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Database: UniProt
Entry: D1QUH1_9BACT
LinkDB: D1QUH1_9BACT
Original site: D1QUH1_9BACT 
ID   D1QUH1_9BACT            Unreviewed;       767 AA.
AC   D1QUH1;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   SubName: Full=Glutamate synthase (NADPH), homotetrameric {ECO:0000313|EMBL:EFB31095.1};
DE            EC=1.4.1.13 {ECO:0000313|EMBL:EFB31095.1};
GN   Name=gltA {ECO:0000313|EMBL:EFB31095.1};
GN   ORFNames=HMPREF0971_02654 {ECO:0000313|EMBL:EFB31095.1};
OS   Prevotella oris F0302.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Prevotella.
OX   NCBI_TaxID=649760 {ECO:0000313|EMBL:EFB31095.1, ECO:0000313|Proteomes:UP000004079};
RN   [1] {ECO:0000313|EMBL:EFB31095.1, ECO:0000313|Proteomes:UP000004079}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0302 {ECO:0000313|EMBL:EFB31095.1,
RC   ECO:0000313|Proteomes:UP000004079};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
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:EFB31095.1}.
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DR   EMBL; ACUZ02000046; EFB31095.1; -; Genomic_DNA.
DR   RefSeq; WP_004374986.1; NZ_GG703888.1.
DR   AlphaFoldDB; D1QUH1; -.
DR   STRING; 649760.HMPREF0971_02654; -.
DR   HOGENOM; CLU_011095_1_0_10; -.
DR   Proteomes; UP000004079; Unassembled WGS sequence.
DR   GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; 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; IPR001433; OxRdtase_FAD/NAD-bd.
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:SF1; OXIDOREDUCTASE AEGA-RELATED; 1.
DR   Pfam; PF10418; DHODB_Fe-S_bind; 1.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF00175; NAD_binding_1; 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   Oxidoreductase {ECO:0000313|EMBL:EFB31095.1}.
FT   DOMAIN          1..95
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          270..309
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   767 AA;  83373 MW;  27ED26735F5DB552 CRC64;
     MNKIISKRQF SEKVFCFDIE APLIAQSRRA GNFVIVRVDK NSERMPLTIA DADKVRGTIK
     LVVQKVGLSS TKLCNLNEGD DVADVVGPLG NPTHIENFGT VICAGGGVGV APMLPIIRAL
     KEAGNRVLSV LAGRNKELII LEDEVRASSN QTIIMTDDGS YGEKGVVTVG IEKLIQQEHI
     DKAFAIGPPI MMKFCCLLTQ KYNIPTDVSL NTIMVDGTGM CGACRLTIGG KTKFVCIDGP
     EFDGALVDWD EMFKRMGTFK AVEKEEMEHY QEHLCTPETE PSAQSASPTP LPKHTPLPQQ
     EPLKAKDRVK IPRVRMPELD PAYRATTRLE EVNQGLTVEM AMREAQRCLD CKHPSCVEGC
     PVNINIPGFI KQIEKGEFIE AVRILKQTSA LPAVCGRVCP QEKQCESRCI HHKMKSEPVA
     IGYLERFAAD YERESGQTVL PEMAASNGIK VAVVGSGPSG LSFAGDMAKN GFDVYVFEAL
     HEIGGVLKYG IPEFRLPNRI VEAEIDNLRK MGVHFQTDVI IGKTISIAEL KAKGFQGIFV
     GSGAGLPNFM DIPGENALNI MSSNEYLTRV NLMDAANPHT DTPINLGKKV LVVGGGNTAM
     DSSRTAKRLG ADVTLVYRRS EAEMPARIEE VKHAKEEGIQ FLTLHNPKEY LTDDNGAVKA
     AILDVMQLGE PDQSGRRRPE TTGQTITIVC DQVIVAVGVS PNPLVPQSIE GLALGRKNTI
     AVNEQMQSNL PEIYAGGDIV RGGATVILAM GDGRRAAENM AKQLTKS
//
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