AGLUS_METJA
ID AGLUS_METJA Reviewed; 510 AA.
AC Q58746; Q4U2V1;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Archaeal glutamate synthase [NADPH];
DE EC=1.4.1.13;
DE AltName: Full=Archaeal NADPH-GOGAT;
GN OrderedLocusNames=MJ1351;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Dincturk H.B.;
RT "Putative FMN-binding domain of glutamate synthase.";
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
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 -!- COFACTOR:
CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the glutamate synthase family. {ECO:0000305}.
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DR EMBL; DQ018115; AAY33887.1; -; Genomic_DNA.
DR EMBL; L77117; AAB99362.1; -; Genomic_DNA.
DR PIR; F64468; F64468.
DR RefSeq; WP_010870869.1; NC_000909.1.
DR AlphaFoldDB; Q58746; -.
DR SMR; Q58746; -.
DR STRING; 243232.MJ_1351; -.
DR EnsemblBacteria; AAB99362; AAB99362; MJ_1351.
DR GeneID; 1452254; -.
DR KEGG; mja:MJ_1351; -.
DR eggNOG; arCOG00619; Archaea.
DR HOGENOM; CLU_023342_1_1_2; -.
DR InParanoid; Q58746; -.
DR OMA; CAWGIAT; -.
DR OrthoDB; 14505at2157; -.
DR PhylomeDB; Q58746; -.
DR BRENDA; 1.4.1.13; 3260.
DR Proteomes; UP000000805; 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; 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..510
FT /note="Archaeal glutamate synthase [NADPH]"
FT /id="PRO_0000170804"
FT DOMAIN 10..37
FT /note="4Fe-4S ferredoxin-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00711"
FT DOMAIN 38..68
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"
FT BINDING 22
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 25
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 29
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 48
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 51
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 54
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 58
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
SQ SEQUENCE 510 AA; 55454 MW; 4EE38CB9351D1CFA CRC64;
MIPSYVPPKY KVEVDPNRCM LCERCTIECS WGVYRREGDR IISYSNRCGA CHRCVVMCPR
DAITIKENAI SWRSHPLWDV DARVDIYNQA KTGCILLSGM GNAKEHPIYF DKIVLDACQV
TNPSIDPLRE PMELRTYIGK KPKQLEFEFV EEEIDGKKIK KAKLKTKIAP NLKLDTPIMI
AHMSYGALSL NAHLSFAKAV KECGTFMGTG EGGLPKALYP YADHIITQVA SGRFGVNEEY
LMKGSAIEIK IGQGAKPGIG GHLPGEKVTA EISATRMIPE GSDAISPAPH HDIYSIEDLA
QLVRSLKEAT RWKKPVFVKI AAVHNAPAIA VGIATSDADA VVIDGYKGGT GAAPKVFRDH
VGIPIEMAIA AVDQRLREEG LRNEISIIAS GGIRCSADVF KAIALGADAV YIGTAAMVAL
GCRVCGRCYT GLCAWGIATQ RPELVKRLDP EVGARRVANL IKAWTHEIKE LLGAAGINSI
ESLRGNRDRL RGVGLNEKEL EVLGIKAAGE
