ID A0A1F8L5W8_9CHLR Unreviewed; 486 AA.
AC A0A1F8L5W8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Glutamate synthase (NADPH), homotetrameric {ECO:0000313|EMBL:OGN81878.1};
GN ORFNames=A2X23_02585 {ECO:0000313|EMBL:OGN81878.1};
OS Chloroflexi bacterium GWC2_73_18.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797616 {ECO:0000313|EMBL:OGN81878.1, ECO:0000313|Proteomes:UP000176763};
RN [1] {ECO:0000313|EMBL:OGN81878.1, ECO:0000313|Proteomes:UP000176763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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:OGN81878.1}.
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DR EMBL; MGMJ01000113; OGN81878.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8L5W8; -.
DR STRING; 1797616.A2X23_02585; -.
DR Proteomes; UP000176763; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR028261; DPD_II.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR InterPro; IPR006004; SudA-like.
DR NCBIfam; TIGR01316; gltA; 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; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 16..124
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 140..444
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 486 AA; 51728 MW; 87EF6129277B3BF4 CRC64;
MAIDRQPMPE QPPEIRIANF EEVNLGFTHR LAIAEAERCI QCPNPVCMEG CPVRVDIPRF
LGLLEQGDLR AAAESLLGDN ALPCVTGRVC PQETQCELRC VRAKKGRPVA IGNLERYVAD
WAAQHPDQLP QTHTEPSGHR VAIVGAGPAG LTAAGELVKY GHQVTIFEAF HSPGGVLVYG
IPEFRLPTRI VEQEVERLVA QGVRIEPNVI IGRTYTLGEL GEMFDAVFIA VGAGLPVFMG
VPGENLKGVY SANEYLTRVN LMGAWTNDAD TPVLHGQRVA VIGGGNVAMD AVRTARRMGA
AEATIVYRRG REELPARVEE VHHAEQEGIR FEYLAAPVEV VGGDDGWVTG LRCIRMELGE
PDDSGRRRPV AVPGSEFVVP CDVVIVAIGT RSNPLLTSTA PGLRLTRAGY IEVDENGMTS
LPGVFAGGDI VRGSATVILA MGDGKRAARA IDNYLVAGVG AVPIAAGTRA GTPAIEAAAV
PARADA
//
