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Database: UniProt
Entry: Q58746
LinkDB: Q58746
Original site: Q58746 
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   16-JAN-2019, entry version 107.
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 /
OS   JCM 10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci;
OC   Methanococcales; 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.,
RA   Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D.,
RA   Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I.,
RA   Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A.,
RA   Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D.,
RA   Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C.,
RA   Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M.,
RA   Klenk H.-P., 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-
CC         glutamine + NADPH; Xref=Rhea:RHEA:15501, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349, 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.
CC       {ECO:0000305}.
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   ProteinModelPortal; 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   eggNOG; COG0069; LUCA.
DR   InParanoid; Q58746; -.
DR   OMA; CAWGIAT; -.
DR   OrthoDB; 14505at2157; -.
DR   PhylomeDB; Q58746; -.
DR   BioCyc; MJAN243232:G1GKE-1464-MONOMER; -.
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; IPR002932; Glu_synthdom.
DR   Pfam; PF01645; Glu_synthase; 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; Complete proteome; Flavoprotein; FMN;
KW   Glutamate biosynthesis; Iron; Iron-sulfur; Metal-binding; NADP;
KW   Oxidoreductase; Reference proteome; Repeat.
FT   CHAIN         1    510       Archaeal glutamate synthase [NADPH].
FT                                /FTId=PRO_0000170804.
FT   DOMAIN       10     37       4Fe-4S ferredoxin-type 1.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   DOMAIN       38     68       4Fe-4S ferredoxin-type 2.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00711}.
FT   METAL        19     19       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        22     22       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        25     25       Iron-sulfur 1 (4Fe-4S). {ECO:0000250}.
FT   METAL        29     29       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        48     48       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        51     51       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        54     54       Iron-sulfur 2 (4Fe-4S). {ECO:0000250}.
FT   METAL        58     58       Iron-sulfur 1 (4Fe-4S). {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
//
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