCPR
DAITVTLNQS CGREHPVWTP EVKQDVVTQA KSGCILLSGM GNAKEYPIYF DKIVLDACQV
TNPSIDPLRE PMELRTYVGK KPEKLEFDYV EDEIDGKKVK KAKLKTKIAP NLKLDTPIMI
GHMSYGALSL NSHKAMAKAV KECGTFMGTG EGGLHRDLYG YSDNVITQVA SGRFGVNSEY
LNKGAAIEIK IGQGAKPGIG GHLPGEKVSA EVSMTRMIPQ GSDAISPAPH HDIYSIEDLA
QLIRSLKEAT RWKMPVFVKI SAVHNVSAIA NGIATSDADA VVIDGFKGGT GAAPKVFRDN
VGIPIEVAIA AVDDRLREQG NRHKISIIAS GGIRNSADVF KSIALGADAV YIGTAAMVAM
GCTVCGRCYT GQCAWGIATQ KPELVKRLEV DDAARRVANL IHAWTHEIQE LLGAAGINSI
ESLRGNRDRL RGVGLSEIEL NTLGIKQAGM
//
