ID   A0A1E5Q6C6_9PROT        Unreviewed;       548 AA.
AC   A0A1E5Q6C6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Glutamate synthase {ECO:0000313|EMBL:OEJ66209.1};
GN   ORFNames=BEN30_12505 {ECO:0000313|EMBL:OEJ66209.1};
OS   Magnetovibrio blakemorei.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Magnetovibrionaceae; Magnetovibrio.
OX   NCBI_TaxID=28181 {ECO:0000313|EMBL:OEJ66209.1, ECO:0000313|Proteomes:UP000095347};
RN   [1] {ECO:0000313|Proteomes:UP000095347}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV-1 {ECO:0000313|Proteomes:UP000095347};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FMN; Xref=ChEBI:CHEBI:58210;
CC         Evidence={ECO:0000256|ARBA:ARBA00001917};
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:OEJ66209.1}.
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DR   EMBL; MCGG01000036; OEJ66209.1; -; Genomic_DNA.
DR   RefSeq; WP_069958414.1; NZ_MCGG01000036.1.
DR   AlphaFoldDB; A0A1E5Q6C6; -.
DR   STRING; 28181.BEN30_12505; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000095347; 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; IPR028261; DPD_II.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   PANTHER; PTHR43073; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR   PANTHER; PTHR43073:SF2; DIHYDROPYRIMIDINE DEHYDROGENASE [NADP(+)]; 1.
DR   Pfam; PF00037; Fer4; 1.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00368; FADPNR.
DR   PRINTS; PR00469; PNDRDTASEII.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 2.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000095347}.
FT   DOMAIN          486..516
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
FT   DOMAIN          517..546
FT                   /note="4Fe-4S ferredoxin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51379"
SQ   SEQUENCE   548 AA;  59923 MW;  D2FDA80799ABBD8F CRC64;
     MSNTDPKLPY AITLDPGTSL ANHTGSWRTF MPVYRDALPP CNNACPAGEN IQGWLYHAEE
     GNYQAAWNVL VQDNPMPAIM GRVCYHPCES ACNRKDLDEA VAVHAVERFL GDEALKQGWM
     PEATHADTGK RVLVVGAGPS GLSAAYHLRR LGHAVTIREA GPMAGGMMRF GIPKYRLPRD
     ILDGEIARIV NFGVTLELNQ KVEDIPAAFE SEGFDAVFIA VGAHLAKRID IPAHAAGRIL
     DAASVLHDME TSPEPLQLGR RVIVYGGGNT AMDVARTAKR LGAEEAMIVY RRSRTEMPAH
     DFEATEAEQE GVLIHWLRTI KHIDETTFTV EKMEIDANGR PQATGEFETL EADTLIMALG
     QDVDTSFLQS VPGVKIARDG VVDVDEHMMT GYTGLFAGGD MVPSERTVTV AVGHGKKAAH
     HIDAWLKGQT YVKPAKHPLA AFDKLNTWYY DDAPQLVQPQ LDIIRRQTSF DEVIGDLDES
     TALFEARRCL SCGNCFECDN CYGVCPDNAV KKLGPGKRFE FLYDFCKGCG LCAAECPCGA
     IDMIPEAS
//