AGLUS_THENN
ID AGLUS_THENN Reviewed; 507 AA.
AC B9KBQ2; Q9EVU9;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Archaeal-type glutamate synthase [NADPH] {ECO:0000303|PubMed:11230537, ECO:0000312|EMBL:ACM22448.1};
DE EC=1.4.1.13 {ECO:0000250|UniProtKB:Q58746};
DE AltName: Full=Archaeal-type NADPH-GOGAT {ECO:0000250|UniProtKB:Q58746};
GN Name=gltB {ECO:0000312|EMBL:CAC21395.1}; OrderedLocusNames=CTN_0272;
OS Thermotoga neapolitana (strain ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=309803;
RN [1] {ECO:0000312|EMBL:ACM22448.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E;
RA Lim S.K., Kim J.S., Cha S.H., Park B.C., Lee D.S., Tae H.S., Kim S.-J.,
RA Kim J.J., Park K.J., Lee S.Y.;
RT "The genome sequence of the hyperthermophilic bacterium Thermotoga
RT neapolitana.";
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAC21395.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 95-402, AND PHYLOGENETIC STUDY.
RC STRAIN=ATCC 49049 / DSM 4359 / NBRC 107923 / NS-E
RC {ECO:0000312|EMBL:CAC21395.1};
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; CP000916; ACM22448.1; -; Genomic_DNA.
DR EMBL; AJ400998; CAC21395.1; -; Genomic_DNA.
DR RefSeq; WP_015918777.1; NC_011978.1.
DR AlphaFoldDB; B9KBQ2; -.
DR SMR; B9KBQ2; -.
DR STRING; 309803.CTN_0272; -.
DR EnsemblBacteria; ACM22448; ACM22448; CTN_0272.
DR KEGG; tna:CTN_0272; -.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG1146; Bacteria.
DR HOGENOM; CLU_023342_1_1_0; -.
DR OMA; CAWGIAT; -.
DR Proteomes; UP000000445; 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_0000420610"
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; 55120 MW; DE7AE1A1C23E894A CRC64;
MAKRKVPAEF VVERDDYKCI RCLACVRVCS YGANYYDENA NRVYTENYKC VGCHFCEAIC
PTEAITVRRN NFDIRPLAHW TPEHLIGIMK QADTGGVLLT SMGNDRPYFS YFDRIVLNAS
QVTNPSIDPL REPMEIRTYI GRKEAKLEIE EDGEGNVALK TEIAPQLKLE VPVMFTAMSY
GSISLNALLS LARAARTIGT FFNTGEGGLP KELREFKDNM IVQVASGRFG VSADYLNAGS
AVEIKIGQGA KPGIGGHLPG EKVTEPISET RMIPVGTDAL SPAPHHDIYS IEDLRQLIYA
IKEATRYEKP VGVKIAAVHN VAPIAAGMVR AGADYIVIDG IRGGTGAAPK VTRDHVGIPI
EFAIAVVDQR LREEGIRHMA SIVVAGGIRN SADVIKAIAL GADAVYIGTA ALVALGCHLC
QTCYLGKCNW GIATQDPKLT KRLNPEIGAR RAANLLRAWA HEIKEILGGM GINAIESLRG
NREALRGVGL HEYELKLLGI KPAGEAW
