ID A0A0S8DJE7_9PROT Unreviewed; 558 AA.
AC A0A0S8DJE7;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Glutamate synthase {ECO:0000313|EMBL:KPK35572.1};
GN ORFNames=AMJ66_00820 {ECO:0000313|EMBL:KPK35572.1};
OS Betaproteobacteria bacterium SG8_40.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1703389 {ECO:0000313|EMBL:KPK35572.1, ECO:0000313|Proteomes:UP000051602};
RN [1] {ECO:0000313|EMBL:KPK35572.1, ECO:0000313|Proteomes:UP000051602}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG8_40 {ECO:0000313|EMBL:KPK35572.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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:KPK35572.1}.
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DR EMBL; LJTS01000008; KPK35572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8DJE7; -.
DR PATRIC; fig|1703389.3.peg.1354; -.
DR Proteomes; UP000051602; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR023753; FAD/NAD-binding_dom.
DR InterPro; IPR009051; Helical_ferredxn.
DR PANTHER; PTHR43100:SF2; FERREDOXIN-DEPENDENT GLUTAMATE SYNTHASE, CHLOROPLASTIC-LIKE; 1.
DR PANTHER; PTHR43100; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF07992; Pyr_redox_2; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 2.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
PE 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 454..483
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 513..543
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
SQ SEQUENCE 558 AA; 61610 MW; E51DA66D49D684EF CRC64;
MINWTSNVFP GVLGRTCDRP CEPACRRGRV EDHNQEKPEP VAICRLKRVA ADSKNDIRER
LPKPPSQGNG KRVACIGAGP ASLTVARDLA PLGYEVTIFD QDPRAGGMIR SQIPRFRLPE
DVIDEEVGYV IDTGVEFRGG VRINSMAKLL GEGFDAIFVG TGAPRGRDLD LPGRKEAAKN
IHIGIDWLSS VSFGHIDKVG KRVIVLGGGN TAMDCCRTAR RLGGEDVKVV VRSGFEEMKA
SPWEKEDAMH EGIPILNFLV PKEFVHDDGK LTGVVFEKVQ AVYDARGRRQ LVPTGDPDEH
FECDDVLVAV GQENAFSWIE RDCGIEFNDW GMPVVDETTL QSSLPGVLFG GDAAFGPKNI
IWAVAHGHEA AISIDRLCHD EDTADRPPPL VNLVSQKMGI HEWTYDNDIS NDLRHKVPLR
EQKIALKNIN VEVELGFDQK LAFDEAQRCL NCDVQTVFSS PLCIECDACV DICPMDCITF
TEDGEEEELR GRLNAPAENP LQDLYVAGAL KTGRIMVKDE DVCLHCGLCA ERCPTGAWDM
RKFLLHMTPA GQGCRDRK
//