AGLUS_THESQ
ID AGLUS_THESQ Reviewed; 507 AA.
AC B1L993; Q9EVU3;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Archaeal-type glutamate synthase [NADPH] {ECO:0000303|PubMed:11230537, ECO:0000312|EMBL:ACB08891.1};
DE EC=1.4.1.13 {ECO:0000250|UniProtKB:Q58746, ECO:0000312|EMBL:ACB08891.1};
DE AltName: Full=Archaeal-type NADPH-GOGAT {ECO:0000250|UniProtKB:Q58746};
GN Name=gltB {ECO:0000312|EMBL:CAC21217.1}; OrderedLocusNames=TRQ2_0537;
OS Thermotoga sp. (strain RQ2).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga;
OC unclassified Thermotoga.
OX NCBI_TaxID=126740;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RQ2;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D.B., Goodwin L., Pitluck S., Saunders E., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga sp. RQ2.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAC21217.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-402, AND PHYLOGENETIC STUDY.
RC STRAIN=RQ2 {ECO:0000312|EMBL:CAC21217.1};
RX PubMed=11230537; DOI=10.1093/oxfordjournals.molbev.a003812;
RA Nesbo C.L., L'Haridon S., Stetter K.O., Doolittle W.F.;
RT "Phylogenetic analyses of two 'archaeal' genes in thermotoga maritima
RT reveal multiple transfers between archaea and bacteria.";
RL Mol. Biol. Evol. 18:362-375(2001).
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:0000250|UniProtKB:Q58746};
CC -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210;
CC Evidence={ECO:0000250|UniProtKB:Q58746};
CC -!- SIMILARITY: Belongs to the glutamate synthase family. {ECO:0000255}.
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DR EMBL; CP000969; ACB08891.1; -; Genomic_DNA.
DR EMBL; AJ401004; CAC21217.1; -; Genomic_DNA.
DR RefSeq; WP_004083229.1; NC_010483.1.
DR AlphaFoldDB; B1L993; -.
DR SMR; B1L993; -.
DR EnsemblBacteria; ACB08891; ACB08891; TRQ2_0537.
DR KEGG; trq:TRQ2_0537; -.
DR HOGENOM; CLU_023342_1_1_0; -.
DR OMA; CAWGIAT; -.
DR OrthoDB; 151647at2; -.
DR Proteomes; UP000001687; 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; 3.20.20.70; -; 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 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 PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 3: Inferred from homology;
KW 4Fe-4S; Amino-acid biosynthesis; Flavoprotein; FMN; Glutamate biosynthesis;
KW Iron; Iron-sulfur; Metal-binding; NADP; Oxidoreductase; Repeat.
FT CHAIN 1..507
FT /note="Archaeal-type glutamate synthase [NADPH]"
FT /id="PRO_0000420609"
FT DOMAIN 10..39
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 41..70
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 19
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
FT BINDING 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
FT BINDING 29
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
FT BINDING 50
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
FT BINDING 53
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
FT BINDING 56
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
FT BINDING 60
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
SQ SEQUENCE 507 AA; 55199 MW; C59B631742EDB9C9 CRC64;
MAKRKVPPEF VVERDDYKCI RCLACVRVCS YGANFYDENA NRVYTENTKC VGCHFCEAIC
PTEAITVRKN DFDIRPLAHW TPEHLIGIMK QAETGGVLLT SMGNDRPYFS YFDRIVLNAS
QVTNPSIDPL REPMEIRTYI GRKEEKLEIE EDEDGTVKLK TEIAPQLKLE VPVMFTAMSY
GSISLNAILS LARAARTVGT FFNTGEGGLP KELREFKDNM IVQVASGRFG VSADYLNAGS
AVEIKIGQGA KPGIGGHLPG EKVTEPISET RMIPVGTDAL SPAPHHDIYS IEDLRQLIYA
IKEATRYEKP VGVKIAAVHN VAPIAAGAVR AGADYIVIDG IRGGTGAAPK ITRDHVGIPI
EFAVAVVDQR LREEGIRHMA SIVVAGGIRN SADVIKAIAL GADAVYIGTA ALISLGCHLC
QTCYLGKCNW GIATQDPKLT KRLNPEIGAR RAANLLRAWA HEIKEILGGM GINAIESLRG
NREVLRGVGL HEYELKLLGI KPAGEAW
