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
//