ID   A0A1H8CKQ1_9BACT        Unreviewed;       787 AA.
AC   A0A1H8CKQ1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=Glutamate synthase (NADPH/NADH) small chain {ECO:0000313|EMBL:SEM95610.1};
GN   ORFNames=SAMN04487902_105167 {ECO:0000313|EMBL:SEM95610.1};
OS   Prevotella sp. ne3005.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=1761887 {ECO:0000313|EMBL:SEM95610.1, ECO:0000313|Proteomes:UP000199132};
RN   [1] {ECO:0000313|Proteomes:UP000199132}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NE3005 {ECO:0000313|Proteomes:UP000199132};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOCK01000005; SEM95610.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H8CKQ1; -.
DR   STRING; 1761887.SAMN04487902_105167; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000199132; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd06219; DHOD_e_trans_like1; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR019480; Dihydroorotate_DH_Fe-S-bd.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   InterPro; IPR006004; SudA-like.
DR   NCBIfam; TIGR01316; gltA; 1.
DR   PANTHER; PTHR42783; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   PANTHER; PTHR42783:SF3; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   Pfam; PF10418; DHODB_Fe-S_bind; 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; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000199132}.
FT   DOMAIN          1..95
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   787 AA;  85420 MW;  BDED81DBF90AD34B CRC64;
     MNKIVRKEQF SEKVFLFEIE APLIAKSRKA GNFVIVRVGK KGERMPLTIA AADIEKGTIT
     LVVQMVGLSS KKLCALNVGD YVTDVVGPLG NPTKIEKYGT VVCAGGGLGV APMLPIIQAL
     KAAGNRVLSV MAGRSKDLII LEDKVRESSD EVIIMTDDGS YGEKGVVTVG IEKFIEQEPH
     VDKVFAIGPP IMMKFSNLTA QKHNIPCEVS LNTIMVDGTG MCGACRLTIG GKTKFVCIDG
     PEFDGALVDW DEMFKRMGTF KREEQEELAH YEEHLDSIED GKLKMESSKT TDVVMDSDPT
     NDTIEVLTDR NAAWRDELRK SMKPKERTQI ERVIMPELDP VYRATTRTEE VNIGLTKEMA
     MTEAKRCLDC AKPSCVEGCP VNINIPSFIK NIERGQFLAA AKVLKNTSAL PAVCGRVCPQ
     EKQCESKCIH LKMNEPAVAI GYLERFAADF ERESGNISLP EIAPANGIKI AVVGSGPAGL
     SFAGDMVKKG YDVYVFEALH EIGGVLKYGI PEFRLPNKIV DVEIENLAKM GVHFQTDVIV
     GKTISVEQLE AQGFKGIFVG SGAGLPNFMN IPGENSINIM SSNEYLTRVN LMDAANPKTD
     TPLNPAKSVL VVGGGNTAMD SCRTAKRLGA EVTLVYRRSE VEMPARLEEV KHAKEEGINF
     LTLHNPIEYI ADEQGAVKQA VLQVMELGEP DASGRRSPVP VEGKTVTLDV DQVIVAVGVS
     PNPLVPKSIQ GLELGRKNTI AVNDDMQSSR AEIFAGGDIV RGGATVILAM GDGRRAALNM
     DKHLRGL
//