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Database: UniProt
Entry: F3PJX5_9BACE
LinkDB: F3PJX5_9BACE
Original site: F3PJX5_9BACE 
ID   F3PJX5_9BACE            Unreviewed;       768 AA.
AC   F3PJX5;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 49.
DE   SubName: Full=Glutamate synthase {ECO:0000313|EMBL:EGF50860.1};
GN   ORFNames=HMPREF9445_02454 {ECO:0000313|EMBL:EGF50860.1};
OS   Bacteroides clarus YIT 12056.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=762984 {ECO:0000313|EMBL:EGF50860.1, ECO:0000313|Proteomes:UP000010321};
RN   [1] {ECO:0000313|EMBL:EGF50860.1, ECO:0000313|Proteomes:UP000010321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIT 12056 {ECO:0000313|EMBL:EGF50860.1,
RC   ECO:0000313|Proteomes:UP000010321};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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:EGF50860.1}.
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DR   EMBL; AFBM01000028; EGF50860.1; -; Genomic_DNA.
DR   RefSeq; WP_009122540.1; NZ_GL882598.1.
DR   AlphaFoldDB; F3PJX5; -.
DR   STRING; 762984.SAMN05444376_0650; -.
DR   eggNOG; COG0493; Bacteria.
DR   eggNOG; COG0543; Bacteria.
DR   HOGENOM; CLU_011095_1_1_10; -.
DR   OrthoDB; 9803192at2; -.
DR   Proteomes; UP000010321; Unassembled WGS sequence.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd06219; DHOD_e_trans_like1; 1.
DR   Gene3D; 1.10.1060.10; Alpha-helical ferredoxin; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR019480; Dihydroorotate_DH_Fe-S-bd.
DR   InterPro; IPR028261; DPD_II.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR023753; FAD/NAD-binding_dom.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR009051; Helical_ferredxn.
DR   InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   InterPro; IPR006004; SudA-like.
DR   NCBIfam; TIGR01316; gltA; 1.
DR   PANTHER; PTHR42783; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   PANTHER; PTHR42783:SF3; GLUTAMATE SYNTHASE [NADPH] SMALL CHAIN; 1.
DR   Pfam; PF10418; DHODB_Fe-S_bind; 1.
DR   Pfam; PF14691; Fer4_20; 1.
DR   Pfam; PF00175; NAD_binding_1; 1.
DR   Pfam; PF07992; Pyr_redox_2; 1.
DR   PRINTS; PR00419; ADXRDTASE.
DR   SUPFAM; SSF46548; alpha-helical ferredoxin; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
FT   DOMAIN          1..95
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          271..293
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   768 AA;  83565 MW;  B9C186B00A6DDC67 CRC64;
     MNKIISKEHF SEKVFKLVIE APLIAKSRKA GHFVIVRVGE KGERMPLTIA SADPVKGTIT
     LVVQEVGLSS TRLCELNEGD YITDVVGPLG QATHIENFGT VVCAGGGVGV APMLPIVQAL
     KAAGNRVITV LAGRTKELII LEKEMRESSD EVIIMTDDGS YGNKGLVTEG VESVINREKV
     DKCFCIGPAI MMKFVCLLTK KYEIPTDVSL NTIMVDGTGM CGACRITIGG KTKFVCVDGP
     EFDGHQVDFD EMLKRMGAFK NIEREEMHKL EEPQTCQATG ENTPEEDEKS RNAAWRQELR
     KSMKAKERTA IPRVEMNELD AEYRSHSRKE EVNRGLTEKQ ALTEAKRCLD CANPGCTEGC
     PVGIDIPRFI KNIERGEFLE AAKTLKETSA LPAVCGRVCP QEKQCESKCI HLKMNEKPVA
     IGYLERFAAD YERESGQISV PEIKEKNGIK IAVIGSGPAG LSFAGDMAKY GYDVTVFEAL
     HEIGGVLKYG IPEFRLPNKV VDVEIENLAQ MGVKFIKDCI IGKTLSVEQL EEEDFKGIFV
     ASGAGLPNFM NIPGENSINI LSSNEYLTRV NLMDAASEDS DTPVPFGKCV AVIGGGNTAM
     DSVRTARRLG AERAMIIYRR SEEEMPARIE EVKHAKEEGV EFLTLHNPIE YIADEQGKVK
     QVVLQKMELG EPDASGRRSP VPIPGATETI DIDLAIVSVG VSPNPIVPSS IKGLELGRKG
     TIAVNDSMQS SIPTIYAGGD IVRGGATVIL AMGDGRKAAA AMNEQLKH
//
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