ID   A0A1I1D5A2_9BURK        Unreviewed;       487 AA.
AC   A0A1I1D5A2;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Glutamate synthase (NADH) small subunit {ECO:0000313|EMBL:SFB69562.1};
GN   ORFNames=SAMN05216204_1017 {ECO:0000313|EMBL:SFB69562.1};
OS   Massilia yuzhufengensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1164594 {ECO:0000313|EMBL:SFB69562.1, ECO:0000313|Proteomes:UP000198639};
RN   [1] {ECO:0000313|EMBL:SFB69562.1, ECO:0000313|Proteomes:UP000198639}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.12041 {ECO:0000313|EMBL:SFB69562.1,
RC   ECO:0000313|Proteomes:UP000198639};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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DR   EMBL; FOLD01000001; SFB69562.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I1D5A2; -.
DR   STRING; 1164594.SAMN05216204_1017; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000198639; 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   487 AA;  53208 MW;  27D37CE701014C78 CRC64;
     MGKITGFMEF ERQEEGHLEP ADRVKNYKEF VLTLSDGQAK VQGARCMDCG IPFCNTGCPV
     NNMIPDWNDL VYHGNYRAAV ENLHSTNNFP EFTGRICPAP CESACTLGIN DDPVGIKSIE
     RKISDAGWEH GWIVPEPAAI KTGKKVAVVG SGPAGLAAAQ QLARAGHAVT VFEKSDRIGG
     LLRYGIPDFK MEKGLIDRRV EQMQAEGVIF RTGVLIGKDF PATVSNMARD TIFPEDLEKE
     FDAVVLAGGA EQPRDLPVPG RELKGVHFAM DFLPQQNRVN AGDKLKDQIK ATGKHVVVIG
     GGDTGSDCVG TSNRHGAASV TQFELMPQPP ELENKPLVWP YWPTRLRTSS SHEEGCERDW
     AVATKRLEGK GGKVERLIAC RVEWKDGKMV EVANSEFELK ADLVFLAMGF VSPVQNVLDA
     FGVQKDARGN ARASTEGDKS YQTSSSKVFA AGDMRRGQSL VVWAIREGRQ CARAVDEFLM
     GSSVLPR
//