ID   A0A2D8PAR7_9RHOB        Unreviewed;       533 AA.
AC   A0A2D8PAR7;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=FMN-binding glutamate synthase family protein {ECO:0000313|EMBL:MAM62555.1};
GN   ORFNames=CMH11_13820 {ECO:0000313|EMBL:MAM62555.1};
OS   Maritimibacter sp.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Maritimibacter.
OX   NCBI_TaxID=2003363 {ECO:0000313|EMBL:MAM62555.1, ECO:0000313|Proteomes:UP000224593};
RN   [1] {ECO:0000313|Proteomes:UP000224593}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Tully B.J., Graham E.D., Heidelberg J.F.;
RT   "The Reconstruction of 2,631 Draft Metagenome-Assembled Genomes from the
RT   Global Oceans.";
RL   Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the glutamate synthase family.
CC       {ECO:0000256|ARBA:ARBA00009716, ECO:0000256|PIRNR:PIRNR006429}.
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:MAM62555.1}.
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DR   EMBL; NZNT01000025; MAM62555.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2D8PAR7; -.
DR   Proteomes; UP000224593; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0015930; F:glutamate synthase activity; IEA:InterPro.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IEA:InterPro.
DR   CDD; cd02808; GltS_FMN; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR024188; GltB.
DR   InterPro; IPR002932; Glu_synthdom.
DR   InterPro; IPR027283; YerD.
DR   PANTHER; PTHR43819:SF1; ARCHAEAL GLUTAMATE SYNTHASE [NADPH]; 1.
DR   PANTHER; PTHR43819; ARCHAEAL-TYPE GLUTAMATE SYNTHASE [NADPH]; 1.
DR   Pfam; PF01645; Glu_synthase; 1.
DR   PIRSF; PIRSF006429; GOGAT_lg_2; 1.
DR   PIRSF; PIRSF500060; UCP500060; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          146..471
FT                   /note="Glutamate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01645"
SQ   SEQUENCE   533 AA;  58013 MW;  482DC5982F7E5323 CRC64;
     MHNIRYLPFI VFVLAVPVGI ALAFTAPFWG GVVAALGLVG SVIGTYDLLQ RKRAVLKNYP
     VLARARFFLE SIRPEIRQYF LESDHEEVPF SREQRALVYR RSKGLEGLRP FGSLRDQHGV
     GHEWINHSLQ ARHLADHDFR VTFGAETCEK PYSASVLNIS GMSFGALSPN AVEALNIGAK
     RGNFCQTTGE GSISRFHTKH GGDLVWQIGS GYFGCRDKQG RFSPDIFAER ATLEQVKMVE
     IKLSQGAKPG HGGILPGAKV TPDIAEARGV PPGVDCLSPP SHSAFSTPTE MVRFIAKLRG
     LSGGKPVGIK MCVGHPWEVF AIAKAMVETG DHPDFITIDG SEGGTGAAPA EFADHIGAPL
     REGLMLVHNV LVGLGLRDKI RLVCSAKLIS AFDMARVFAL GADTCNMGRG YMFSLGCIQA
     QTCHTGRCPT GVTSQDPGRY KALDVQDKAE RVHQFHENTL KALAETIGAT GLSHPRDLKP
     DHLMIRINAR EVRSARSQYD WVGPGELLDH NVAHPAFAKF WDMARADSFA AAV
//