ID   A0A1Q3L8G8_9BACT        Unreviewed;       474 AA.
AC   A0A1Q3L8G8;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Glutamate synthase {ECO:0000313|EMBL:OJU41612.1};
GN   ORFNames=BGN96_02520 {ECO:0000313|EMBL:OJU41612.1};
OS   Bacteroidales bacterium 45-6.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX   NCBI_TaxID=1895719 {ECO:0000313|EMBL:OJU41612.1, ECO:0000313|Proteomes:UP000185892};
RN   [1] {ECO:0000313|EMBL:OJU41612.1, ECO:0000313|Proteomes:UP000185892}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=45-6 {ECO:0000313|EMBL:OJU41612.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OJU41612.1}.
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; MKRS01000723; OJU41612.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3L8G8; -.
DR   Proteomes; UP000185892; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR006005; Glut_synth_ssu1.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   NCBIfam; TIGR01317; GOGAT_sm_gam; 1.
DR   PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   PANTHER; PTHR43100:SF1; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 2.
PE   4: Predicted;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW   Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          25..129
FT                   /note="Dihydroprymidine dehydrogenase"
FT                   /evidence="ECO:0000259|Pfam:PF14691"
FT   DOMAIN          144..460
FT                   /note="FAD/NAD(P)-binding"
FT                   /evidence="ECO:0000259|Pfam:PF07992"
SQ   SEQUENCE   474 AA;  51902 MW;  AFF5635BE164D19F CRC64;
     MGNPKAFLTV KRKEAGYRPV QERILDFGEV EQTLNTEDRR EQAARCMDCG IPFCHWGCPL
     GNKMPEWQDY IYKGNWKLGA DVLQQTNDFP EFTGRICPAP CEKSCVLSIH REPVTIRENE
     AAVMELAFNA GFIIPVPPKT RTGKKVAVIG SGPAGLAVAN QLNHKGHEVT VYEKSANIGG
     LLRYGIPDFK LNKNIIERRV NLMLAEGVKF VTGVEVGKDI PGKELLEGND AVCLAIGSQV
     PRDLKVEGRD LKGVYFAMEY LGQQNKLVGK EEVPADQIIN ARGKKVLVIG GGDTGSDCIG
     TANRQEAASI LQIEILPKPE ALENMENPWP NPYPVVLKTS SSHKEGCERR WSLNTKRFIG
     ENGVLKAVEL VEVAWSKDEK GNHVMSEIGK PEIIEFDLAF LALGFVHPIQ EGLLAELGIQ
     VDGRKNVATN GSRLTSTSKV FGAGDCVSGQ SLVVKCIASG RETAAHINEF LTKE
//