ID A0A094P7Z3_9ACTN Unreviewed; 483 AA.
AC A0A094P7Z3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Glutamate synthase small subunit {ECO:0000313|EMBL:KGA05584.1};
GN ORFNames=GM46_10875 {ECO:0000313|EMBL:KGA05584.1};
OS actinobacterium acAcidi.
OC Bacteria; Actinomycetota; Actinomycetes.
OX NCBI_TaxID=1504320 {ECO:0000313|EMBL:KGA05584.1, ECO:0000313|Proteomes:UP000029305};
RN [1] {ECO:0000313|EMBL:KGA05584.1, ECO:0000313|Proteomes:UP000029305}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Ghai R., Mizuno C.M., Picazo A., Camacho A., Rodriguez-Valera F.;
RT "Key roles for freshwater Actinobacteria revealed by deep metagenomic
RT sequencing.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
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:KGA05584.1}.
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DR EMBL; JNSG01000110; KGA05584.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094P7Z3; -.
DR PATRIC; fig|1504320.4.peg.2185; -.
DR Proteomes; UP000029305; 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 483 AA; 52854 MW; D94D1CA09BC0BA82 CRC64;
MGEPTGFIQW GRKSPKRRPI PVRVADWKEV YEPFPQSELV HQAGRCMDCG IPFCNNGCPL
GNLIPDWNDL VYRDHWYDAL ERLHATNNFP EFTGRLCPAP CESACVLGIN QDPVSIKQVE
VEIIDRAWNE GWVTPHISHH KTGKRVAVIG SGPAGLAAAQ QLTRAGHDVV VLERADRIGG
LLRYGIPEFK MEKRHIDRRV EQMKQEGTEF RTNAAVGDNV DIDVLMASHD AVVLACGATS
WRDLPVPGRE FGGIYQAMEF LPPANRVQQG DFEETSISAR GKHVVIIGGG DTGADCLGTA
IRQGAASITQ LEIMPRPPDL RAGTNPWPQW SMVYRTSSAH EEGGERVFSV NTERFLADED
GNVRSLVLNE VVFNNGKFEI VEGTERELPC DLVLLALGFV GPEKGTWLDQ LGVALDDRGN
IARTDTYATN VPGVFVAGDM GRGQSLIVWA IAEGRACAAA VDERLMGSTT LPSPIVSSAR
PMA
//