AGLUS_ARCFU
ID AGLUS_ARCFU Reviewed; 511 AA.
AC O29309;
DT 09-JAN-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Archaeal glutamate synthase [NADPH];
DE EC=1.4.1.13 {ECO:0000250|UniProtKB:Q58746};
DE AltName: Full=Archaeal NADPH-GOGAT;
GN Name=gltB {ECO:0000303|PubMed:11230537}; OrderedLocusNames=AF_0953;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1] {ECO:0000312|EMBL:AAB90287.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2] {ECO:0000305}
RP PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND 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}.
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DR EMBL; AE000782; AAB90287.1; -; Genomic_DNA.
DR PIR; A69369; A69369.
DR RefSeq; WP_010878453.1; NC_000917.1.
DR AlphaFoldDB; O29309; -.
DR SMR; O29309; -.
DR STRING; 224325.AF_0953; -.
DR PRIDE; O29309; -.
DR EnsemblBacteria; AAB90287; AAB90287; AF_0953.
DR GeneID; 1484176; -.
DR KEGG; afu:AF_0953; -.
DR eggNOG; arCOG00619; Archaea.
DR HOGENOM; CLU_023342_1_1_2; -.
DR OMA; CAWGIAT; -.
DR OrthoDB; 14505at2157; -.
DR PhylomeDB; O29309; -.
DR BRENDA; 1.4.1.13; 414.
DR Proteomes; UP000002199; 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; PF00037; Fer4; 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; 2.
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..511
FT /note="Archaeal glutamate synthase [NADPH]"
FT /id="PRO_0000420606"
FT DOMAIN 15..44
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 46..75
FT /note="4Fe-4S ferredoxin-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT BINDING 24
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
FT BINDING 27
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
FT BINDING 30
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
FT BINDING 34
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
FT BINDING 55
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
FT BINDING 58
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
FT BINDING 61
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
FT BINDING 65
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q58746"
SQ SEQUENCE 511 AA; 56204 MW; 0FA661F793D6983F CRC64;
MMLEGEFHTH MLPEFMIERR QDRCIRCRVC ERQCGFNVHW YDEEMDMMRE DEMKCVGCQR
CAVMCPTNAL VVKPHPGNYK PNANWTRERL QDLKKQAETG GVLLTGSGND KPYRIYWDHI
VLNASQVTNP SIDPLREPME LRTFLGRKQD RLEFKYSEDF EDIEITTELY PNVQIETPIV
FSAMSYGAIS YQAFKSLAMA ASEFGTLFNT GEGGLPKELR KYGKNAIVQC ASGRFGVDPE
YLNVAAVVEI KIGQGAKPGI GGHLPGEKVT LPISVTRMIP EGTDALSPAP QHDIYSIEDL
SMLIYALKEA TNYEKPVSVK IAAVHNVAAI ASGMVRAGAD IIAIDGLRGG TGAAPKMIRD
NVGIPVELAL AAVDQRLRDE GIRNKASILV AGGFRCSADV VKAIALGADA VYIGTPALVA
MGCTLCQKCH TGICNWGICT QDPYLAKRLN PEITAKRLVN LLRAWSHEIK EMLGGMGINA
IESLRGNREQ LRGVGLEDWE LEVLGIKGAG E
