AGLUS_THEMA
ID AGLUS_THEMA Reviewed; 507 AA.
AC Q9WYM8; G4FHV6;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Archaeal-type glutamate synthase [NADPH] {ECO:0000303|PubMed:11230537};
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:0000303|PubMed:11230537}; OrderedLocusNames=TM_0397;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1] {ECO:0000312|EMBL:AAD35482.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2] {ECO:0000305}
RP PHYLOGENETIC STUDY.
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}.
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; AE000512; AAD35482.1; -; Genomic_DNA.
DR PIR; F72382; F72382.
DR RefSeq; NP_228207.1; NC_000853.1.
DR RefSeq; WP_004083229.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9WYM8; -.
DR SMR; Q9WYM8; -.
DR STRING; 243274.THEMA_02745; -.
DR PRIDE; Q9WYM8; -.
DR EnsemblBacteria; AAD35482; AAD35482; TM_0397.
DR KEGG; tma:TM0397; -.
DR eggNOG; COG0069; Bacteria.
DR eggNOG; COG1146; Bacteria.
DR InParanoid; Q9WYM8; -.
DR OMA; CAWGIAT; -.
DR OrthoDB; 151647at2; -.
DR Proteomes; UP000008183; 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; Reference proteome;
KW Repeat.
FT CHAIN 1..507
FT /note="Archaeal-type glutamate synthase [NADPH]"
FT /id="PRO_0000420608"
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
