ID A0A1I0QPZ6_9BACT Unreviewed; 477 AA.
AC A0A1I0QPZ6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=glutamate synthase (NADPH) {ECO:0000256|ARBA:ARBA00012079};
DE EC=1.4.1.13 {ECO:0000256|ARBA:ARBA00012079};
GN ORFNames=SAMN05216290_2562 {ECO:0000313|EMBL:SEW29517.1};
OS Roseivirga pacifica.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Roseivirgaceae;
OC Roseivirga.
OX NCBI_TaxID=1267423 {ECO:0000313|EMBL:SEW29517.1, ECO:0000313|Proteomes:UP000199437};
RN [1] {ECO:0000313|Proteomes:UP000199437}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12402 {ECO:0000313|Proteomes:UP000199437};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 L-glutamate + NADP(+) = 2-oxoglutarate + H(+) + L-glutamine
CC + NADPH; Xref=Rhea:RHEA:15501, ChEBI:CHEBI:15378, ChEBI:CHEBI:16810,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349,
CC ChEBI:CHEBI:58359; EC=1.4.1.13;
CC Evidence={ECO:0000256|ARBA:ARBA00001895};
CC -!- PATHWAY: Amino-acid biosynthesis; L-glutamate biosynthesis via GLT
CC pathway; L-glutamate from 2-oxoglutarate and L-glutamine (NADP(+)
CC route): step 1/1. {ECO:0000256|ARBA:ARBA00037898}.
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DR EMBL; FOIR01000002; SEW29517.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0QPZ6; -.
DR STRING; 1267423.SAMN05216290_2562; -.
DR OrthoDB; 9803192at2; -.
DR Proteomes; UP000199437; 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; 1.
PE 4: Predicted;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW Glutamate biosynthesis {ECO:0000256|ARBA:ARBA00023164};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000199437}.
FT DOMAIN 24..129
FT /note="Dihydroprymidine dehydrogenase"
FT /evidence="ECO:0000259|Pfam:PF14691"
FT DOMAIN 145..461
FT /note="FAD/NAD(P)-binding"
FT /evidence="ECO:0000259|Pfam:PF07992"
SQ SEQUENCE 477 AA; 52791 MW; 1B1DE0B1C502C2B8 CRC64;
MGDIKGFLKH GRAKKAYESP QERVHHFEEF SKPWAQEEYK EQAARCMDCG IPFCHEGCPL
GNKIPDFNDA VYRGEWKEAW SVLKQTNNFP EFTGRICPAP CEASCVLGLN NQAVNIEHIE
KQIAETAFLE GWETPTATTK QRPEKVAVIG SGPAGLATAE ELHKQGFQVT VFERDQEAGG
LLRYGIPDFK LDKQVVQRRV DLMKAGGIEF RTGIEIGKDI EATALKAQFD VVVLCTGSTV
PRDLDIEGRD LAGVHFAMDF LKHQNQLIAG EVTEHLPKYN AVGKQVLVIG GGDTGADCVG
TSNRQGAVKV TQIELLDKPP HARLETNPWP EWPMTLTTST SHEEGVDRDW AVLTKRFVGE
KGKLTGVETV KIKWTDKAKF QFEEIVGTEE VVPCELALLA IGFIHHEKSL SAQFGLELDP
RGNVKTTGFK ASRTNQNDKP VFAAGDCRRG QSLVVWAIAE GRRVAQAVGK QFELEKV
//