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Database: UniProt
Entry: A0A1G5A6F8_9BURK
LinkDB: A0A1G5A6F8_9BURK
Original site: A0A1G5A6F8_9BURK 
ID   A0A1G5A6F8_9BURK        Unreviewed;       492 AA.
AC   A0A1G5A6F8;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=glutamate synthase (NADPH) {ECO:0000256|ARBA:ARBA00012079};
DE            EC=1.4.1.13 {ECO:0000256|ARBA:ARBA00012079};
GN   ORFNames=SAMN03159363_5155 {ECO:0000313|EMBL:SCX73424.1};
OS   Variovorax sp. EL159.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1566270 {ECO:0000313|EMBL:SCX73424.1, ECO:0000313|Proteomes:UP000199507};
RN   [1] {ECO:0000313|EMBL:SCX73424.1, ECO:0000313|Proteomes:UP000199507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EL159 {ECO:0000313|EMBL:SCX73424.1,
RC   ECO:0000313|Proteomes:UP000199507};
RA   de Groot N.N.;
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; FMUJ01000006; SCX73424.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5A6F8; -.
DR   STRING; 1566270.SAMN03159363_5155; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000199507; 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; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR017896; 4Fe4S_Fe-S-bd.
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; 2.
DR   PROSITE; PS51379; 4FE4S_FER_2; 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}.
FT   DOMAIN          37..68
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   492 AA;  53821 MW;  DD54B7DCCA416E82 CRC64;
     MGKITGFMEH ERIEEGYKPV DERVKHYKEF VVGLNTEQAK VQGARCMDCG TPFCNSGCPV
     NNIIPDFNDL VYRNDWQNAF AVLDSTNNFP EFTGRICPAP CEAACVLNVN DDAVGIKSLE
     HAIIDRAWDE GWVAPRVAKH KTGKKVAVVG AGPAGMAAAQ QLARVGHDVT LFEKNDRIGG
     LLRYGIPDFK MEKTHIDRRV EQMKAEGVIF RTGVMVGAAK DPLGKGSKVT NLAKETITPE
     QLQKEFDAVL LTGGAEQSRD LPVPGRDLDG IHFAMEFLPQ QNRVNAGDKV KGQLRADGKH
     VIVIGGGDTG SDCVGTSNRH GAVSVTQFEL MPQPPEEENR PLTWPYWPIK LRTSSSHEEG
     CEREFAISTK EFIGEKGKVT GLKTVRVEWK DGKMQEVAGS EQVLKADLVL LAMGFISPVA
     TVLDAFGVEK DARGNARATV DFIGGYATNV PKVFAAGDIR RGQSLVVWAI REGRQAARSV
     DEFLMGFSDL PR
//
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