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Database: UniProt
Entry: A0A2B2CDU5_9BACI
LinkDB: A0A2B2CDU5_9BACI
Original site: A0A2B2CDU5_9BACI 
ID   A0A2B2CDU5_9BACI        Unreviewed;       521 AA.
AC   A0A2B2CDU5;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 13.
DE   SubName: Full=FMN-binding glutamate synthase family protein {ECO:0000313|EMBL:PFP30499.1};
GN   ORFNames=COJ96_04600 {ECO:0000313|EMBL:PFP30499.1};
OS   Bacillus sp. AFS073361.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2033511 {ECO:0000313|EMBL:PFP30499.1, ECO:0000313|Proteomes:UP000223997};
RN   [1] {ECO:0000313|EMBL:PFP30499.1, ECO:0000313|Proteomes:UP000223997}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AFS073361 {ECO:0000313|EMBL:PFP30499.1,
RC   ECO:0000313|Proteomes:UP000223997};
RG   Agbiome Team Llc;
RA   Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA   Shank E.A., Bowers A.;
RT   "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT   roles of natural products in bacterial physiology.";
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:PFP30499.1}.
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DR   EMBL; NUZU01000007; PFP30499.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2B2CDU5; -.
DR   OrthoDB; 9758182at2; -.
DR   Proteomes; UP000223997; 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   PANTHER; PTHR43819; ARCHAEAL-TYPE GLUTAMATE SYNTHASE [NADPH]; 1.
DR   PANTHER; PTHR43819:SF1; ARCHAEAL-TYPE GLUTAMATE SYNTHASE [NADPH]; 1.
DR   Pfam; PF01645; Glu_synthase; 1.
DR   PIRSF; PIRSF006429; GOGAT_lg_2; 1.
DR   SUPFAM; SSF51395; FMN-linked oxidoreductases; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000223997};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          117..489
FT                   /note="Glutamate synthase"
FT                   /evidence="ECO:0000259|Pfam:PF01645"
SQ   SEQUENCE   521 AA;  57962 MW;  055F9BD166CE02F9 CRC64;
     MVWTIFIFLL IVFIIGPIAL LIWLHILAKK PQHSIIRAHP YLGWMRYLLE KIGPEFRQYW
     FDDDNSGKPF SRTDFLGIVF SAKYRSDLLS FGSKRDFDNP GYYIANGLFP LLNEELRVDN
     QEKVHSMKYK IDHEGLFTRH EQLEKDQTTR WLYHEEETII VGGDRKFPWR LSGPFGVSAT
     SYGAVGENYI LSTGRGSYLA GGSWINTGEG GVAPEHLESG VDVVAQIGPG IFGFRDDEGN
     FSLDEFKCKA KEPNIKAFEL KFGQGAKIRG GHLEGSKVST KVATIRKVPV GKTINSPNRF
     PFLHNALETL EFIKMLQEEG GKPIGIKIVV GHPSSLNELF ESMNHLKIYP DFITVDGGEG
     GTGATYKSMA DTMGLPLYPA LIAVVDKAHQ FGVRKKLKIF ASGKLISADK IAIALAIGAD
     AVNSARGFMI ANGCIMALQC HTGKCPTGVT TTDPKYQEAL VPEEKKWRVM NYIINVRQGL
     FALAAACGID SPCKFTREHI VFKDVDGRIK KLSELFPMID S
//
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